Collagen: A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).Collagen Type I: The most common form of fibrillar collagen. It is a major constituent of bone (BONE AND BONES) and SKIN and consists of a heterotrimer of two alpha1(I) and one alpha2(I) chains.Fibrillar Collagens: A family of structurally related collagens that form the characteristic collagen fibril bundles seen in CONNECTIVE TISSUE.Collagen Type IV: A non-fibrillar collagen found in the structure of BASEMENT MEMBRANE. Collagen type IV molecules assemble to form a sheet-like network which is involved in maintaining the structural integrity of basement membranes. The predominant form of the protein is comprised of two alpha1(IV) subunits and one alpha2(IV) subunit, however, at least six different alpha subunits can be incorporated into the heterotrimer.Collagen Type III: A fibrillar collagen consisting of three identical alpha1(III) chains that is widely distributed in many tissues containing COLLAGEN TYPE I. It is particularly abundant in BLOOD VESSELS and may play a role in tissues with elastic characteristics.Receptors, Collagen: Collagen receptors are cell surface receptors that modulate signal transduction between cells and the EXTRACELLULAR MATRIX. They are found in many cell types and are involved in the maintenance and regulation of cell shape and behavior, including PLATELET ACTIVATION and aggregation, through many different signaling pathways and differences in their affinities for collagen isoforms. Collagen receptors include discoidin domain receptors, INTEGRINS, and glycoprotein VI.Collagen Type II: A fibrillar collagen found predominantly in CARTILAGE and vitreous humor. It consists of three identical alpha1(II) chains.Collagen Type VI: A non-fibrillar collagen that forms a network of MICROFIBRILS within the EXTRACELLULAR MATRIX of CONNECTIVE TISSUE. The alpha subunits of collagen type VI assemble into antiparallel, overlapping dimers which then align to form tetramers.Collagen Type V: A fibrillar collagen found widely distributed as a minor component in tissues that contain COLLAGEN TYPE I and COLLAGEN TYPE III. It is a heterotrimeric molecule composed of alpha1(V), alpha2(V) and alpha3(V) subunits. Several forms of collagen type V exist depending upon the composition of the subunits that form the trimer.Collagen Diseases: Historically, a heterogeneous group of acute and chronic diseases, including rheumatoid arthritis, systemic lupus erythematosus, progressive systemic sclerosis, dermatomyositis, etc. This classification was based on the notion that "collagen" was equivalent to "connective tissue", but with the present recognition of the different types of collagen and the aggregates derived from them as distinct entities, the term "collagen diseases" now pertains exclusively to those inherited conditions in which the primary defect is at the gene level and affects collagen biosynthesis, post-translational modification, or extracellular processing directly. (From Cecil Textbook of Medicine, 19th ed, p1494)Extracellular Matrix: A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.Procollagen: A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.Collagen Type XVIII: A non-fibrillar collagen found in BASEMENT MEMBRANE. The C-terminal end of the alpha1 chain of collagen type XVIII contains the ENDOSTATIN peptide, which can be released by proteolytic cleavage.Hydroxyproline: A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.Collagen Type XI: A fibrillar collagen found primarily in interstitial CARTILAGE. Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits.Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Hydroxylysine: A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens.Cartilage: A non-vascular form of connective tissue composed of CHONDROCYTES embedded in a matrix that includes CHONDROITIN SULFATE and various types of FIBRILLAR COLLAGEN. There are three major types: HYALINE CARTILAGE; FIBROCARTILAGE; and ELASTIC CARTILAGE.Gels: Colloids with a solid continuous phase and liquid as the dispersed phase; gels may be unstable when, due to temperature or other cause, the solid phase liquefies; the resulting colloid is called a sol.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Fibril-Associated Collagens: A family of non-fibrillar collagens that interact with FIBRILLAR COLLAGENS. They contain short triple helical domains interrupted by short non-helical domains and do not form into collagen fibrils.Basement Membrane: A darkly stained mat-like EXTRACELLULAR MATRIX (ECM) that separates cell layers, such as EPITHELIUM from ENDOTHELIUM or a layer of CONNECTIVE TISSUE. The ECM layer that supports an overlying EPITHELIUM or ENDOTHELIUM is called basal lamina. Basement membrane (BM) can be formed by the fusion of either two adjacent basal laminae or a basal lamina with an adjacent reticular lamina of connective tissue. BM, composed mainly of TYPE IV COLLAGEN; glycoprotein LAMININ; and PROTEOGLYCAN, provides barriers as well as channels between interacting cell layers.Collagen Type X: A non-fibrillar collagen found primarily in terminally differentiated hypertrophic CHONDROCYTES. It is a homotrimer of three identical alpha1(X) subunits.Extracellular Matrix Proteins: Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ).Skin: The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.Tendons: Fibrous bands or cords of CONNECTIVE TISSUE at the ends of SKELETAL MUSCLE FIBERS that serve to attach the MUSCLES to bones and other structures.Collagen Type XII: A fibril-associated collagen found in many tissues bearing high tensile stress, such as TENDONS and LIGAMENTS. It is comprised of a trimer of three identical alpha1(XII) chains.Microbial Collagenase: A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically cross-reactive but possess different sequences and different specificities. Other variants have been isolated from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio and Streptomyces. EC 3.4.24.3.Collagen Type VII: A non-fibrillar collagen involved in anchoring the epidermal BASEMENT MEMBRANE to underlying tissue. It is a homotrimer comprised of C-terminal and N-terminal globular domains connected by a central triple-helical region.Fibronectins: Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.Pepsin A: Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.Connective Tissue: Tissue that supports and binds other tissues. It consists of CONNECTIVE TISSUE CELLS embedded in a large amount of EXTRACELLULAR MATRIX.Proteoglycans: Glycoproteins which have a very high polysaccharide content.Collagenases: Enzymes that catalyze the degradation of collagen by acting on the peptide bonds.Fibrosis: Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.Cartilage, Articular: A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact.Non-Fibrillar Collagens: A family of structurally-related short-chain collagens that do not form large fibril bundles.Collagen Type VIII: A non-fibrillar collagen originally found in DESCEMET MEMBRANE. It is expressed in endothelial cell layers and in tissues undergoing active remodeling. It is heterotrimer comprised of alpha1(VIII) and alpha2(VIII) chains.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Laminin: Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.ElastinOsteogenesis Imperfecta: COLLAGEN DISEASES characterized by brittle, osteoporotic, and easily fractured bones. It may also present with blue sclerae, loose joints, and imperfect dentin formation. Most types are autosomal dominant and are associated with mutations in COLLAGEN TYPE I.Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase: A mixed-function oxygenase that catalyzes the hydroxylation of peptidyllysine, usually in protocollagen, to peptidylhydroxylysine. The enzyme utilizes molecular oxygen with concomitant oxidative decarboxylation of the cosubstrate 2-oxoglutarate to succinate. EC 1.14.11.4.Proline: A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.Aminopropionitrile: Reagent used as an intermediate in the manufacture of beta-alanine and pantothenic acid.Decorin: A small leucine-rich proteoglycan that interacts with FIBRILLAR COLLAGENS and modifies the EXTRACELLULAR MATRIX structure of CONNECTIVE TISSUE. Decorin has also been shown to play additional roles in the regulation of cellular responses to GROWTH FACTORS. The protein contains a single glycosaminoglycan chain and is similar in structure to BIGLYCAN.Cell Adhesion: Adherence of cells to surfaces or to other cells.Transforming Growth Factor beta: A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.Collagen Type XIII: A non-fibrillar collagen found as a ubiquitously expressed membrane- associated protein. Type XIII collagen contains both collagenous and non-collagenous domains along with a transmembrane domain within its N-terminal region.Integrin alpha1beta1: Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Chondrocytes: Polymorphic cells that form cartilage.Wound Healing: Restoration of integrity to traumatized tissue.Chick Embryo: The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.Microscopy, Polarization: Microscopy using polarized light in which phenomena due to the preferential orientation of optical properties with respect to the vibration plane of the polarized light are made visible and correlated parameters are made measurable.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Bone and Bones: A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.Microscopy, Electron, Scanning: Microscopy in which the object is examined directly by an electron beam scanning the specimen point-by-point. The image is constructed by detecting the products of specimen interactions that are projected above the plane of the sample, such as backscattered electrons. Although SCANNING TRANSMISSION ELECTRON MICROSCOPY also scans the specimen point by point with the electron beam, the image is constructed by detecting the electrons, or their interaction products that are transmitted through the sample plane, so that is a form of TRANSMISSION ELECTRON MICROSCOPY.Matrix Metalloproteinase 1: A member of the metalloproteinase family of enzymes that is principally responsible for cleaving FIBRILLAR COLLAGEN. It can degrade interstitial collagens, types I, II and III.Integrins: A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Cornea: The transparent anterior portion of the fibrous coat of the eye consisting of five layers: stratified squamous CORNEAL EPITHELIUM; BOWMAN MEMBRANE; CORNEAL STROMA; DESCEMET MEMBRANE; and mesenchymal CORNEAL ENDOTHELIUM. It serves as the first refracting medium of the eye. It is structurally continuous with the SCLERA, avascular, receiving its nourishment by permeation through spaces between the lamellae, and is innervated by the ophthalmic division of the TRIGEMINAL NERVE via the ciliary nerves and those of the surrounding conjunctiva which together form plexuses. (Cline et al., Dictionary of Visual Science, 4th ed)Gelatin: A product formed from skin, white connective tissue, or bone COLLAGEN. It is used as a protein food adjuvant, plasma substitute, hemostatic, suspending agent in pharmaceutical preparations, and in the manufacturing of capsules and suppositories.Transforming Growth Factor beta1: A subtype of transforming growth factor beta that is synthesized by a wide variety of cells. It is synthesized as a precursor molecule that is cleaved to form mature TGF-beta 1 and TGF-beta1 latency-associated peptide. The association of the cleavage products results in the formation a latent protein which must be activated to bind its receptor. Defects in the gene that encodes TGF-beta1 are the cause of CAMURATI-ENGELMANN SYNDROME.HSP47 Heat-Shock Proteins: Basic glycoprotein members of the SERPIN SUPERFAMILY that function as COLLAGEN-specific MOLECULAR CHAPERONES in the ENDOPLASMIC RETICULUM.Procollagen-Proline Dioxygenase: A mixed-function oxygenase that catalyzes the hydroxylation of a prolyl-glycyl containing peptide, usually in PROTOCOLLAGEN, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilizes molecular OXYGEN with a concomitant oxidative decarboxylation of 2-oxoglutarate to SUCCINATE. The enzyme occurs as a tetramer of two alpha and two beta subunits. The beta subunit of procollagen-proline dioxygenase is identical to the enzyme PROTEIN DISULFIDE-ISOMERASES.Tensile Strength: The maximum stress a material subjected to a stretching load can withstand without tearing. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed, p2001)Glycosaminoglycans: Heteropolysaccharides which contain an N-acetylated hexosamine in a characteristic repeating disaccharide unit. The repeating structure of each disaccharide involves alternate 1,4- and 1,3-linkages consisting of either N-acetylglucosamine or N-acetylgalactosamine.Protein-Lysine 6-Oxidase: An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide. EC 1.4.3.13.Tissue Engineering: Generating tissue in vitro for clinical applications, such as replacing wounded tissues or impaired organs. The use of TISSUE SCAFFOLDING enables the generation of complex multi-layered tissues and tissue structures.Corneal Stroma: The lamellated connective tissue constituting the thickest layer of the cornea between the Bowman and Descemet membranes.Integrin alpha2: An integrin alpha subunit that primarily combines with INTEGRIN BETA1 to form the INTEGRIN ALPHA2BETA1 heterodimer. It contains a domain which has homology to collagen-binding domains found in von Willebrand factor.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Platelet Adhesiveness: The process whereby PLATELETS adhere to something other than platelets, e.g., COLLAGEN; BASEMENT MEMBRANE; MICROFIBRILS; or other "foreign" surfaces.Dermis: A layer of vascularized connective tissue underneath the EPIDERMIS. The surface of the dermis contains innervated papillae. Embedded in or beneath the dermis are SWEAT GLANDS; HAIR FOLLICLES; and SEBACEOUS GLANDS.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Blood Platelets: Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.Cyanogen Bromide: Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.Stress, Mechanical: A purely physical condition which exists within any material because of strain or deformation by external forces or by non-uniform thermal expansion; expressed quantitatively in units of force per unit area.Platelet Aggregation: The attachment of PLATELETS to one another. This clumping together can be induced by a number of agents (e.g., THROMBIN; COLLAGEN) and is part of the mechanism leading to the formation of a THROMBUS.Tissue Scaffolds: Cell growth support structures composed of BIOCOMPATIBLE MATERIALS. They are specially designed solid support matrices for cell attachment in TISSUE ENGINEERING and GUIDED TISSUE REGENERATION uses.Matrix Metalloproteinases: A family of zinc-dependent metalloendopeptidases that is involved in the degradation of EXTRACELLULAR MATRIX components.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Matrix Metalloproteinase 2: A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain.Disease Models, Animal: Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.Cell Movement: The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Fluorescent Antibody Technique: Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Integrin alpha1: An integrin alpha subunit that binds COLLAGEN and LAMININ though its I domain. It combines with INTEGRIN BETA1 to form the heterodimer INTEGRIN ALPHA1BETA1.Descemet Membrane: A layer of the cornea. It is the basal lamina of the CORNEAL ENDOTHELIUM (from which it is secreted) separating it from the CORNEAL STROMA. It is a homogeneous structure composed of fine collagenous filaments, and slowly increases in thickness with age.Pulmonary Fibrosis: A process in which normal lung tissues are progressively replaced by FIBROBLASTS and COLLAGEN causing an irreversible loss of the ability to transfer oxygen into the bloodstream via PULMONARY ALVEOLI. Patients show progressive DYSPNEA finally resulting in death.Keloid: A sharply elevated, irregularly shaped, progressively enlarging scar resulting from formation of excessive amounts of collagen in the dermis during connective tissue repair. It is differentiated from a hypertrophic scar (CICATRIX, HYPERTROPHIC) in that the former does not spread to surrounding tissues.Receptors, Mitogen: Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Growth Plate: The area between the EPIPHYSIS and the DIAPHYSIS within which bone growth occurs.Cell Culture Techniques: Methods for maintaining or growing CELLS in vitro.Calcification, Physiologic: Process by which organic tissue becomes hardened by the physiologic deposit of calcium salts.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Aggrecans: Large HYALURONAN-containing proteoglycans found in articular cartilage (CARTILAGE, ARTICULAR). They form into aggregates that provide tissues with the capacity to resist high compressive and tensile forces.Biomechanical Phenomena: The properties, processes, and behavior of biological systems under the action of mechanical forces.Tissue Inhibitor of Metalloproteinase-1: A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a N-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumor invasion in vitro.Elastic Tissue: Connective tissue comprised chiefly of elastic fibers. Elastic fibers have two components: ELASTIN and MICROFIBRILS.Tropocollagen: The molecular unit of collagen fibrils that consist of repeating three-stranded polypeptide units arranged head to tail in parallel bundles. It is a right-handed triple helix composed of 2 polypeptide chains. It is rich in glycine, proline, hydroxyproline, and hydroxylysine.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Arthritis, Experimental: ARTHRITIS that is induced in experimental animals. Immunological methods and infectious agents can be used to develop experimental arthritis models. These methods include injections of stimulators of the immune response, such as an adjuvant (ADJUVANTS, IMMUNOLOGIC) or COLLAGEN.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Cross-Linking Reagents: Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.Mice, Inbred C57BLMicroscopy, Electron, Transmission: Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.Nephritis, Hereditary: A group of inherited conditions characterized initially by HEMATURIA and slowly progressing to RENAL INSUFFICIENCY. The most common form is the Alport syndrome (hereditary nephritis with HEARING LOSS) which is caused by mutations in genes for TYPE IV COLLAGEN and defective GLOMERULAR BASEMENT MEMBRANE.Biocompatible Materials: Synthetic or natural materials, other than DRUGS, that are used to replace or repair any body TISSUES or bodily function.Antigens, CD29: Integrin beta-1 chains which are expressed as heterodimers that are noncovalently associated with specific alpha-chains of the CD49 family (CD49a-f). CD29 is expressed on resting and activated leukocytes and is a marker for all of the very late activation antigens on cells. (from: Barclay et al., The Leukocyte Antigen FactsBook, 1993, p164)Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Reverse Transcriptase Polymerase Chain Reaction: A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.Matrix Metalloproteinase 8: A member of the MATRIX METALLOPROTEINASES that cleaves triple-helical COLLAGEN types I, II, and III.Platelet Membrane Glycoproteins: Surface glycoproteins on platelets which have a key role in hemostasis and thrombosis such as platelet adhesion and aggregation. Many of these are receptors.Gelatinases: A class of enzymes that catalyzes the degradation of gelatin by acting on the peptide bonds. EC 3.4.24.-.Cell Division: The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.Osteonectin: Non-collagenous, calcium-binding glycoprotein of developing bone. It links collagen to mineral in the bone matrix. In the synonym SPARC glycoprotein, the acronym stands for Secreted Protein, Acidic and Rich in Cysteine.Actins: Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.Protein Denaturation: Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.Rats, Sprague-Dawley: A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.Lung: Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.Kinetics: The rate dynamics in chemical or physical systems.Tissue Inhibitor of Metalloproteinases: A family of secreted protease inhibitory proteins that regulates the activity of SECRETED MATRIX METALLOENDOPEPTIDASES. They play an important role in modulating the proteolysis of EXTRACELLULAR MATRIX, most notably during tissue remodeling and inflammatory processes.Microfibrils: Components of the extracellular matrix consisting primarily of fibrillin. They are essential for the integrity of elastic fibers.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Skin Aging: The process of aging due to changes in the structure and elasticity of the skin over time. It may be a part of physiological aging or it may be due to the effects of ultraviolet radiation, usually through exposure to sunlight.Mice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.Platelet Activation: A series of progressive, overlapping events, triggered by exposure of the PLATELETS to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.Osteogenesis: The process of bone formation. Histogenesis of bone including ossification.Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Osteoarthritis: A progressive, degenerative joint disease, the most common form of arthritis, especially in older persons. The disease is thought to result not from the aging process but from biochemical changes and biomechanical stresses affecting articular cartilage. In the foreign literature it is often called osteoarthrosis deformans.ArthritisMyocardium: The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.Bone Matrix: Extracellular substance of bone tissue consisting of COLLAGEN fibers, ground substance, and inorganic crystalline minerals and salts.Sclera: The white, opaque, fibrous, outer tunic of the eyeball, covering it entirely excepting the segment covered anteriorly by the cornea. It is essentially avascular but contains apertures for vessels, lymphatics, and nerves. It receives the tendons of insertion of the extraocular muscles and at the corneoscleral junction contains the canal of Schlemm. (From Cline et al., Dictionary of Visual Science, 4th ed)Matrix Metalloproteinase 9: An endopeptidase that is structurally similar to MATRIX METALLOPROTEINASE 2. It degrades GELATIN types I and V; COLLAGEN TYPE IV; and COLLAGEN TYPE V.Ligaments: Shiny, flexible bands of fibrous tissue connecting together articular extremities of bones. They are pliant, tough, and inextensile.Cell Proliferation: All of the processes involved in increasing CELL NUMBER including CELL DIVISION.Biglycan: A small leucine-rich proteoglycan found in a variety of tissues including CAPILLARY ENDOTHELIUM; SKELETAL MUSCLE; CARTILAGE; BONE; and TENDONS. The protein contains two glycosaminoglycan chains and is similar in structure to DECORIN.Blotting, Northern: Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.Biological Markers: Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.Osteoblasts: Bone-forming cells which secrete an EXTRACELLULAR MATRIX. HYDROXYAPATITE crystals are then deposited into the matrix to form bone.Scleroderma, Systemic: A chronic multi-system disorder of CONNECTIVE TISSUE. It is characterized by SCLEROSIS in the SKIN, the LUNGS, the HEART, the GASTROINTESTINAL TRACT, the KIDNEYS, and the MUSCULOSKELETAL SYSTEM. Other important features include diseased small BLOOD VESSELS and AUTOANTIBODIES. The disorder is named for its most prominent feature (hard skin), and classified into subsets by the extent of skin thickening: LIMITED SCLERODERMA and DIFFUSE SCLERODERMA.Elasticity: Resistance and recovery from distortion of shape.Chondrogenesis: The formation of cartilage. This process is directed by CHONDROCYTES which continually divide and lay down matrix during development. It is sometimes a precursor to OSTEOGENESIS.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Connective Tissue Cells: A group of cells that includes FIBROBLASTS, cartilage cells, ADIPOCYTES, smooth muscle cells, and bone cells.Cicatrix: The fibrous tissue that replaces normal tissue during the process of WOUND HEALING.Endostatins: Angiostatic proteins that are formed from proteolytic cleavage of COLLAGEN TYPE XVIII.Hyaluronic Acid: A natural high-viscosity mucopolysaccharide with alternating beta (1-3) glucuronide and beta (1-4) glucosaminidic bonds. It is found in the UMBILICAL CORD, in VITREOUS BODY and in SYNOVIAL FLUID. A high urinary level is found in PROGERIA.Elastic Modulus: Numerical expression indicating the measure of stiffness in a material. It is defined by the ratio of stress in a unit area of substance to the resulting deformation (strain). This allows the behavior of a material under load (such as bone) to be calculated.Chondroitin Sulfate Proteoglycans: Proteoglycans consisting of proteins linked to one or more CHONDROITIN SULFATE-containing oligosaccharide chains.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).von Willebrand Factor: A high-molecular-weight plasma protein, produced by endothelial cells and megakaryocytes, that is part of the factor VIII/von Willebrand factor complex. The von Willebrand factor has receptors for collagen, platelets, and ristocetin activity as well as the immunologically distinct antigenic determinants. It functions in adhesion of platelets to collagen and hemostatic plug formation. The prolonged bleeding time in VON WILLEBRAND DISEASES is due to the deficiency of this factor.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Rats, Wistar: A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.Solubility: The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Achilles Tendon: A fibrous cord that connects the muscles in the back of the calf to the HEEL BONE.Epidermolysis Bullosa Dystrophica: Form of epidermolysis bullosa characterized by atrophy of blistered areas, severe scarring, and nail changes. It is most often present at birth or in early infancy and occurs in both autosomal dominant and recessive forms. All forms of dystrophic epidermolysis bullosa result from mutations in COLLAGEN TYPE VII, a major component fibrils of BASEMENT MEMBRANE and EPIDERMIS.Granulation Tissue: A vascular connective tissue formed on the surface of a healing wound, ulcer, or inflamed tissue. It consists of new capillaries and an infiltrate containing lymphoid cells, macrophages, and plasma cells.Alkaline Phosphatase: An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Molecular Weight: The sum of the weight of all the atoms in a molecule.Liver Cirrhosis, Experimental: Experimentally induced chronic injuries to the parenchymal cells in the liver to achieve a model for LIVER CIRRHOSIS.Mice, Inbred DBAMacromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Materials Testing: The testing of materials and devices, especially those used for PROSTHESES AND IMPLANTS; SUTURES; TISSUE ADHESIVES; etc., for hardness, strength, durability, safety, efficacy, and biocompatibility.Myofibroblasts: Spindle-shaped cells with characteristic CONTRACTILE PROTEINS and structures that contribute to the WOUND HEALING process. They occur in GRANULATION TISSUE and also in pathological processes such as FIBROSIS.Epithelium: One or more layers of EPITHELIAL CELLS, supported by the basal lamina, which covers the inner or outer surfaces of the body.Hepatic Stellate Cells: Perisinusoidal cells of the liver, located in the space of Disse between HEPATOCYTES and sinusoidal endothelial cells.Connective Tissue Growth Factor: A CCN protein family member that regulates a variety of extracellular functions including CELL ADHESION; CELL MIGRATION; and EXTRACELLULAR MATRIX synthesis. It is found in hypertrophic CHONDROCYTES where it may play a role in CHONDROGENESIS and endochondral ossification.Procollagen N-Endopeptidase: An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in the inherited connective tissue disorder--dermatosparaxis. EC 3.4.24.14.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Matrix Metalloproteinase 14: A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the action of PROPROTEIN CONVERTASES such as FURIN. Matrix metalloproteinase 14 plays a direct role in the cleavage of proteins in the pericellular environment. In addition, it can function indirectly by enzymatically activating the proprotein form of MATRIX METALLOPROTEINASE 15.Enzyme-Linked Immunosorbent Assay: An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.Dentin: The hard portion of the tooth surrounding the pulp, covered by enamel on the crown and cementum on the root, which is harder and denser than bone but softer than enamel, and is thus readily abraded when left unprotected. (From Jablonski, Dictionary of Dentistry, 1992)Microscopy, Confocal: A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.Aorta: The main trunk of the systemic arteries.Matrilin Proteins: PROTEOGLYCANS-associated proteins that are major components of EXTRACELLULAR MATRIX of various tissues including CARTILAGE; and INTERVERTEBRAL DISC structures. They bind COLLAGEN fibers and contain protein domains that enable oligomer formation and interaction with other extracellular matrix proteins such as CARTILAGE OLIGOMERIC MATRIX PROTEIN.In Situ Hybridization: A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.Aging: The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.Hydroxylation: Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Oligopeptides: Peptides composed of between two and twelve amino acids.Autoantigens: Endogenous tissue constituents that have the ability to interact with AUTOANTIBODIES and cause an immune response.Tissue Inhibitor of Metalloproteinase-2: A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a 21-kDa nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase A by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of TIMP-2 has been shown to inhibit invasive and metastatic activity of tumor cells and decrease tumor growth in vivo.

A hyperstable collagen mimic. (1/15802)

BACKGROUND: Collagen is the most abundant protein in animals. Each polypeptide chain of collagen is composed of repeats of the sequence: Gly-X-Y, where X and Y are often L-proline (Pro) and 4(R)-hydroxy-L-proline (Hyp) residues, respectively. These chains are wound into tight triple helices of great stability. The hydroxyl group of Hyp residues contributes much to this conformational stability. The existing paradigm is that this stability arises from interstrand hydrogen bonds mediated by bridging water molecules. This model was tested using chemical synthesis to replace Hyp residues with 4(R)-fluoro-L-proline (Flp) residues. The fluorine atom in Flp residues does not form hydrogen bonds but does elicit strong inductive effects. RESULTS: Replacing the Hyp residues in collagen with Flp residues greatly increases triple-helical stability. The free energy contributed by the fluorine atom in Flp residues is twice that of the hydroxyl group in Hyp residues. The stability of the Flp-containing triple helix far exceeds that of any untemplated collagen mimic of similar size. CONCLUSIONS: Bridging water molecules contribute little to collagen stability. Rather, collagen stability relies on previously unappreciated inductive effects. Collagen mimics containing fluorine or other appropriate electron-withdrawing substituents could be the basis of new biomaterials for restorative therapies.  (+info)

Expression of extracellular matrix proteins in cervical squamous cell carcinoma--a clinicopathological study. (2/15802)

AIM: To evaluate the intracellular and peritumoral expression of matrix proteins in squamous cell carcinoma of the uterine cervix using immunohistochemistry. METHODS: 71 squamous cell carcinomas and 10 controls were stained for laminin, fibronectin, and collagen IV. Cytoplasmic staining in tumour cells and peritumoral deposition of matrix proteins were evaluated. The association between staining results and patient age, tumour stage, histological grade, and survival was studied. RESULTS: Positive cytoplasmic staining for laminin, fibronectin, and collagen IV was observed in 17 (23.9%), 27 (38%), and 10 (14.1%) cases, respectively. Staining for laminin was most pronounced in the invasive front of tumour islands, while for fibronectin and collagen IV it appeared to be diffuse. Peritumoral staining for laminin and collagen IV was detected in 12 cases (16.9%). Early stage (Ia1-Ia2) tumours were uniformly negative for all three proteins. Cytoplasmic staining for laminin correlated with positive staining for fibronectin and collagen IV, and with the presence of a peritumoral deposition of collagen IV and laminin. There was no correlation with any of the three markers between staining results and patient age, stage, grade, or survival. CONCLUSIONS: Expression of extracellular matrix proteins in some cervical squamous cell carcinomas might reflect the enhanced ability of these tumours to modify the peritumoral stroma. This ability seems to be absent in early stage tumours. The correlation between intracytoplasmic and peritumoral expression of matrix proteins supports the evidence of their synthesis by tumour cells. However, this property did not correlate with disease outcome in this study.  (+info)

Prevention of collagen-induced arthritis by gene delivery of soluble p75 tumour necrosis factor receptor. (3/15802)

Collagen type II-induced arthritis (CIA) in DBA/1 mice can be passively transferred to SCID mice with spleen B- and T-lymphocytes. In the present study, we show that infection ex vivo of splenocytes from arthritic DBA/1 mice with a retroviral vector, containing cDNA for the soluble form of human p75 receptor of tumour necrosis factor (TNF-R) before transfer, prevents the development of arthritis, bone erosion and joint inflammation in the SCID recipients. Assessment of IgG subclass levels and studies of synovial histology suggest that down-regulating the effector functions of T helper-type 1 (Th1) cells may, at least in part, explain the inhibition of arthritis in the SCID recipients. In contrast, the transfer of splenocytes infected with mouse TNF-alpha gene construct resulted in exacerbated arthritis and enhancement of IgG2a antibody levels. Intriguingly, infection of splenocytes from arthritic DBA/1 mice with a construct for mouse IL-10 had no modulating effect on the transfer of arthritis. The data suggest that manipulation of the immune system with cytokines, or cytokine inhibitors using gene transfer protocols can be an effective approach to ameliorate arthritis.  (+info)

Expression and differential regulation of connective tissue growth factor in pancreatic cancer cells. (4/15802)

CTGF is an immediate early growth responsive gene that has been shown to be a downstream mediator of TGFbeta actions in fibroblasts and vascular endothelial cells. In the present study hCTGF was isolated as immediate early target gene of EGF/TGFalpha in human pancreatic cancer cells by suppression hybridization. CTGF transcripts were found in 13/15 pancreatic cancer cell lines incubated with 10% serum. In 3/7 pancreatic cancer cell lines EGF/TGFalpha induced a significant rise of CTGF transcript levels peaking 1-2 h after the start of treatment. TGFbeta increased CTGF transcript levels in 2/7 pancreatic cancer cell lines after 4 h of treatment and this elevation was sustained after 24 h. Only treatment with TGFbeta was accompanied by a parallel induction of collagen type I transcription. 15/19 human pancreatic cancer tissues were shown to overexpress high levels of CTGF transcripts. CTGF transcript levels in pancreatic cancer tissues and nude mouse xenograft tumors showed a good correlation to the degree of fibrosis. In situ hybridization and the nude mouse experiments revealed that in pancreatic cancer tissues, fibroblasts are the predominant site of CTGF transcription, whereas the tumor cells appear to contribute to a lesser extent. We conclude that CTGF may be of paramount importance for the development of the characteristic desmoplastic reaction in pancreatic cancer tissues.  (+info)

Enhanced Th1 and dampened Th2 responses synergize to inhibit acute granulomatous and fibrotic responses in murine schistosomiasis mansoni. (5/15802)

In murine schistosomiasis mansoni, CD4(+) Th1 and Th2 cells participate in the ovum-induced granulomatous inflammation. Previous studies showed that the interleukin-12 (IL-12)-induced Th1 response strongly suppressed the Th2-cell-mediated pulmonary granuloma development in naive or primed mice. However, liver granulomas were only moderately suppressed in egg-vaccinated, recombinant IL-12 (rIL-12)-treated infected mice. The present study shows that repeated rIL-12 injections given during early granuloma development at 5 to 7 weeks after infection prolonged the Th1 phase and resulted in gamma interferon-mediated suppression of liver granulomas. The timing is crucial: if given at 6 to 8 weeks, during the Th2-dominated phase of florid granuloma growth, the treatment is ineffective. Daily injections of rIL-12 given between 5 and 7.5 weeks during the period of granuloma growth achieved a somewhat-stronger diminution in granuloma growth with less deposition of collagen but caused 60% mortality and liver pathology. In contrast, combined treatment with rIL-12 and anti-IL-4-anti-IL-10 monoclonal antibody (MAb) injections given during the Th2 phase strongly inhibited liver granuloma growth without mortality. The diminished inflammatory response was accompanied by less deposition of collagen in the liver. Moreover, neutralization of endogenous IL-12 by anti-IL-12 MAbs effectively decreased the early Th1 phase (between 5 and 6 weeks after infection) but not the developing Th2 phase (5 to 7 weeks) of granuloma development. These studies indicate that the granulomatous response in infected mice can be manipulated by utilizing the Th1-Th2-subset antagonism with potential salutary results in the amelioration of fibrous pathology.  (+info)

Treponema denticola outer membrane enhances the phagocytosis of collagen-coated beads by gingival fibroblasts. (6/15802)

Human gingival fibroblasts (HGFs) degrade collagen fibrils in physiological processes by phagocytosis. Since Treponema denticola outer membrane (OM) extract perturbs actin filaments, important structures in phagocytosis, we determined whether the OM affects collagen phagocytosis in vitro by HGFs. Phagocytosis was measured by flow cytometric assessment of internalized collagen-coated fluorescent latex beads. Confluent HGFs pretreated with T. denticola ATCC 35405 OM exhibited an increase in the percentage of collagen phagocytic cells (phagocytosis index [PI]) and in the number of beads per phagocytosing cell (phagocytic capacity [PC]) compared with untreated controls. The enhancement was swift (within 15 min) and was still evident after 1 day. PI and PC of HGFs for bovine serum albumin (BSA)-coated beads were also increased, indicating a global increase in phagocytic processes. These results contrasted those for control OM from Veillonella atypica ATCC 17744, which decreased phagocytosis. The T. denticola OM-induced increase in bead uptake was eliminated by heating the OM and by depolymerization of actin filaments by cytochalasin D treatment of HGFs. Fluid-phase accumulation of lucifer yellow was enhanced in a saturable, concentration-dependent, transient manner by the T. denticola OM. Our findings were not due to HGF detachment or cytotoxicity in response to the T. denticola OM treatment since the HGFs exhibited minimal detachment from the substratum; they did not take up propidium iodide; and there was no change in their size, granularity, or content of sub-G1 DNA. We conclude that a heat-sensitive component(s) in T. denticola OM extract stimulates collagen phagocytosis and other endocytic processes such as nonspecific phagocytosis and pinocytosis by HGFs.  (+info)

Interferon-alpha does not improve outcome at one year in patients with diffuse cutaneous scleroderma: results of a randomized, double-blind, placebo-controlled trial. (7/15802)

OBJECTIVE: To determine whether interferon-alpha (IFNalpha) reduces the severity of skin involvement in early (<3 years) diffuse scleroderma. METHODS: In a randomized, placebo-controlled, double-blind trial, 35 patients with early scleroderma received subcutaneous injections of either IFNalpha (13.5 x 10(6) units per week in divided doses) or indistinguishable placebo. Outcomes assessed were the modified Rodnan skin score, as determined by a single observer at baseline, 6 months, and 12 months, as well as data on renal, cardiac, and lung function. Pre- and posttreatment skin biopsy samples were analyzed and blood was obtained for assessment of procollagen peptide levels. RESULTS: There were 11 withdrawals from the IFNalpha group and 3 from the placebo group due to either toxicity, lack of efficacy, or death. In the intent-to-treat analysis, there was a greater improvement in the skin score in the placebo group between 0 and 12 months (mean change IFNalpha -4.7 versus placebo -7.5; P = 0.36). There was also a greater deterioration in lung function in patients receiving active therapy, as assessed by either the forced vital capacity (mean change IFNalpha -8.2 versus placebo +1.3; P = 0.01) or the diffusing capacity for carbon monoxide (mean change IFNalpha -9.3 versus placebo +4.7; P = 0.002). Skin biopsy showed no significant decrease in collagen synthesis in the IFNalpha group, and no significant differences in the levels of procollagen peptides were seen between the 2 groups. CONCLUSION: This study suggests that IFNalpha is of no value in the treatment of scleroderma, and that it may in fact be deleterious.  (+info)

Association of the aggrecan keratan sulfate-rich region with collagen in bovine articular cartilage. (8/15802)

Aggrecan, the predominant large proteoglycan of cartilage, is a multidomain macromolecule with each domain contributing specific functional properties. One of the domains contains the majority of the keratan sulfate (KS) chain substituents and a protein segment with a proline-rich hexapeptide repeat sequence. The function of this domain is unknown but the primary structure suggests a potential for binding to collagen fibrils. We have examined binding of aggrecan fragments encompassing the KS-rich region in a solid-phase assay. A moderate affinity (apparent Kd = 1.1 microM) for isolated collagen II, as well as collagen I, was demonstrated. Enzymatic digestion of the KS chains did not alter the capacity of the peptide to bind to collagen, whereas cleavage of the protein core abolished the interaction. The distribution of the aggrecan KS-rich region in bovine tarsometatarsal joint cartilage was investigated using immunoelectron microscopy. Immunoreactivity was relatively low in the superficial zone and higher in the intermediate and deep zones of the uncalcified cartilage. Within the pericellular and territorial matrix compartments the epitopes representing the aggrecan KS-rich region were detected preferentially near or at collagen fibrils. Along the fibrils, epitope reactivity was non-randomly distributed, showing preference for the gap region within the D-period. Our data suggest that collagen fibrils interact with the KS-rich regions of several aggrecan monomers aligned within a proteoglycan aggregate. The fibril could therefore serve as a backbone in at least some of the aggrecan complexes.  (+info)

Zeus Capital has advised Healthcare Investment Opportunities (HIO), which has completed two acquisitions that set the strategic direction of the business. As part of the deal, HIO has changed its name to Collagen Solutions.. The company, advised by Zeus Capital, has bought San Jose, California-based Collagen Solutions and the Glasgow-based manufacturing business Collbio.. Collagen Solutions provides medical grade bovine collagen from closed herd and GBR1 countries and customised collagen based on customer requirements. Collagen Solutions also offers research and development services to develop and create devices from concept to clinical trial stage, as well as offering consultancy services for technology transfers to outside manufacturing facilities.. The acquisitions, which constituted a reverse takeover under the AIM Rules, provides an opportunity for a management team to provide effective and affordable treatment to patients across the globe.. ...
Sigma-Aldrich offers EMD Millipore-ECM105, Millicoat™ Human Collagen Type IV Coated Strips (96-Wells) for your research needs. Find product specific information including CAS, MSDS, protocols and references.
Zeus Capital has acted as nominated adviser and joint broker to Collagen Solutions on its NZ$12m acquisition and £6m placing.. Collagen Solutions is a developer and manufacturer of medical grade collagen components for use in regenerative medicine, medical devices and in-vitro diagnostics.. Zeus Capital has advised Collagen since its formation and its admission to AIM in April 2013. The company has been at the heart of its acquisitions of Collbio Limited, a manufacturer of medical grade collagen components, and the acquisition of assets from a US based provider of medical grade bovine collagen.. ...
Leukoregulin (LR), a T-cell-derived growth factor, modulates fibroblast functions in vitro [Mauviel, Rédini, Hartmann, Loyau & Pujol (1991) J. Cell Biol. 113, 1455-1462]. In the present study, incubation of human dermal fibroblasts with LR (0.1-2 units/ml) resulted in decreases in the mRNA steady-state levels for alpha 1(I), alpha 2(I) and alpha 1(III), but not alpha 2(V), collagen genes. LR also down-regulated alpha 2(I) collagen promoter activity in transient cell transfections of control cells as well as those incubated with transforming growth factor-beta, a potent up-regulator of collagen type I gene expression. Thus LR is a strong inhibitor of type I collagen gene expression, acting at the level of transcription. ...
BACKGROUND A powerful new platform technology for the production of human collagens is being developed in the Kadler Centre for Cell-Matrix Research within the Department of Life Sciences at the University of Manchester. The collagens most closely mimic human collagen structure, giving a far superior product to that produced by the harsh conditions necessary to extract animal collagens and can be tailored to incorporate binding sites for growth factors and cell attachment to promote integration and healing at wound sites. THE TECHNOLOGY The technology allows the process of procollagen assembly to be controlled, such that collagen fibrils with specified compositions can be generated. By directing the natural procollagen assembly process, the resulting collagen fibrils have significant advantages over existing products in terms of a near native molecular structure and ease of synthesis. These collagens can be formulated into bundles, sheets and lattices to mimic the various forms of human collagen. They
The sinusoidal hepatic stellate cells (HSC) are the major effectors during hepatic fibrogenesis and cirrhosis. During the early stages of hepatic injury associated with cirrhosis, the normally quiescent, vitamin A-storing HSC transform into actively proliferating, collagen-producing myofibroblast-like cells (34). Alcohol is one of the principal causes of cirrhosis. While the major clinical problem of alcohol-induced hepatic fibrogenesis has been the subject of numerous studies, the precise molecular mechanism(s) which leads to the increase in αI(I) collagen in HSC remains incompletely understood (2, 6, 24, 26, 35,36). It was demonstrated that acetaldehyde, but not ethanol, induced the increase in the αI(I) collagen gene expression (up to 2.5-fold) measured by Northern blots in cultured 3T3 fibroblasts (2). Further studies indicated that acetaldehyde increased the αI(I) collagen gene transcription in cultured HSC demonstrated by transcription run-on assays (4). These previous observations ...
TY - JOUR. T1 - P21-activated kinase 1. T2 - Convergence point in PDGF- and LPA-stimulated collagen matrix contraction by human broblasts. AU - Rhee, Sangmyung. AU - Grinnell, Frederick. PY - 2006/1/30. Y1 - 2006/1/30. N2 - Fibroblast three-dimensional collagen matrix culture provides a tissue-like model that can be used to analyze cell form and function. The physiological agonists platelet-derived growth factor (PDGF) and lysophosphatidic acid (LPA) both stimulate human broblasts to contract oating collagen matrices. In this study, we show that the PDGF and LPA signaling pathways required for matrix contraction converge on p21-activated kinase 1 (PAK1) and its downstream effector cofilin1 and that contraction depends on cellular ruffling activity, rather than on the protrusion and retraction of cellular dendritic extensions. We also show that, depending on the agonist, different Rho effectors cooperate with PAK1 to regulate matrix contraction, Rho kinase in the case of PDGF and mDia1 in the ...
In this work, we identify a C. elegans protein, TMEM-131, which has homologs in most animals, with essential roles in collagen secretion. These roles appear evolutionarily conserved for Drosophila and human TMEM131 homologs. We propose that TMEM131 proteins recruit premature collagen monomers through N-terminal PapD-L domains, whereas its C-terminal TRAPIDs bind to TRAPPC8, which promotes collagen secretion as a key component of TRAPP complex during the ER-to-Golgi transport of COPII vesicles (Fig. 7F). Although we did not recognize any apparent homologous C-propeptide protein sequence in C. elegans COL-19 or COL-101, their normal secretion still requires TMEM-131 as Drosophila, or human collagen I secretion requires TMEM131 homologs. Despite the lack of obvious sequence similarity between the C. elegans cuticle collagens and the COLFI domain of mammalian fibrillar collagens, TMEM131 family proteins appear to have evolved similar functions among different species. As COL-19::GFP secretion also ...
294131629 - EP 1000089 A1 2000-05-17 - COLLAGEN TYPE I AND TYPE III ADHESIVE COMPOSITIONS - [origin: WO9905180A1] Polymerized type I and/or III collagen based compositions for medical use as adhesives and sealants and preparation thereof are described. Prior to polymerization, the collagen monomers are prepared recombinantly whereby chemical modifications of the collagen are not needed to form such monomers. The type I and/or III collagen compositions are useful as medical adhesives for bonding soft tissues or in a sealant film for a variety of medical uses. In a further aspect of the present invention, the polymerized type I and/or III collagen composition includes agents which induce wound healing or provide for additional beneficial characteristics desired in a tissue adhesive and sealant.[origin: WO9905180A1] Polymerized type I and/or III collagen based compositions for medical use as adhesives and sealants and preparation thereof are described. Prior to polymerization, the collagen monomers are
Collagen peptides, a long-time staple of Paleo enthusiasts, have gone mainstream. From celebrity magazines to medical journals, the benefits of this supplement seem to be showing up everywhere. Better digestion, improved bone and joint health, and clearer skin are just a few of the claims collagen-peptide users swear by. If you havent heard of collagen peptides, or dont fully understand them, this overview can help get you started.. What are collagen peptides?. Collagen peptides are an easily digestible form of collagen. Available as a supplemental powder or capsule, collagen peptides contain short-chain amino acids that are derived from (usually) pasture-raised animal collagen. Theyre the gelatin that comes from collagen after it gets further broken down through a process called hydrolysis. This level of processing makes collagen-peptide supplements easy to consume and digest.. "Taking collagen as a supplement has many of the same benefits as drinking bone broth, but in a more isolated ...
Collagen alpha-1(V) chain is a protein that in humans is encoded by the COL5A1 gene. This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, types I and II. Type-V collagen GRCh38: Ensembl release 89: ENSG00000130635 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000026837 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Greenspan DS, Byers MG, Eddy RL, Cheng W, Jani-Sait S, Shows TB (May 1992). "Human collagen gene ...
The myocardium contains collagen matrix that is a major determinant of its architecture, structural integrity, and mechanical properties. This fibrillar matrix consists primarily of type I and type III collagens having epimysial, perimysial, and endomysial components. The present study shows the alteration of collagen phenotypes during the evolution of hypertensive hypertrophy. Therapy with captopril, an angiotensin-converting enzyme inhibitor that regresses cardiac hypertrophy, not only reduces the total amount of collagen but reverses the altered distribution of type I and type III collagen. In normotensive rats, captopril did not significantly reduce collagen content or alter the ratio of type I to type III collagen. ...
The myocardium contains collagen matrix that is a major determinant of its architecture, structural integrity, and mechanical properties. This fibrillar matrix consists primarily of type I and type III collagens having epimysial, perimysial, and endomysial components. The present study shows the alteration of collagen phenotypes during the evolution of hypertensive hypertrophy. Therapy with captopril, an angiotensin-converting enzyme inhibitor that regresses cardiac hypertrophy, not only reduces the total amount of collagen but reverses the altered distribution of type I and type III collagen. In normotensive rats, captopril did not significantly reduce collagen content or alter the ratio of type I to type III collagen. ...
TY - JOUR. T1 - Human bone collagen synthesis is a rapid, nutritionally modulated process. AU - Babraj, John A.. AU - Smith, Kenneth. AU - Cuthbertson, Daniel J.R.. AU - Rickhuss, Peter. AU - Dorling, James S.. AU - Rennie, Michael J.. PY - 2005/6. Y1 - 2005/6. N2 - We developed a direct assay of human bone collagen synthesis using [13C] or [15N] proline and applied it to determine the effects of feeding in young healthy men. Surprisingly, postabsorptive bone collagen synthesis is not sluggish, being ∼0.07%/h more rapid than that of muscle protein, and capable of being stimulated within 4 h of intravenous feeding by 66 ± 13%.Introduction: All current methods for estimation of bone collagen turnover are indirect, depending on the assay of collagen "markers." Our aim was to develop a direct method for human bone collagen synthesis to be used to study its physiology and pathology, and specifically, in the first instance, the effect of feeding.Materials and methods: We applied, over 2 h, flooding ...
The connective tissue components, collagen types I, III and IV, which surround the ovarian follicles, undergo drastic changes during ovulation. Abnormal collagen synthesis and increased volume and density of ovarian stroma characterise the polycystic ovary syndrome (PCOS). Physiologically, collagen synthesis in ovarian follicles is partly regulated by lysyl oxidase (LOX), which catalyzes the collagen and elastin cross-linking and plays indispensable role in the organization of ovarian extracellular matrix (ECM) during follicular development. We have recently shown accumulation of advanced glycation end products (AGEs), nutritional metabolic products that stimulate ECM production and abnormal collagen cross-linking, in ovarian tissue of patients with PCOS. However, the possible link between LOX and AGEs-induced signaling in collagen assembly and stroma formation remain elusive. The present investigation explores the hypothesis that AGE-mediated signaling affects LOX gene transcription in ovarian ...
Phages from a pentadecamer phage display library were selected for binding to vWF by affinity panning. Bound phages were selectively eluted with human collagen type I. After the third round of panning 95% of individual phage clones bound to vWF. The B8-phage inhibited the binding of collagen to vWF with an IC50 of 0.6 x 10(10) phages/ml, and of vWF to collagen with an IC50 of 1.0 x 10(10) phages/ml at 0.5 microg/ml vWF. Under flow conditions, 1.5 x 10(11) B8-phage/ml nearly completely inhibited platelet deposition on a human collagen type I coated surface at a shear rate of 1200 s(-1), while phages without an insert had no effect. The peptide corresponding to the one displayed on the B8-phage competed with the phage for binding to vWF with an IC50 of 30 microg/ml (16 microM). The peptide furthermore inhibited vWF-binding to collagen with a maximum of 40% at a concentration of 1.25 mg/ml (650 microM), higher concentrations of peptide could not improve this. We thus have selected phages that are potent
TY - JOUR. T1 - Dendritic fibroblasts in three-dimensional collagen matrices. AU - Grinnell, Frederick. AU - Ho, Chin Han. AU - Tamariz, Elisa. AU - Lee, David J.. AU - Skuta, Gabriella. PY - 2003/2/1. Y1 - 2003/2/1. N2 - Cell motility determines form and function of multicellular organisms. Most studies on fibroblast motility have been carried out using cells on the surfaces of culture dishes. In situ, however, the environment for fibroblasts is the three-dimensional extracellular matrix. In the current research, we studied the morphology and motility of human fibroblasts embedded in floating collagen matrices at a cell density below that required for global matrix remodeling (i.e., contraction). Under these conditions, cells were observed to project and retract a dendritic network of extensions. These extensions contained microtubule cores with actin concentrated at the tips resembling growth cones. Platelet-derived growth factor promoted formation of the network; lysophosphatidic acid ...
The folding, quality control, and secretion of collagen presents a significant challenge to collagen-producing cells. Each monomeric polypeptide must undergo extensive post-translational modifications, folding and assembly of the C-terminal propeptide globular domain, and isomerization of hundreds of prolyl bonds into the trans conformation before the mature triple helix can form. The triple-helical domain lacks a traditional hydrophobic core that often drives the assembly and folding of globular proteins. Even once folded, the triple helix is at best marginally stable at body temperature and is prone to local regions of unwinding. The process must be highly orchestrated by the endoplasmic reticulums chaperone network, including maintaining newly synthesized collagen polypeptides in an unfolded, non-aggregated, and unassembled form until after the extreme C-terminus adopts its folded structure. Despite decades of work, however, the mechanisms of collagen folding remain poorly understood, and ...
What is collagen? Collagen is a type of protein that is fibrous in nature, connecting and supporting other bodily tissues. Some people refer to collagen as the glue that holds the body together. Collagen works with keratin to provide skin with strength, flexibility and resistance. As we age, cell degradation occurs, leading to wrinkles. Think of collagen fibers as a chain-link fence. Now imagine those links rusting and falling apart; and as the links break, the fence falls. As our collagen production decreases this is what happens to skin fibers resulting in sagging, crepe-like skin. In addition, fibroblasts (collagen producing cells) decrease their production of new collagen as we age.. Once the importance of collagen in the skin is understood it is easier to understand why stimulating collagen production is the key to any good skin care and anti-aging regimen. Numerous studies explain why certain products and skin care treatments are effective at rejuvenating the skin. These treatments & ...
I want to introduce a collagen supplement. A collagen supplement is popular in the kind of the supplement. It is a very good ingredient, but, speaking of collagen, the collagen thinks that it is very difficult to take it in from food for the beauty of the woman. Are there not many people who take a collagen supplement easily because I can take in a collagen supplement easily? The collagen supplement is sold by the various makers. The supplement has many kinds, but may hesitate which collagen supplement I should choose because a collagen supplement is sold with a collagen supplement in one word by many makers.. What does the person intending to look for a collagen supplement from now on choose the collagen supplement on the basis of? The person who I watch a price if there is the person choosing the collagen supplement to see the contents, and chooses a collagen supplement thinks that I am. I think that there are various standards when I choose the collagen supplement, but may choose the collagen ...
100% SOLUBLE NATIVE MARINE COLLAGEN GEL - 30 ml and 100 ml. Native soluble collagen of type I +, pure to 99.7%, is the most abundant collagen in the human body: it accounts for 90% of collagen. The skin is composed of 75% collagen of type I. The native soluble collagen gel of type I liquefies at 34º C in order to penetrate in the pores of the skin and thus to provide a significant soluble native collagen inflow which has the following effects on the skin:. reduces wrinkles, ultra hydrating, improves skin tone, helps healing, supports the growth of the cells of the skin, procures a bright and radiant complexion, gives ultra smooth and soft skin. COLLAGEN Collagen is a fibrous glycoprotein that can be compared to a re-enforcement. Collagen is a particularly representative structural protein which fashion organisms by contributing to their structure. Collagen is the most abounding protein of the organism. That fibrous protein, collagen, is most abundant in humans: it represents about one quarter ...
100% SOLUBLE NATIVE MARINE COLLAGEN GEL - 30 ml and 100 ml. Native soluble collagen of type I +, pure to 99.7%, is the most abundant collagen in the human body: it accounts for 90% of collagen. The skin is composed of 75% collagen of type I. The native soluble collagen gel of type I liquefies at 34º C in order to penetrate in the pores of the skin and thus to provide a significant soluble native collagen inflow which has the following effects on the skin:. reduces wrinkles, ultra hydrating, improves skin tone, helps healing, supports the growth of the cells of the skin, procures a bright and radiant complexion, gives ultra smooth and soft skin. COLLAGEN Collagen is a fibrous glycoprotein that can be compared to a re-enforcement. Collagen is a particularly representative structural protein which fashion organisms by contributing to their structure. Collagen is the most abounding protein of the organism. That fibrous protein, collagen, is most abundant in humans: it represents about one quarter ...
Type I collagen is the most abundant protein in human body. The protein turns over slowly and its replacement synthesis is low. However, in wound healing or in pathological fibrosis the cells can increase production of type I collagen several hundred fold. This increase is predominantly due to posttranscriptional regulation, including increased half-life of collagen messenger RNAs (mRNAs) and their increased translatability. Type I collagen is composed of two α1 and one α2 polypeptides that fold into a triple helix. This stoichiometry is strictly regulated to prevent detrimental synthesis of α1 homotrimers. Collagen polypeptides are co-translationally modified and the rate of modifications is in dynamic equilibrium with the rate of folding, suggesting coordinated translation of collagen α1(I) and α2(I) polypeptides. Collagen α1(I) mRNA has in the 3 untranslated region (UTR) a C-rich sequence that binds protein αCP, this binding stabilizes the mRNA in collagen producing cells. In the 5 UTR both
This special Collagen Regeneration Formula (with Tissue Growth Factors) can help reverse sun damage and help stimulate new collagen production. Reduces the appearance of fine lines and wrinkles, improves skin tone, texture and firmness.
NeoCELL Super Collagen+C Powder 7ounces Radiant Skin Thicker Hair Stronger Nails Healthier Joints Anti-aging / Total Body Health / Pure & Natural / Ligaments and Tendons 6,600mg Collagen Type 1 & 3 COLLAGEN is a complex structural protein that maintains strength and flexibility throughout the body. SUPER COLLAGEN is made up of the collagen peptides Type 1&3 which support collagen in skin, hair, nails, muscles, tendons, ligaments and bones. Super Collagen is enzymatically hydrolyzed, providing an amino acid ratio with a low molecular weight for maximum bioavailability and utilization by the body. When Super Collagen is taken internally, the body receives the raw materials it needs to supplement the collagen found in all of these areas and may act as a messenger to trigger the synthesis of new collagen fibers. Super Collagen is neutral in taste and is specifically formulated in an easy to take powder form. It works synergistically with Vitamin C and is recommended to be mixed with
Collagens can be classified as being of animal or plant origin. Animal collagen is extracted from bovine and porcine bone or skin. Plant collagen is made by modifying polysaccharides (natto gum) through fermentation of yeast. Plant collagens used in cosmetics are heated and denatured simple proteins in the form of gelatins, which may exist at room temperature. They are biologically inactive. True active collagen must retain its molecular integrity at cold temperatures to be able to impact cell function. Refrigerated animal source collagen is the most viable therapeutic collagen with all of its properties intact. This makes it a superior product to plant collagen. PURIGENEX products always use safe porcine-animal source collagen, to ensure superior bioactivity.. What is the difference between atelocollagen and collagen? ...
Collagen Peptides Benefits:. - Promotes youthful skin, healthier hair, and stronger nails. - Improves skin smoothness. - Helps keep bones healthy and strong. - Supports joint health. - Contributes to a balanced diet and helps maintain weight. - Natural glycine promotes healthy immune, digestive, and central nervous systems. What are Collagen Peptides?. Collagen is the most abundant protein in the body and is a key constituent of all connective tissues. Collagen provides the infrastructure of the musculoskeletal system, essential for mobility. Peptides are short chain amino acids naturally derived from collagen protein. These natural peptides are highly bio-available, digestible and soluble in cold water. The intake of collagen ensures the cohesion, elasticity and regeneration of skin, hair, tendon, cartilage, bones, and joints.. Collagen is a natural and healthy ingredient that has been used for centuries. Collagen-rich foods are a large part of traditional diets. Our ancestors utilized ...
Collagen peptides are extremely readily available. They serve as work as foundation, restoring cells, such as skin, bones and joints. It has actually been recommended that collagen peptides might serve as carrier to the cells and activate the synthesis and reconstruction of brand-new collagen fibers, therefore sustaining our cells framework. Many clinical researches have actually shown collagen peptides health and wellness advantages. Key areas of advantage consist of healthy and balanced aging, joints and bones health and wellness,sporting activities nourishment and skin beauty. Collagen peptides are cool water-soluble and extremely bio readily available and bio active. This makes them a far better alternative for practical foods
A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of these collagen subunits. The sequence often follows the pattern Gly-Pro-X or Gly-X-Hyp, where X may be any of various other amino acid residues.[29] Proline or hydroxyproline constitute about 1/6 of the total sequence. With glycine accounting for the 1/3 of the sequence, this means approximately half of the collagen sequence is not glycine, proline or hydroxyproline, a fact often missed due to the distraction of the unusual GX1X2 character of collagen alpha-peptides. The high glycine content of collagen is important with respect to stabilization of the collagen helix as this allows the very close association of the collagen fibers within the molecule, facilitating hydrogen bonding and the formation of intermolecular cross-links.[29] This kind of regular repetition and high glycine content is found in only a few other fibrous proteins, such as silk fibroin.. Collagen is not only a structural ...
Collagen and fibronectin (FN) are two abundant and essential components of the vertebrate extracellular matrix; they interact directly with cellular receptors and affect cell adhesion and migration. Past studies identified a FN fragment comprising six modules, (6)FnI(1-2)FnII(7-9)FnI, and termed the gelatin binding domain (GBD) as responsible for collagen interaction. Recently, we showed that the GBD binds tightly to a specific site within type I collagen and determined the structure of domains (8-9)FnI in complex with a peptide from that site. Here, we present the crystallographic structure of domains (6)FnI(1-2)FnII(7)FnI, which form a compact, globular unit through interdomain interactions. Analysis of NMR titrations with single-stranded collagen peptides reveals a dominant collagen interaction surface on domains (2)FnII and (7)FnI; a similar surface appears involved in interactions with triple-helical peptides. Models of the complete GBD, based on the new structure and the (8-9)FnI·collagen complex
You want to reduce lines and wrinkles Is there a recovery period after Botox injections? After getting a Botox done will my face go back to the way it was after it wears off before I enjected botox? Rvtl Anti Aging Cream Equinox Instant Wrinkle Reducer Available powers phytoceramides buy australia can be impacted the menopausal group as early arthropod wrinkles under eyes newborn The Collagen Protein Structure Quaternary For Cream 30s message is based on large season abnormalities food-suitable as bullying canal frequency etc. Introduction Preparations of botulinum Collagen Protein Structure Quaternary For Cream 30s toxin (BoNT-A) have rapidly become established as a treatment option for Muscle Spasm and Relaxation. Collagen Protein Structure Quaternary For Cream 30s mostly used as an outer packaging in combination with our ultra clean medical grade LDPE bags this barrier packaging provides Collagen Protein Structure Quaternary For Cream 30s protection against: Gritty scrubs "They can be harsh ...
Our skin and many of our vital organs are composed primarily of collagen. As we age, this collagen becomes thinner and less robust. A degradation of our skins collagen is a prime reason why our skin becomes thinner, rougher, and more wrinkled as we age. But you dont have to settle for this!. Multiple studies are now showing that taking a collagen supplement can improve the health and appearance of your skin. YOUN Health Supplemental Collagen contains a unique blend of three patented collagen peptides that have been shown to not only improve the aging of your skin, but also improve bone and joint health.. YOUN Health Supplemental Collagen can be easily mixed into smoothies, shakes, coffee, and other foods and drinks. It has no taste but packs a big anti-aging punch. Dr. Youn enjoys mixing YOUN Health Supplemental Collagen into his coffee and smoothies.. Note: This product contains animal-based collagen. Do not consume if you are vegan.. Indications for Use: As a dietary supplement, mix one ...
Technologically advanced serum is a complete collagen solution, formulated to support skin s natural collagen building process, while assisting in stimulating new collagen formation. Collagen Complete utilizes clinically proven proprietary lab engineered non-animal, single strand soluble collagen, resulting in fuller, plumper looking skin immediately and over time.
A reduced collagen amount in arterial walls is one of the prominent pathological features of CAs,2,3 which is confirmed also in the present study (supplemental Figure I). Excessive collagenolysis in CA walls is induced by the imbalanced expression between MMPs and TIMPs,7 and between cathepsins and cystatin C.5 Decreased collagen biosynthesis in CA walls, the other important aspect of degenerative changes in CA walls, was observed in this study. Expression of procollagen type I and III was downregulated in CA walls at the transcriptional level (Figure 1). Some studies showed a reduced level of type-III collagen in patients with CAs.24,25 Although no mutations were found in the type-III procollagen gene in patients with CAs,26,27 reduced production of type-III collagen may be derived from impaired regulation of gene expression of the type-III procollagen gene.. Collagens must be crosslinked to exhibit the normal physical properties of tensile strength. LOX catalyzes the final enzymatic step for ...
The walls of your arteries are mostly composed of collagen. So having healthy collagen is one of the best ways to prevent hardening of the arteries.. One of the early researchers into this condition, Linus Pauling, recommended a regimen of Vitamin C, lysine and proline to reverse atherosclerosis. Vitamin C is the most important vitamin for growing new collagen. As you know, a lack of Vitamin C will lead to scurvy, which is when your body cant make new collagen! Lysine and proline are two of the more abundant amino acids found in hydrolyzed collagen. So maybe Linus Pauling was onto something.. In our supplement, Collagen Complete, weve combined hydrolyzed collagen with eight other collagen-boosting nutrients. Each serving contains:. 10 grams of Hydrolyzed Collagen. ...
unsatisfactory having been of necessity based on the etiology. Given a case, nouvelle skin collagen cream, ecclivmoses it contained about 10 oiuic s of a yellowish fluid, nouvelle skin collagen cream reviews, with as much caution as he would a penetrating wound of any, nouvelle skin collagen cream amazon, nouvelle skin collagen cream where to buy, been referred to and a general diagnostic rule laid down. ...
Vital Proteins Collagen Peptides are sourced from grass-fed, pasture-raised bovine hides to ensure a natural, sustainable source of this ancient nutrient.
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Saitta B., Wang Y.-M., Renkart L., Zhang R.-Z., Pan T.-C., Timpl R., Chu M.-L.. The alpha 1(VI) and alpha 2(VI) chains, two of the three constituent chains of type VI collagen, are highly similar in size and domain structure. They are encoded by single-copy genes residing in close proximity on human chromosome 21. To study the evolution of the type VI collagen genes, we have isolated and characterized genomic clones coding for the triple-helical domains of the human alpha 1(VI) and alpha 2(VI) chains, which consist of 336 and 335 amino acid residues, respectively. Nucleotide sequencing indicates that, in both genes, the exons are multiples of 9 bp in length (including 27, 36, 45, 54, 63, and 90 bp) except for those encoding for regions with triple-helical interruptions. In addition, the introns are positioned between complete codons. The most predominant exon size is 63 bp, instead of 54 bp as seen in the fibrillar collagen genes. Of particular interest is the finding that the exon structures of ...
... is extracted from the skins of various select fish. This collagen is then purified and dried, and mixed with buffers before it is added to capsules for supplementation. Like chicken collagen, the ability for the body to absorb this fish collagen is only about 15 percent. This means that although the collagen may be more potent than that, it is unable to be absorbed properly into the bloodstream, which renders it less powerful.. On the flip side, bovine collagen that undergoes the same purifying and drying process, but goes a step further, is going to be much more effective. When the collagen is nurtured further under laboratory conditions, its amino acid chains have more time to grow, and they will more closely resemble human amino acid chains. This allows for greater absorption into the bloodstream at rates as high as 95 percent. When you are ordering any collagen supplements, it is wise to investigate how the collagen is processed before being sold.. ...
Paraffin sections of human skeletal tissues were studied in order to identify cells responsible for production of types I, II, and III collagens by in situ hybridization. Northern hybridization and sequence information were used to select restriction fragments of cDNA clones for the corresponding mRNAs to obtain probes with a minimum of cross-hybridization. The specificity of the probes was proven in hybridizations to sections of developing fingers: osteoblasts and chondrocytes, known to produce only one type of fibrillar collagen each (I and II, respectively) were only recognized by the corresponding cDNA probes. Smooth connective tissues exhibited variable hybridization intensities with types I and III collagen cDNA probes. The technique was used to localize the activity of type II collagen production in the different zones of cartilage during the growth of long bones. Visual inspection and grain counting revealed the highest levels of pro alpha 1(II) collagen mRNAs in chondrocytes of the ...
Using a transgenic mouse model in which the human B-myb cDNA was driven by the basal CMV promoter, this study demonstrates for the first time that B-Myb leads to markedly reduced neointima formation after mechanical injury to the vasculature and to decreased α1(I) collagen mRNA expression in the aorta and femoral artery of adult animals. Three independent transgenic mouse lines were generated, all of which apparently developed and bred normally. An inverse relationship between levels of B-Myb protein and expression of α1(I) collagen mRNA in the adult aorta was demonstrated. A decrease was also seen in α2(V) collagen mRNA levels in the aorta and in cultured aortic SMCs isolated from adult transgenic B-myb mice (data not shown). Importantly, when a femoral artery model of endothelial denudation was used, a dramatic reduction in neointima formation was observed in arteries of transgenic versus WT mice 4 weeks after injury. After injury, the neointimal area and the ratio of the areas of the ...
There is disclosed a process for the mineralization of collagen fibers whereby collagen fibers formed from collagen are contacted with a solution of calcium and phosphate ions under conditions to effect nucleation and in-vitro growth of mineral crystals within and on the surface of the collagen fibers to form intact collagen fibers with subfibrillar substructure and wherein preparations of such mineralized collagen fibers are used in bone replacement therapy as well as to induce repair in bony defects.
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We previously advanced the hypothesis that a highly regulated balance of synthesis and degradation determines collagen content in the fibrous cap of atherosclerotic plaques.1,2 In turn, collagen levels critically influence the integrity of the plaques cap, a structure whose biomechanical failure may cause most myocardial infarctions. Earlier indirect evidence suggested that collagenases of the MMP family can regulate collagen content in the plaque.5-12 We initially demonstrated overexpression of the prototypical interstitial collagenase MMP-1 in human atheromata5 and later showed colocalization of MMP-1/collagenase-1 and MMP-13/collagenase-3 with degraded collagen in these lesions as detected by an antibody specific for the collagenase cleavage site of collagen.9 Recently, our group showed that human atheromata contain a third interstitial collagenase, MMP-8/collagenase-2,11 also present in mouse atheromata, as shown here (Figure 2C). Shah et al32 reported that conditioned media of cultured ...
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A bacterial collagen-like proteins Scl2 continues to be developed like a recombinant collagen magic size program to host human being collagen ligand-binding sequences, with the purpose of generating biomaterials with selective collagen bioactivities. at the best testable concentrations, the build was struggling to promote DDR autophosphorylation. The recombinant collagen indicated in will not consist of hydroxyproline (Hyp), and complementary artificial peptide studies demonstrated that alternative of Hyp by Pro in the important Gly-Val-Met-Gly-Phe-Hyp position reduced the DDR-binding affinity and therefore required an increased focus for the induction of receptor activation. The power from the recombinant bacterial collagen to bind the DDRs without inducing kinase activation recommended it could hinder the relationships between pet collagen as well as the DDRs, and this inhibitory part was verified and with a cell migration assay. This study illustrates that recombinant collagen can complement ...
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Collagen on the go - perfect for your handbag and travelling!. O Nutricia collagen helps plump the outer layer of your skin naturally, thus reducing the appearance of ne lines and other aws. Hair is improved by replenishing the hair follicles with collagen.. Cartilage is regenerated by stimulating chondrocytes. Stimulating osteoblasts, improves bone density. Collagen contains Proline and Glycine, that can help repair damaged cells in the intestinal wall.. The health conscious, athletes, Banters and those following Paleolithic Nutrition principles can use O Nutricia Collagen. Improved results may be seen when used in conjunction with a low carbohydrate lifestyle. Whilst our body produces sufcient amounts of amino acids, during times of stress or sickness these levels drop and so supplementation is essential. Collagen peptides have a higher rate of absorption and bio-availability, than Gelatine and work on a cellular level.. ...
Rabbit anti Human collagen IV antibodyrecogizes human collagen IV, also known as Collagen alpha-1(IV) chain. Collagen IV is a 1497 amino a
I would increase the collagen concentration. However, Ive never tried to make collagen gels on glass surfaces. I regularly grow cells in collagen gels in 24-well and 6-well plates (plastic) and as long as the collagen is at high enough concentration, the collagen stays attached to the plastic. Also, you should consider increasing the amount of collagen gel mix you add to the well. The pH of the gel is also critical for good gel integrity, so consider adding more NaOH. Also, be gentle when pipetting and removing media (thats usually not an issue if the collagen has good integrity; but it could be critical for collagen attached to glass).. ...
This happens because we lose collagen as we get older. Collagen is the building block of skin, and as it diminishes so too does the plumped skin of our youth.. Collagen loss starts early. During our early 30s collagen production slows, and from this point our faces starts to lose volume.. How fast you lose collagen depends on genetics and environmental factors. If skin is exposed to too much ultra-violet light from the sun, collagen is lost more quickly. By our early 40s many of us will already be looking gaunt.. Thankfully, though, there are ways to restore lost collagen and re-plump skin. Here are our two favourite choices.. Sculptra. This treatment involves injecting a substance call poly-L-lactic acid (PLLA) into the face. PLLA triggers fibroblast cells in the skin to secrete collagen.. PLLA has been used in surgical sutures for many years, so is known to be safe.. A few treatments are needed but over the coming months you will start to see a difference as the fibroblast cells produce more ...
2150-0060 recognizes human Collagen type II, an extracellular matrix protein found mainly in cartilaginous tissue. The antibody reacts with both native and
This is one of the most unique products I have ever seen and Im thrilled to be able to offer this exclusive Collagen Superfood Formula that you cannot get ANYWHERE ELSE!" - Jordan Rubin, New York Times best-selling author of The Makers Diet and founder of Garden of Life. When the body doesnt have enough collagen, the skin starts to thin, wrinkle and sag. Hair gets lifeless or limp, and tendons and ligaments arent as elastic as they use to be. Your joints can feel it, too. They can get stiff and "creaky.". However, supplementing with collagen can help boost collagen levels in the body to support healthy tendons, ligaments, joints, and skin. Additionally, collagen protein supplements may support better metabolism, boost energy levels and help to maintain healthy muscle tissue. Collagen does so much for the body and in the body to keep it healthy. Its literally the "glue" that holds us together, so make sure you get enough of it. Theres no need for you or your health to fall apart. Bone Broth ...
This MAV Nutrition collagen protein supplement is another product that combined types I, II, III, IV and X collagen, to rip the benefits of their joint action on your skin, hair, joints, digestive tract, and immune system.. Two downsides stem from the otherwise top-quality collagen hydrolysate used:. 1) the end product is premium, so quite expensive and 2) it takes a while to see the improvements after starting to supplement your diet with this product.. Even if it takes a while to work, you have the 60-days money back guarantee if youre not happy with the product.. This powder is healthy, with natural ingredients and it mixes well in all sorts of drinks and shakes.. However, it is one of the few collagen protein powders that might contain traces of nuts and dairy. ...
Triple-helical peptides (THPs) have been utilized as collagen models since the 1960s. The original focus for THP-based research was to unravel the structural determinants of collagen. In the last two decades, virtually all aspects of collagen structural biochemistry have been explored with THP models. More specific
Human body has numerous components for performing diverse functions. One such component in human skin is collagen, which helps in retaining the elasticity of the skin. Collagen is one abundant protein inside body that provides structural support for bones, ligaments and tendons. The texture and shape of human skin depend upon the amount of collagen protein in our body. But the synthesis of collagen gradually decreases as an individual grows old; this results in the appearance of fine lines and wrinkles around eye and lip areas. A new method of cosmetic skin treatment to maintain the collagen level includes a non-surgical method to inject synthetic collagen in to human skin. Collagen injection methods are widely used for providing a temporary solution to those individuals seeking for instant face lift for a youthful and wrinkle-free skin. As a non-surgical method, this method is also easy to handle with absolutely no pain after treatment. Additionally, patients do not have to lose time from their ...
Collagen is the main structural protein found in skin and connective tissues like joints, tendons, cartilage and ligaments. In fact, 30% of the total protein in a dogs body is collagen. It determines the strength and elasticity of their hair, bones, nails, and teeth. As dogs age, their capacity to produce collagen diminishes making them more susceptible to injuries, painful conditions of the bones and joints, and poor skin and coat health.. The depletion of healthy collagen in the body is a natural part of the aging process, but that does not mean that it is gone forever. Lost collagen can be replaced through supplementation, and the earlier you begin providing additional collagen in your dogs diet, the more likely you are to stave off problems.. ...
What is Collagen? Collagen is a protein that can be found in 75% of the skin. It plays a vital role in maintaining healthy-looking skin, as well as skin cell structure. Collagen can help boost elasticity, suppleness and skin tone, so maintaining healthy levels within the body is important to ensure your skin is kept in optimal health. After the age of 25, collagen synthesis, the process of combining different amino acids and components to make new collagen, begins to decrease at a rate of 1.5% each year. By the age of 45, collagen levels may fall as much as 30%, which could cause the appearance of wrinkles, fine lines and dry skin. Helps support your joints Collagen forms around one-third of the proteins present in the joints, tendons, ligaments and bones. These proteins also contain naturally produced glucosamine and chondroitin, which play incredibly important roles in maintaining healthy joint movement and function. Collagen is also present in the synovial membrane that surrounds joints and acts
Barbara Brodskys research focuses on collagen, an extracellular matrix component critical for tissue structure, mechanical properties, cell adhesion and receptor mediated cell signaling. She characterizes structural features of collagen using model peptides and a recently developed recombinant bacterial collagen. The recombinant molecules serve as an excellent model system for defining collagen binding sites and the effects of collagen mutations, while the peptides allow definition of high resolution features at biologically important sites. Research is currently underway to clarify the pathway from human collagen mutations to hereditary bone disorders, kidney disease, and vascular pathology. Studies are being initiated to utilize the recombinant collagen system as a scaffold to promote bone generation by human stem cells and for the development of biomaterials.. ...
Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. ...
So what is collagen and how does it actually work? Collagen is the most common protein found in the body; we have it in all of our connective tissues and its especially common in the skin. Collagen is a type of protein that creates structure and strength in many of our tissues. Our body produces less and less collagen as we age - this is part of our normal ageing process. Many people know that by taking a collagen supplement they can make a dramatic improvement in the appearance of their skin (visually reduce wrinkle depth and improve skin tone), but much more important is how DeepMarines small-molecule, fish-scale collagen can treat and heal eczema and dermatitis. DeepMarine works by reducing inflammation, which stops the itch and allows skin to heal. Its also important to know that inflammation causes cell damage and cell death. DeepMarines small-molecule, fish-scale collagen also has a significant protective effect for skin cells, which diminishes damage from inflammation in the skin. ...
Collagen is the most abundant protein in the body, but you lose it as you age. Supplementing with bovine collagen can help, along with benefit your health.
Most of the time the first place you will notice collagen loss will be in your face area. This is where your collagen decreases first. If youre on the search for ways how to restore collagen in the face then your new best friend will be vitamin C! Vitamin C is full of powerful antioxidant properties that restore and renew your skin keeping you looking younger, longer. Whether you decide to use a vitamin C serum or a supplement, they are both great for aiding in skin health.. When you begin to lack vitamin C in your body you will notice sagginess in your breasts, face and chest area due to loss of elasticity. You can rebuild the collagen and elasticity in these areas by taking a supplement that includes natural herbs and vitamin C. You need collagen for skin tightening along with other vitamins. If your concern is your breast area, you may take a natural breast enhancer that includes vitamin C to repair the tissues in your chest making them appear fuller. The best way to take any supplement that ...
Buy LOréal Wrinkle Decrease Collagen Day Cream 50ml from our Moisturisers range at Tesco direct. We stock a great range of products at everyday prices. Clubcard points on every order.
Collagen Solutions Plc. (the "Company" or the "Group"). Trading Update and Notice of Results. Collagen Solutions plc (AIM: COS), the developer and manufacturer of medical grade collagen-based biomaterials for use in research, diagnostics, medical devices, and regenerative medicine, provides an update on trading for the six months to 30 September 2017.. Revenue and other income is expected to be £1.86m, (H1 2016: £1.89m). Whilst the quality and scale of our sales pipeline are both at their highest levels to date, our first half revenues have been impacted by revenue recognition issues (£150k) and anticipated orders which, for various reasons, have either not materialised or have been delayed by our customers own internal issues (2016 equivalent £341k). Those revenues affected by revenue recognition will flow through positively during the second-half of the financial year. As already highlighted in our August AGM statement, revenue growth this year is expected to occur in the second-half of ...
A process for producing a collagen-based cross-linked biopolymer is provided in which a collagen solution free of low-molecular impurities is saturated with nitrogen protoxide, its concentration is brought to maximum 80 mass percent and the solution is exposed to an ionizing radiation in a dose of 0.5 to 15 kGy. An implant for hermetization of corneal and scleral wounds involved in eye injuries prepared from said bipolymer has the shape and size that provide for complete hermetization of said wounds. The method for its preparation comprises saturation of a collagen solution free of impurities and having a concentration of 0.2 to 1.3 mass percent, with nitrous oxide, filling of a mould with said solution and its exposure to an ionizing radiation in a dose of 0.5 to 15 kGy. The resultant blank is dried to a moisture content in its biopolymer of 30 to 50 mass percent, whereupon the blank is given the shape and size of a required implant. The method of hermetization of said wounds is carried into effect by
Made In Japan Best Collagen Supplements For Anti Aging And Japanese Collagen Supplements japanese collagen supplements whitening fish collagen vitamin c supplements made in japan view, japanese collagen supplements made in japan best collagen supplements for anti aging and, high quality collagen powder contained japanese super popular japanese collagen supplements, made in japan best collagen supplements for anti aging and japanese collagen supplements, ...
withinUs TruMarine™ Collagen is an ultra-pure, premium select grade collagen peptide. Free from artificial colours, flavours, additives, preservatives, and stabilizers, it is simply the highest grade of collagen available.Health Canada approved and Non-GMO Project Verified, our collagen is produced using only the scales of wild, sustainably-sourced fish from the deep, pristine waters of the South Pacific. We use an enzymatic process, rather than heat or chemicals. withinUs TruMarine™ Collagen is highly bioavailable which ensures maximum absorption.Collagen is the most important structural protein in the body, representing 75% of our skin and 7% of our total body weight. However, from the age of 25, we lose approximately 1% of our collagen each year, which causes skin to wrinkle, joints to stiffen and bones to weaken. Our ultra-pure TruMarine™ Collagen offers a high concentration of specific amino acids, which have been scientifically proven to help with the formation of collagen within the body.
Enhance your natural beauty from the inside out. Isagenix Collagen Bone Broth can positively support collagen production, that naturally declines as we age and keeps you feeling satisfied on cleanse days. Our Collagen Bone Broth is infused with collagen peptides and Vitamin C --both crucial components the body needs to produce collagen and boost the vitality of skin, when taken on a regular basis. Indulge in the restorative experience you deserve. 8g of high-quality collagen peptides and bone broth protein from grass fed cows never treated with hormones or routine antibiotics.
COLLAGEN. Natural Collagen transdermal Gel collagen COSMECEUTICALS with cure effects on skin collagen, nails, hair and the whole body collagen
20 Grams of Collagen. 1 Simple Ingredient. 0 Flavors, Colors, or Sweeteners. 0 Banned Substances. Hair, Skin, Nails, and Joints. Made Form Grass-Fed Bovine Hide, Rivalus Collagen Peptides Are A Premium Source Of The Emerging Nutritional Ingredient. Collagen Is The Most Abundant Protein In The Body, Supporting The Vitality Of Skin, Hair, Nails, Bones, And Joints. Why Rivalus Collagen Peptides? Sugar Free. Gluten Free. Keto Friendly. Paleo Friendly. Filler Free ...
Context. - The deposition of extracellular matrix is a major pathogenic mechanism leading to fibrosis and progressive decline in renal function in patients with lupus nephritis (LN). Currently, available clinicopathologic features cannot predict renal outcome consistently. Objective. - To test that the expression of renal fibrogenic genes correlates with renal fibrosis at the time of biopsy and is predictive of renal outcomes. Design. - Renal gene expression levels of transforming growth factor β-1 (TGFB1), and collagen I (COL1) were studied by real-time multiplex quantitative polymerase chain reaction in a prospective cohort of patients with LN (n = 39). Extracellular matrix index (ECMI) and collagen I/ III matrix index were measured from Picro-Sirius Red- stained slides under normal and polarized light, respectively. Results. - After follow-up (median, 43.9 months), renal failure (50% reduction in glomerular filtration rate [GFR] or dialysis) had developed in 13 subjects. The expression ...
TY - JOUR. T1 - Inhibitory effect of dicationic diphenylfurans on production of type I collagen by human fibroblasts and activated hepatic stellate cells. AU - Stefanovic, Lela. AU - Stephens, Chad E.. AU - Boykin, David. AU - Stefanovic, Branko. PY - 2005/3/11. Y1 - 2005/3/11. N2 - Excessive production of extracellular matrix is responsible for clinical manifestations of fibroproliferative disorders and drugs which can inhibit excessive synthesis of type I collagen are needed for the therapy. Several dicationic diphenylfurans were synthesized and were found to bind RNA. Two of these type compounds were able to reduce synthesis of type I collagen by human fibroblasts and human activated hepatic stellate cells (HSCs). Activated HSCs are responsible for collagen production in liver fibrosis. When added at 40 μM compound 588 reduced intracellular level and secretion of procollagen α1(I) by 50%, while compound 654 reduced these parameters by more than 80% at 20 μM. 654 also significantly reduced ...
Many people take collagen to stop creases, or to fix already existing skin damage. Thus far, its uncertain how effective collagen supplements are in enhancing skin wellness, says Dr. Patricia Farris, a skin doctor and also clinical associate teacher at Tulane College School of Medication.. Essential Proteins Collagen Peptides are sourced from grass-fed, pasture-raised bovine hides to make sure a natural, high quality, and also lasting source of this old nutrient. Collagen is one of the most abundant healthy protein in the body guaranteeing the wellness as well as vigor of your skin, hair, ligament, cartilage material, bones, as well as joints. ** These all-natural peptides are extremely bio-available, digestible and also soluble in cool or warm liquids.. Naturally, collagen originates from animal bones, ligaments, and cartilage, commonly in the form of jelly-- jelly is the prepared form of collagen. Thats why bone broth has actually come to be such an en vogue food product, especially for ...
Collagen loss is one of the most troublesome areas when it comes to aging and your skin and peptides can help to fight this issue. Peptides are chains of amino acids that serve as the building of protein in the skin, such as collagen. Collagen is responsible for skin thickness and suppleness, but your production naturally slows down as you age. When peptides form a short chain of amino acids, they can send signals to your skin cells that tell them how they should be behaving. Applied topically, peptides send signals to your cells that indicates its time to begin the formation of new collagen. As new collagen forms, the appearance of fine lines and wrinkles is diminished.. Anti-aging ingredients can be very powerful on their own, but most work better when combined with other ingredients as well. Now that you know what these amazing anti-aging ingredients do, you can look for products that contain them with confidence that they are going to perform well for your needs.. ...
Bovine collagen is a naturally occurring protein that is found in the skin, bones, and muscles of cows. This collagen is so similar to human collagen that many people in
Collagen injections are used in correcting fine lines and wrinkles, as well as shallow scars. Collagen injections and other injectable fillers give your skin plumber, smoother appearance. Normally, collagen injections treat areas around the mouth, like laugh lines and deep nasolabial creases. Although collagen is the best known filler, there are many other substances doctors can use to treat your skin, including fat from your own body and synthetic materials.. Doctors can use collagen injections to supplement the bodys natural collagen supply, which decreases over time. Using a series of collagen injections, doctors can raise the treated area, smoothing wrinkles and creases. Although many patients want to go through these procedures to treat areas of the face, there are other known uses for collagen injections which include softening of scar tissue, and creating fuller lips. Those who are interested in collagen injections must consult with a physician to ensure that they qualify. There are ...
The veggie blend dissolves in water which makes it perfect for smoothies, but Im using it raw in these fat balls which works fine too!. 2. They have gut healing collagen protein.. You guys know I love vital proteins collagen protein. Not only does it add a boost of protein to snacks like these to make it more satiating, but collagen protein also contains gut healing properties that support gut health, hair and nail health, and more. I recommend collagen as a part of my 30 day gut healing guide, and to most of my clients on gut healing protocols. 3. Theyre full of healthy fat.. These are largely coconut butter based with some coconut oil as well, which are both healthy, nourishing fats. Healthy fats are vital for the health of our brain, our hormones, our blood sugar, and for keeping us full!. The biggest mistake that I see people make with snacks is reach for something sugar heavy without any fat. While natural sugar here and there is fine, relying on sugar alone to satiate us is not a ...
After MI in rats, systolic function declines and the LV cavity dilates significantly, and these changes progress over time. We noted improved systolic performance after P4H inhibition. This improvement was quite dramatic and was sustained from week 1 to week 4, suggesting that fibrosis in the noninfarcted myocardium after MI contributes to LV dysfunction.. The early increase in LV cavity dimension in MI-control animals in this study is consistent with previous studies.19,20 In contrast, the MI-FG041-treated animals had an altered pattern of LV dilatation with less progressive cavity dilatation. This finding should be contrasted with previously published work. Specifically, Zhao and others6,21 suggested that collagen matrix disruption is a primary factor involved in LV dilatation during ischemic cardiomyopathy, whereas Rohde et al22 showed that MMP inhibition, which preserved extracellular collagen, decreased early dilatation of the LV after MI in mice. In addition, a number of studies using ACE ...
The invention provides graft, prothesis, orthopaedic structures, implants and like body replacement parts which are constituted of synthetic collagen fibers, an embodiment of which is a tendon or a ligament prosthesis, graft or implants. These body parts have a combination of very useful properties, particularly high tensile strength combined with biocompatability.
Collagen Hybridizing Peptides (CHP) conjugates from Advanced BioMatrix are labeled with 5-FAM (F-CHP, Catalog No. 5264-60UG) / sulfo-Cyanine3 (R-CHP, Catalog No. 5276-60UG) for fluorescence detection, or biotin (B-CHP, Catalog No. 5265-UG) for avidin/streptavidin-mediated detection.. The triple helix is the hallmark protein structure of collagen. During tissue remodeling, the triple helical collagen molecules are degraded by specific proteases (e.g., MMP or cathepsin K) and become unfolded at body temperature. The Collagen Hybridizing Peptide (CHP) is a synthetic peptide that can specifically bind to such denatured collagen strands through hydrogen bonding, both in histology, in vivo, and in vitro (3D cell culture). By sharing the structural motif and the Gly-X-Y repeating sequence of natural collagen, CHP has a strong capability to hybridize with denatured collagen strands, in a fashion that is similar to a DNA fragment annealing to its complimentary DNA strand during PCR. CHP is an extremely ...
Structural protein are essential for providing structure and rigidity to fluid biological cells and components. Structural proteins are fibrous proteins which provide support for the cells. Structural proteins are usually very large and are made up with up to thousands of amino acids. Insects and spiders use silk fibers to for various tasks such as making their cocoons and webs [1]. Another example of a structural protein can be seeing in Keratin which is the protein of hair, feathers and horns among other things [1]. Actin and collagen are specific examples that fall under this category of proteins. Collagen, recognized as one of the most abundant proteins in mammals, is the main component in connective tissue. Collagen can be found in the tendons, ligament and skin. Collagen can also be found abundant in cornea, cartilage, bone, and blood vessels. Collagen composes about 25-35% of the entire protein content in the human body, which illustrates the importance of structural proteins such as this ...
Collagen is a very abundant, natural protein in the body that creates tissue strength and structure. Its composed of long chains of amino acids and known to have tremendous tensile strength. It ensures the soft tissues in joints are durable and sturdy. When we are young our collagen will regenerate quickly, but as we age our bodys tissues repair themselves more slowly and less efficiently. Also, inherent in the aging process is a decline in our bodys ability to produce collagen; unbelievably, this decline begins around age 25! Joint and back pain is not a problem that is exclusively restricted to "old people." Many young and middle-aged people suffer greatly from joint pain, which is immensely disruptive to their lives. In these cases, collagen can be extremely helpful in regenerating tissues in the joints and reducing the associated stiffness. With healthier joint tissues comes decreased aches and pains ...
Purpose: Our goal is to develop and apply a set of optical and computational tools to enable large-scale investigations of the interaction between collagen and tumor cells. Methods: We have built a novel imaging system for automating the capture of whole-slide second harmonic generation (SHG) images of collagen in registry with bright field (BF) images of hematoxylin and eosin stained tissue. To analyze our images, we have integrated a suite of supervised learning tools that semi-automatically model and score collagen interactions with tumor cells via a variety of metrics, a method we call Electronic Tumor Associated Collagen Signatures (eTACS). This group of tools first segments regions of epithelial cells and collagen fibers from BF and SHG images respectively. We then associate fibers with groups of epithelial cells and finally compute features based on the angle of interaction and density of the collagen surrounding the epithelial cell clusters. These features are then processed with a ...
For Any Query, Contact Our Expert. In Nutshell, the report focuses on global major leading Collagen Market players with information such as company profiles, contact information. Collagen Market Sales, Price, Revenue, Gross Margin and Market Share, Product Type and Applications, Regions, analysis is also carried out. Whats more, the Global Collagen Market development trends and marketing channels are analysed.. Price of Report: $3480 (Single User License). Ask for Discount @ http://www.marketreportsworld.com/enquiry/request-discount/10289499. Table and Figures Covered in This Report:. · Table and Figure: Collagen Product Picture. · Table and Figure: Development of Collagen Manufacturing Technology. · Table and Figure: Manufacturing Process of Collagen. · Table and Figure: Company Collagen Product and Specifications. · Table and Figure: Company Collagen Product Capacity, Production, and Production Value etc. List. · Table and Table and Figure: Global Collagen Key Manufacturers Capacity ...
Gentaur molecular products has all kinds of products like :search , AbD \ RABBIT ANTI HUMAN COLLAGEN IV, Product Type Polyclonal Antibody, Specificity COLLAGEN IV, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications C, E, IF, P*, \ 2150-0140 for more molecular products just contact us
As you aged, there is global volume loss of internal facial tissues. There is loss of bone density as your skull becomes smaller, loss of collagen and muscle tissues, as well as fat resorption.. As a result of the aging processes, your skin sags and becomes droopy. Folds at the cheeks, tear trough, laugh lines and corners of the mouth become more prominent. There is development and deepening of wrinkles. There is also development of pigmentation of the skin associated with aging.. Collagen Stimulators helps to replace and reinforce the skins collagen structure within the deep dermis. This reinforced collagen structure provides a foundation that gradually restores the fullness of your facial contour which in term smooths out shallow to deep facial wrinkles and folds that has been depleted over time. The result? A refined, more youthful looking appearance over time that are potentially long lasting.. ...
Appearance: off white powder Particle size|0.35mm: 95% Made from bovine skin Hydrolyzed Bovine collagen is made of fresh Bovine skin through pretreatment and biodegradation of the collagen with biological enzyme, to form macromolecular collagen...
COLLAGEN. Transdermal Gel Natural Collagen COSMECEUTICALS with cure effects on skin collagen, hair, nails and the entire body collagen
Peptides or short protein domains derived from the extracellular matrix are reported to possess anti-tumor properties. In the present study, one such molecule "Hexastatin or [α6(IV)NC1]" a non-collagenous domain of α6 chain of type (IV) collagen was derived from the carboxy terminal and was found to inhibit tumor growth, but the mechanism by which it inhibits the growth of solid tumors has not been reported yet. In the present study, we identified that the biological functions of hexastatin are attributed to its binding to different cell surface integrins. We identified that hexastatin binds to α3β1, αVβ3 and α5β1 integrins and inhibits p38-MAPK signaling. Hexastatin competes with human vascular endothelial cells in binding to α1β1 integrins on type IV collagen, and or with α5β1/αVβ3 integrins on fibronectin/vitronectin matrix, thus inhibiting endothelial migration and tube formation. Interestingly, p38-MAPK phosphorylation was not inhibited in α3 and β3 integrin null endothelial ...
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LAIR-1 is a collagen receptor. (A) SK-BR3 cells express a collagen ligand for LAIR-1 that is not collagen XVII. HT29 or SK-BR3 cells were stained with hLAIR-1-IgG or anti-collagen XVII mAb (filled histograms) with or without pretreatment with collagenase. Open histograms represent staining with isotype-matched control Ig. (B) 293T cells were transiently transfected with control vector (open histograms) or indicated HIS-tagged collagens (gray histograms) and stained with hLAIR-1-IgG (top) or anti-HIS antibody (bottom). Similar results were obtained using hLAIR-2-IgG, mLAIR-1-IgG, and rLAIR-1-IgG. (C) Fluorescently labeled wt K562 cells (open bars) or K562 cells expressing hLAIR-1 (black bars) or KIR3DL1 (gray bars) were monitored for their capacity to bind immobilized collagens I, II, and III. Where indicated, cells were preincubated with anti-hLAIR-1 F(ab′)2 (8A8) fragments (hatched bars). Two other members of the IgSF (CD48 and CD80 transfected in K562 cells) did not associate with collagens ...
TY - JOUR. T1 - Effect of HINS light on the contraction of fibroblast populated collagen lattices. AU - McDonald, R.. AU - MacGregor, S.J.. AU - Maclean, M.. AU - Anderson, J.G.. AU - Grant, M.H.. PY - 2009. Y1 - 2009. N2 - High intensity narrow spectrum (HINS) light has been shown to have bactericidal effects on a range of medically important bacteria[1]. HINS technology could potentially be useful as a method for disinfecting medical implants, tissue engineered constructs and wounds. The fibroblast populated collagen lattice (FPCL) was used as an in vitro model to investigate the effect of HINS light on the wound contraction phase of wound healing.. AB - High intensity narrow spectrum (HINS) light has been shown to have bactericidal effects on a range of medically important bacteria[1]. HINS technology could potentially be useful as a method for disinfecting medical implants, tissue engineered constructs and wounds. The fibroblast populated collagen lattice (FPCL) was used as an in vitro model ...
In order to be collected for use, collagen is taken from other dead mammals (usually livestock for commercial use). The basic extraction is generally done using a process of cooking cartilaginous animal materials, such as bones, connective tissues and skin. This process creates gelatin (a form of collagen that has experienced partial hydrolysis, combining with the water at a molecular level) and can often be witnessed in the home during the cooking of meat bones into soup. How the collagen gelatin is treated depends on what it is going to be used for, but it must at least be purified to remove other materials from the animal matter, such as fats and salts.. In some cases, collagen can also be collected from human remains (donated or leftover from surgical operations) for the sake of medical uses of the protein, since human-extracted collagen is less likely to be rejected by another human body.. ...
SureCoat®, Bovine Collagen, Solution, 3 mg/mL [BM-5057-100ML] - SureCoat® collagen is provided for coating surfaces and is not intended for gel applications. SureCoat® is highly purified (|99.9% collagen content) and has excellent coating functionality and properties. SureCoat® is isolated from bovine hides sourced from the only controlled, closed herd in the United States. Advanced BioMatrixs manufacturing processes comply with stringent
Unilever Collagen Pills Phytoceramides offer dietary support for aging skin. Ahc Collagen Cleansing Cream 1 Type stop the problem before its too late. only collagen itself can restore the collagen layer.. Blocked sinuses can lead to swelling temporarily causing dark circles. Commonly reported side effects and conditions associated with Undenatured Type II Collagen laser wrinkle removal ireland Cartagena was signed phytoceramides review info to relativity records phytoceramides review info the sexual seeds recording ine and Botox Treatments for Bruxism now available in our Harley Street clinic. Revitaliserende planteekstrakter fr Bone oth is considered to be most full of nutrient-dense goodness if it gels. 4.3 Stars out of 73 reviews. phytoceramide capsules plant derived Differences allegedly worked means munitions 1990s and shares Proflex also effectively stimulate collagen production by adding collagen alpha II hydrolysate to its composition.. Do you experience leakage due to an overactive ...
William C. Robbins, Robert F. Watson, George D. Pappas, Keith R. Porter; Some Effects of Anti-Collagen Serum on Collagen Formation in Tissue Culture: A Preliminary Report . J Biophys and Biochem Cytol 25 July 1955; 1 (4): 381-384. doi: https://doi.org/10.1083/jcb.1.4.381. Download citation file:. ...
(Bristol, PA - December 2014) Gentell, Inc. (www.gentell.com), a leading manufacturer of wound and skin care products, recently announced the introduction of four new collagen products designed to treat chronic, non-healing wounds. Gentell Collagen, a product derived from bovine collagen, is now available in a powdery particle form 1g bottle, or as dressing sheets in 2 x 2 , 4 x 5.25 , and 8 x 12 sizes, for the treatment of aggressive wounds., , , , Collagen reduces high levels of matrix...
In cartilage collagen type XI exists as heterotrimeric molecules composed of alpha 1(XI), alpha 2(XI) and alpha 3(XI) subunits. Messenger RNAs for some of the alpha chains of collagen type XI have also been found in non-chondrogenic tissues but the chain composition of the molecule in these sites is not known. Some non-chondrogenic tissues also contain heterotrimers containing collagen alpha 2(V) and alpha 1(XI) chains. We have explored the possibility that collagen type XI could exist in differing trimeric forms in non-chondrogenic tissues and aimed to predict the subunit composition of this collagen in those tissues. The distribution and relative levels of expression of collagen alpha 1(XI), alpha 2(XI) and alpha 3(XI)/alpha 1(II) mRNAs in different human fetal tissues were studied. Expression of mRNAs for all three genes of collagen type XI is not restricted to cartilage but is widespread. However, in some non-chondrogenic tissues, the mRNAs for all three alpha chains of collagen type XI were ...
TY - JOUR. T1 - Ultrafine carbon black particles inhibit human lung fibroblast-mediated collagen gel contraction. AU - Kim, Huijung. AU - Liu, Xiangde. AU - Kobayashi, Tetsu. AU - Kohyama, Tadashi. AU - Wen, Fu Qiang. AU - Romberger, Debra J.. AU - Conner, Heather. AU - Gilmour, Peter S.. AU - Donaldson, Kenneth. AU - MacNee, William. AU - Rennard, Stephen I.. PY - 2003/1/1. Y1 - 2003/1/1. N2 - Both acute and chronic exposure to particulates have been associated with increased mortality and morbidity from a number of causes, including chronic obstructive pulmonary disease and other chronic lung diseases. The current study evaluated the hypothesis that ultrafine carbon particles, a component of ambient particulates, could affect tissue repair. To assess this, the three-dimensional collagen gel contraction model was used. Ultrafine carbon black particles, but not fine carbon black, inhibited fibroblast-mediated collagen gel contraction. Although previous research has indicated that inflammatory ...
Type V collagen may play a role in graft rejection following lung transplants (See Review: Sumpter TL, Wilkes DS. Role of autoimmunity in organ allograft rejection: a focus on immunity to type V collagen in the pathogenesis of lung transplant rejection. Am J Physiol Lung Cell Mol Physiol 2004; 286: L1129-39). It has been shown that oral tolerance induction by oral administration of type V collagen prevents lung allograft rejection in animal models, and is expected to be used for humans. Importantly, it has been reported that patients who were previously sensitized by type V collagen and positive for type V collagen-DTH reactions tend to develop idiopathic pulmonary fibrosis (58.8%, 10/17) compared to patients who were negative for the DTH reaction (15.8%, 6/38) (Bobadilla JL, Love RB, Jankowska-Gan E, Xu Q, et al. Th-17, monokines, collagen type V, and primary graft dysfunction in lung transplantation. Am J Respir Crit Care Med 2008; 177: 660-8).. Type V and Type XI Collagen ...
Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene. This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. In the absence of mutations, however, an autoimmune response against type VII collagen can result in an acquired form of this disease called epidermolysis bullosa acquisita. Type VII collagen is also found in the retina; its function in this organ is unknown. COL7A1 is located on the short arm of human chromosome 3, in the chromosomal region denoted 3p21.31. The gene is approximately 31,000 base pairs in size and is remarkable for the extreme fragmentation of its coding sequence into 118 exons. COL7A1 is transcribed into ...
OBJECTIVES--To analyse the collagen composition of normal adult human supraspinatus tendon and to compare with: (1) a flexor tendon (the common biceps tendon) which is rarely involved in any degenerative pathology; (2) degenerate tendons from patients with chronic rotator cuff tendinitis. METHODS--Total collagen content, collagen solubility and collagen type were investigated by hydroxyproline analysis, acetic acid and pepsin digestion, cyanogen bromide peptide analysis, SDS-PAGE and Western blotting. RESULTS--The collagen content of the normal cadaver supraspinatus tendons (n = 60) was 96.3 micrograms HYPRO/mg dry weight (range 79.3-113.3) and there was no significant change across the age range 11 to 95 years. There was no significant difference from the common biceps tendon [93.3 (13.5) micrograms HYPRO/mg dry weight, n = 24]. Although extremely insoluble in both acetic acid and pepsin, much of the collagen was soluble after cyanogen bromide digestion [mean 47.9% (29.8)]. Seventeen per cent ...
Phosphatidylinositol 3-kinaseβ (PI3Kβ) plays a predominant role in integrin outside-in signaling and in platelet activation by GPVI engagement. We have shown that the tyrosine kinase Pyk2 mediates PI3Kβ activation downstream of integrin αIIbβ3, and promotes the phosphorylation of the PI3K-associated adaptor protein c-Cbl. In this study, we compared the functional correlation between Pyk2 and PI3Kβ upon recruitment of the two main platelet collagen receptors, integrin α2β1 and GPVI. PI3Kβ-mediated phosphorylation of Akt was inhibited in Pyk2-deficient platelets adherent to monomeric collagen through integrin α2β1, but occurred normally upon GPVI ligation. Integrin α2β1 engagement led to Pyk2-independent association of c-Cbl with PI3K. However, c-Cbl was not phosphorylated in adherent platelets, and phosphorylation of Akt occurred normally in c-Cbl-deficient platelets, indicating that the c-Cbl is dispensable for Pyk2-mediated PI3Kβ activation. Stimulation of platelets with CRP, a ...
This is a non-randomized study. All eyes that qualify for the study will receive the cross-linking (CXL) procedure. Corneal collagen cross-linking is performed as a single treatment. Depending on the patients condition, the CXL procedure may be performed under sedation or anesthesia. Subjects are followed for 12 months after the procedure to evaluate the long term effects of corneal collagen cross-linking ...
A serum-free chemically defined medium (CDM) has been developed which sustains the growth in culture of the highly differentiated human hepatoma cell line Hep G2. Unlike rodent hepatoma lines, Hep G2 cells in serum-free medium have an absolute requirement for lipoprotein lipids (either low density lipoprotein (LDL) or high density lipoprotein (HDL)) for growth. In the presence of LDL (or HDL) growth was further enhanced by insulin, triiodo-L-thyronine, 17 alpha-ethinylestradiol but not by epidermal growth factor (EGF). On type I collagen gels cells cultured in CDM were contact inhibited and formed monolayers. This contrasted with the pattern of growth of cells cultured in the presence of serum on type I collagen gels and cells cultured on tissue-culture plastic in either CDM or medium containing serum which formed foci of multilayered cells. Expression of the LDL receptor and HMG-CoA (3-hydroxy-3-methylglutaryl coenzyme A) reductase genes was comparable in Hep G2 cells cultured in CDM and ...
Reporting of immunofluorescent (IF) double staining for alpha 2 and alpha 5 chains of type IV collagen on kidney biopsies:. 1) Normal pattern of staining (ie, preserved linear alpha 5 staining of glomerular basement membranes, Bowman capsule, and distal tubular basement membranes). This pattern of staining is seen in normal individuals and patients with thin glomerular basement membrane disease but does not exclude the diagnosis of hereditary nephritis/Alport syndrome.. 2) Consistent with X-linked hereditary nephritis (Alport syndrome). There is global or segmental loss of alpha 5 staining of glomerular basement membranes, Bowman capsule, and distal tubular basement membranes. This pattern of loss of staining is usually due to mutations in the COL4A5 gene on the X chromosome.. 3) Consistent with autosomal hereditary nephritis (Alport syndrome). There is global or segmental loss of alpha 5 staining of glomerular basement membranes but preserved alpha 5 staining of Bowman capsule and distal ...
Corneal collagen cross-linking[edit]. Corneal collagen cross-linking may delay or eliminate the need for corneal ... To make the material, the researchers placed a human gene that regulates the natural production of collagen into specially ... "Corneal collagen cross-linking for treating keratoconus". The Cochrane Database of Systematic Reviews. 3: CD010621. doi:10.1002 ...
Bone and collagen[edit]. Cortisol reduces bone formation,[3] favoring long-term development of osteoporosis (progressive bone ... Cortisol down-regulates the synthesis of collagen.[19] Amino acid[edit]. Cortisol raises the free amino acids in the serum by ... Collagen is an important component of connective tissue. It is vital for structural support and is found in muscles, tendons, ... Kucharz EJ (1988). "Hormonal control of collagen metabolism. Part II". Endocrinologie. 26 (4): 229-37. PMID 3062759.. ...
Collagen[edit]. Collagens are the most abundant protein in the ECM. In fact, collagen is the most abundant protein in the human ... and epidermolysis bullosa are linked with genetic defects in collagen-encoding genes.[9] The collagen can be divided into ... Laminins bind other ECM components such as collagens and nidogens.[9] Development[edit]. There are many cell types that ... In biology, the extracellular matrix (ECM) is a three-dimensional network of extracellular macromolecules, such as collagen, ...
Corneal collagen cross-linking[edit]. Main article: Corneal collagen cross-linking. There is evidence suggesting corneal ... Spadea, Leopoldo (2010). "Corneal Collagen Cross-Linking with Riboflavin and UVA Irradiation in Pellucid Marginal Degeneration ... Research shows some promising results by combining collagen cross linking with photorefractive keratectomy, or with topography- ... "Management of pellucid marginal corneal degeneration with simultaneous customized photorefractive keratectomy and collagen ...
Retrieved from "https://en.wikipedia.org/w/index.php?title=Collagen,_type_XX,_alpha_1&oldid=705418915" ...
... is a protein that has been hydrolyzed or broken down into its component amino acids. While there are many means of achieving this, two of the most common methods are prolonged boiling in a strong acid (acid-HVP) or strong base or using an enzyme such as pancreatic protease to simulate the naturally occurring hydrolytic process. Protein hydrolysis can be used to modify the allergenic properties of infant formula. The size of cow milk proteins in the formula and the milk becomes more suitable for consumption by babies suffering of Milk protein intolerance. Common hydrolyzed products used in food are hydrolyzed soy protein and hydrolyzed yeast, which is used as a flavor enhancer. Hydrolyzed Protein is also used in the manufacturing process of certain specially formulated Hypoallergenic Dog Foods for dogs and puppies that suffer from allergies caused by certain protein and carbohydrate types in standard commercial dog food brands. This means that the protein contents of the food ...
InChI=1S/C26H37NO3/c1-18(2)26(29)30-25-13-12-21(17-28)16-24(25)23(22-10-8-7-9-11-22)14-15-27(19(3)4)20(5)6/h7-13,16,18-20,23,28H,14-15,17H2,1-6H3/t23-/m1/s1 ...
collagen. collagen. collagen. none. α-chitin. α-chitin Molting Generally no;[20] but some polychaetes molt their jaws, and ... Annelids' cuticles are made of collagen fibers, usually in layers that spiral in alternating directions so that the fibers ... is made of tough but flexible collagen[7] and does not molt[20] - on the other hand arthropods' cuticles are made of the more ... in other words a combination of cells and non-cellular materials such as collagen. Below this are two layers of muscles, which ...
collagen-containing extracellular matrix. Biological process. • animal organ morphogenesis. • cell proliferation. • ... Tzaphlidou M (2004). "The role of collagen and elastin in aged skin: an image processing approach". Micron. 35 (3): 173-7. doi: ... Fischer GM, Llaurado JG (Aug 1966). "Collagen and elastin content in canine arteries selected from functionally different ...
Saad, Mohamed (Oct 1994). Low resolution structure and packing investigations of collagen crystalline domains in tendon using ... collagen, elastin, and fibroin. The roles of such proteins include protection and support, forming connective tissue, tendons, ... such as a collagen helix. The structures often feature cross-links between chains (e.g., cys-cys disulfide bonds between ...
... acts on M2 and M3[3] subtypes of muscarinic receptors whereas older antimuscarinic treatments for overactive bladder act more specifically on M3 receptors. Tolterodine, although it acts on all types of receptors, has fewer side effects than oxybutynin (M3 and M1 selective, but more so in the parotid than in the bladder) as tolterodine targets the bladder more than other areas of the body. This means that less drug needs to be given daily (due to efficient targeting of the bladder) and so there are fewer side effects.[citation needed] ...
... is an endopeptidase involved in the processing of collagen. The proteases removes the terminal peptides of the procollagen. ...
The cytokeratins are encoded by a family encompassing 30 genes. Among them, 20 are epithelial genes and the remaining 10 are specific for trichocytes. All cytokeratin chains are composed of a central α-helix-rich domain (with a 50-90% sequence identity among cytokeratins of the same type and around 30% between cytokeratins of different type) with non-α-helical N- and C-terminal domains. The α-helical domain has 310-150 amino acids and comprises four segments in which a seven-residue pattern repeats. Into this repeated pattern, the first and fourth residues are hydrophobic and the charged residues show alternate positive and negative polarity, resulting in the polar residues being located on one side of the helix. This central domain of the chain provides the molecular alignment in the keratin structure and makes the chains form coiled dimers in solution. The end-domain sequences of type I and II cytokeratin chains contain in both sides of the rod domain the subdomains V1 and V2, which have ...
... ( anticholinergic agent) is a group of substances that blocks the action of the neurotransmitter acetylcholine (ACh) at synapses in the central and the peripheral nervous system, and, in broad terms, neuromuscular junction.[1][2] These agents inhibit parasympathetic nerve impulses by selectively blocking the binding of the neurotransmitter acetylcholine to its receptor in nerve cells. The nerve fibers of the parasympathetic system are responsible for the involuntary movement of smooth muscles present in the gastrointestinal tract, urinary tract, lungs, and many other parts of the body;[3] cholinergic process otherwise by enhancing ACh function.[3] In broad terms, anticholinergics are divided into two categories in accordance with their specific targets in the central, peripheral nervous system and neuromuscular junction:[3] antimuscarinic agents, and antinicotinic agents (ganglionic blockers, neuromuscular blockers).[4] In strict terms, anticholinergic only comprises ...
collagen-containing extracellular matrix. Biological process. • regulation of cell adhesion. • cell adhesion. • extracellular ... collagens I, III, IV, c-myc and p53". Archives of Oral Biology. 46 (6): 545-55. doi:10.1016/S0003-9969(01)00014-0. PMID ...
... produces a vivid color change in urine, typically to a dark orange to reddish color. This effect is common and harmless, and indeed a key indicator of the presence of the medication in the body. Users of phenazopyridine are warned not to wear contact lenses, as phenazopyridine has been known to permanently discolor contact lenses and fabrics.[1][5] Some may be mistakenly concerned that this indicated blood in the urine. Phenazopyridine can also cause headaches, upset stomach (especially when not taken with food), or dizziness. Less frequently it can cause a pigment change in the skin or eyes, to a noticeable yellowish color. This is due to a depressed excretion via the kidneys causing a buildup of the medication in the skin, and normally indicates a need to discontinue usage.[2] Other such side effects include fever, confusion, shortness of breath, skin rash, and swelling of the face, fingers, feet, or legs.[1][2] Long-term use may cause yellowing of nails.[6] Phenazopyridine ...
Okada M et al (2007) Primary collagen VI deficiency is the second most common congenital muscular dystrophy in Japan. Neurolog ... that is caused by a mutation in one of the three genes coding for type VI collagen.[2] These include COL6A1, COL6A2, and COL6A3 ... "Collagen VI related muscle disorders" (PDF). J. Med. Genet. 42 (9): 673-85. doi:10.1136/jmg.2002.002311. PMC 1736127 . PMID ...
Collagen disease. COL1:. *Osteogenesis imperfecta. *Ehlers-Danlos syndrome, types 1, 2, 7 ...
The organic compound citrulline is an α-amino acid. Its name is derived from citrullus, the Latin word for watermelon, from which it was first isolated in 1914 by Koga and Odake.[2] It was finally identified by Wada in 1930.[3] It has the formula H2NC(O)NH(CH2)3CH(NH2)CO2H. It is a key intermediate in the urea cycle, the pathway by which mammals excrete ammonia by converting it into urea. Citrulline is also produced as a byproduct of the enzymatic production of nitric oxide from the amino acid arginine, catalyzed by nitric oxide synthase.[4] ...
"OMIM Entry - *113811 - COLLAGEN, TYPE XVII, ALPHA-1; COL17A1".. [permanent dead link] ... and/or type XVII collagen, also called Bullous Pemphigoid Antigen 2,[6] which is a component of hemidesmosomes. A different ...
Collagen disease. COL1:. *Osteogenesis imperfecta. *Ehlers-Danlos syndrome, types 1, 2, 7 ...
Amino acid supplements, including L-ornithine, are frequently marketed to bodybuilders and weightlifters with claims for increasing levels of human growth hormone (HGH), muscle mass and strength. A clinical study reported that L-ornithine at 2 g/d did not increase HGH.[6] A review on the topic concluded "The use of specific amino acids to stimulate GH release by athletes is not recommended."[7] ...
Neurons that produce GABA as their output are called GABAergic neurons, and have chiefly inhibitory action at receptors in the adult vertebrate. Medium spiny cells are a typical example of inhibitory central nervous system GABAergic cells. In contrast, GABA exhibits both excitatory and inhibitory actions in insects, mediating muscle activation at synapses between nerves and muscle cells, and also the stimulation of certain glands.[4] In mammals, some GABAergic neurons, such as chandelier cells, are also able to excite their glutamatergic counterparts.[5] GABAA receptors are ligand-activated chloride channels: when activated by GABA, they allow the flow of chloride ions across the membrane of the cell. Whether this chloride flow is depolarizing (makes the voltage across the cell's membrane less negative), shunting (has no effect on the cell's membrane potential), or inhibitory/hyperpolarizing (makes the cell's membrane more negative) depends on the direction of the flow of chloride. When net ...
Collagen disease. COL1:. *Osteogenesis imperfecta. *Ehlers-Danlos syndrome, types 1, 2, 7 ...
Crick engaged in several X-ray diffraction collaborations such as one with Alexander Rich on the structure of collagen.[57] ... "The structure of collagen" (PDF reprint). Nature. 176 (4489): 915-6. Bibcode:1955Natur.176..915R. doi:10.1038/176915a0. PMID ...
protein tyrosine kinase collagen receptor activity. • protein tyrosine kinase activity. • ATP binding. • collagen binding. ... collagen-activated tyrosine kinase receptor signaling pathway. • ossification. • phosphorylation. • collagen fibril ... Leitinger B (May 2011). "Transmembrane collagen receptors". Annu. Rev. Cell Dev. Biol. 27: 265-90. doi:10.1146/annurev-cellbio- ... Leitinger B, Kwan AP (2006). "The discoidin domain receptor DDR2 is a receptor for type X collagen". Matrix Biol. 25 (6): 355- ...
... a minor fibrillar collagen. It is located on chromosome 6 very close to but… ... This gene encodes one of the two alpha chains of type XI collagen, ... Background of Collagen type XI alpha 2 chain antibody. This gene encodes one of the two alpha chains of type XI collagen, a ... Type XI collagen is a heterotrimer but the third alpha chain is a post-translationally modified alpha 1 type II chain. ...
Find out information about Collagen-vascular disease. see autoimmune disease autoimmune disease, any of a number of abnormal ... collagen disease. (redirected from Collagen-vascular disease). Also found in: Medical. collagen disease:. see autoimmune ... Click the link for more information. ; collagencollagen. , any of a group of proteins found in skin, ligaments, tendons, bone ... collagen disease. [′kä·lə·jən di‚zēz] (medicine) Any of various clinical syndromes characterized by widespread alterations of ...
Collagen vascular disease and pregnancy the. Nonetheless, due to limited space we do ask that you invite no collagen vascular ... Click right here coklagen read extra about our work collagen vascular disease and pregnancy the impression we gascular collagen ... Hughes E, Collins J, Vandekerckhove P. Some ladies resolve to hire a collagen vascular disease and pregnancy to assist help ... Collahen involuntary leaking could occur when coughing, sneezing and collagen vascular disease and pregnancy laughing. As ...
Injectable Homone from Injectable Polypeptide Hormones Corticotropin Muscle Building and Collagen Diseases - Wuhan Yuancheng ... China Injectable Polypeptide Hormones Corticotropin Muscle Building and Collagen Diseases, Find details about China Muscle ... 99% Injectable Polypeptide Hormones Corticotropin CAS 9002-60-2 ACTH For Muscle Building & Collagen Diseases. 1. ... lupus and other collagen diseases. Clinical use of cortisone similar.. 2.Description: ...
Reporting of immunofluorescent (IF) double staining for alpha 2 and alpha 5 chains of type IV collagen on kidney biopsies: ... Reporting of IF double staining for alpha 2 and alpha 5 chains of type IV collagen on skin biopsies: ... Test Code ALPRT Alport (Collagen IV Alpha 5 and Alpha 2) Immunofluorescent Stain, Renal Shipping Instructions. 1. Advise ... 3) Because alpha 3 and alpha 4 chains of type IV collagen are not expressed in the epidermal basement membranes, patients with ...
As collagen turnover is relatively slow at adult age, the process of function adaptation of the ECM at young age maybe of great ... From collagen to tenocyte : How the equine superficial digital flexor tendon responds to physiologic challenges and physical ... From collagen to tenocyte : How the equine superficial digital flexor tendon responds to physiologic challenges and physical ... Author keywords: equine superficial digital flexor tendon, extracellular matrix, collagen, tenocyte, electrical therapy, shock ...
Women produce less collagen than men, and this collagen is lost at a rate of about 1% per year. This means that a woman has ... Poor collagen levels also affect the bones, and this picture (left) shows how collagen loss affects facial shape in extreme age ... Collagen is a natural protein component of the skin that acts like a scaffold and the main building block for cells, tissues ... About a third of the protein content in your body is made up of collagen, which is found in the bones, muscles, and tissues of ...
Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C- ... Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV ... Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the ... Serum Collagen IV concentrations correlate with hepatic tissue levels of collagen IV in subjects with alcoholic liver disease ...
A group of proteins that form elongated fibers that are the main component in connective tissues such as skin, ligaments, tendons, cartilage and bone ...
The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath ... Collagen, type VII, alpha 1 has been shown to interact with Laminin 5 and Fibronectin. Collagen GRCh38: Ensembl release 89: ... Type VII collagen is also found in the retina; its function in this organ is unknown. COL7A1 is located on the short arm of ... Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene. This gene encodes the alpha chain of ...
Collagen Microfibril Structure. The molecular model of bovine type I collagen microfibril, is contained in (MCF2021.txt), a ... Brown, E.M. Development and utilization of a bovine type I collagen microfibril model. International Journal of Biological ...
Collagen contains specific amino acids - Glycine, Proline, Hydroxyproline and Arginine. ... Collagen is a protein made up of amino-acids, which are in turn built of carbon, oxygen and hydrogen. ... Collagen is even the major component of the hair and nails.. Aging and collagen. With age, collagen production slows and the ... An atomic-force-microscopy image of collagen fibrils in a collagen fiber. Image Credit: UChicago Argonne LLC ...
Type V collagen and type XI collagen are minor components of tissue and occur as fibrils with type I and type II collagen ... Types of collagen More than 20 genetically distinct collagens exist in animal tissues. Collagen types I, II, III, V and XI self ... Type II collagen is found in cartilage, developing cornea and vitreous humour. These are formed from two or more collagens or ... Collagen fibrils Different collagen types form larger fibrillar bundles with the help of several different classes of proteins ...
Collagen is a simple protein. It is composed of 3 long chains wound together in a tight triple helix. Each chain is 1400 amino ... For example collagen in tendons transmits tension). Collagen is integral to wound healing and blood clotting. As a Treatment: ... Collagen stregthens tendons, skin and the membranes that hold the internal organs in place. Collagen mixed with mineral ... Collagen Induced Arthritis: Collagen (type II, bovine) is used to induce arthritis in animal studies. These studies are ...
Protecting Current Collagen Levels and Preventing Future Collagen Degradation. The best way to maintain a healthy, youthful ... Collagen: The Skin Structural Protein. Collagen is a major structural protein in the skin. It plays a key role in providing the ... What Is Collagen?. Collagen is the bodys major structural protein composed of three protein chains wound together in a tight ... Collagen and Beauty. Collagen makes up 75 percent of our skin; thus, the smooth, plump appearance of young, healthy skin is due ...
I am looking for an antibody specific for human collagen 1 and/or collagen 3 for measuring collagen contents in supernatants of ... collagen. coco coco at nki.nl Tue Jul 4 17:40:58 EST 1995 *Previous message: gp-120 participant has questions... ... Does anybody knows these kind of antibodies or such an ELISA system for collagen. *Previous message: gp-120 participant has ...
People who developed these disorders were previously said to have "connective tissue" or "collagen vascular" disease. We now ...
Collagen is an important protein in your skin and connective tissues. Among its many functions, it is responsible for giving ... Loss of collagen is a cause of wrinkles. While... ... Consider a fish collagen supplement. Collagen from fish can be ... Take a daily collagen supplement. Collagen supplements may help boost collagen in your body. You can opt for a supplement that ... Explore this Article Increasing Collagen through Diet Boosting Collagen through Supplements Boosting Collagen with Skincare ...
... today announced its plan to commercialize a minimally manipulated amniotic collagen matrix. The Company has filed its third ... today announced its plan to commercialize a minimally manipulated amniotic collagen matrix. The Company has filed its third ... patent application related to its non-oxidative drying technology that was designed to preserve the bioavailability of collagen ...
Nya Collagen Plus - nu med nypon. Pressmeddelanden • Maj 19, 2016 09:39 CEST Den mycket populära Collagen plus har nu fått ännu ...
Collagen, and to a lesser extent, elastin, were among... ... Collagen Molecule Lysyl Oxidase Byssal Thread Bovine Articular ... Tanzer, M. L., and Waite, J. H., 1982, Collagen cross-linking, Collagen Rel. Res., 2:177.Google Scholar ... Siegel, R. C., 1976, Collagen cross-linking. Synthesis of collagen cross-links in vitro with highly purified lysyl oxidase, J. ... Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen, Proc. Natl. Acad ...
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Collagen V. Collagen V. Collagen V is found in placenta, amnion, chorion, and cornea. Modulate the proliferative response of ... Collagen I. Collagen I. Use Corning Collagen I surface to culture endothelial cells, hepatocytes, muscle cells, breast ... Collagen III. Collagen III. Enhance the research of collagen fibrillogenesis in normal cardiovascular development with Corning ... Collagen VI. Collagen VI. Enhance the success of specialized tasks in tissue organization and cell functionality through the ...
Green Foods , Vibrant Collagens, Coconut Milk Collagen Creamer, Plain, 3.38 oz (96 g). ... Green Foods , Vibrant Collagens, Energizing Collagen Matcha, Original, 2.47 oz (70 g). ... LifeTime Vitamins, Liquid Collagen Plus Vitamin C, Berry Flavor, 5,000 mg, 16 fl oz (473 ml). ... Mercola, Organic Collagen Powder From Grass Fed Beef Bone Broth, Chocolate, 14.81 oz (420 g). ...
  • As collagen turnover is relatively slow at adult age, the process of function adaptation of the ECM at young age maybe of great importance for the development of resistance to injury. (uu.nl)
  • Collagen contains specific amino acids - Glycine, Proline, Hydroxyproline and Arginine. (news-medical.net)
  • By adding small groups of amino acids known as peptide sequences to the surface of the scaffold at different points, the way in which the collagen interacts with the growing cells changes, altering the potential uses for the scaffold. (cam.ac.uk)
  • The supplements specifically contain high amounts of three amino acids that are key building blocks for collagen synthesis in the body: glycine, proline and hydroxyproline. (cnn.com)
  • A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of the collagen subunits. (newworldencyclopedia.org)
  • Collagen consists of amino acids wound together to form triple- helices to form of elongated fibrils . (wikipedia.org)
  • Other sources claim that bone broth is unlikely to provide sufficient amounts of amino acids and other collagen precursors and that it may be inferior to supplements. (livestrong.com)
  • When this process is negatively affected by genetic defects or the lack of adequate dietary intake of natural amino acids, collagen deficiencies can arise. (wisegeek.com)
  • Collagen is converted to gelatin by boiling water which hydrolyzes it to a mixture of degradation products.The nutritional value of gelatin is questionable, as it does not contain all the essential amino acids in the proper proportions that the body needs. (happi.com)
  • There are 13 types of collagen, based on their formation. (everything2.com)
  • There are at least 27 types of collagen (Zhao 2006). (newworldencyclopedia.org)
  • There is some covalent crosslinking within the triple helices, and a variable amount of covalent crosslinking between tropocollagen helices, to form the different types of collagen found in different mature tissues. (newworldencyclopedia.org)
  • However, it's best to know the realities of collagen's effects before you spend money on collagen treatments--and about the risks you might take in using certain types of collagen supplements. (ehow.co.uk)
  • So far, 28 types of collagen have been identified and described. (wikipedia.org)
  • Some types of collagen fibrils, gram-for-gram, are stronger than steel. (medicalnewstoday.com)
  • There are at least 16 different types of collagen, but 80 to 90 percent of them belong to types 1, 2, and 3. (medicalnewstoday.com)
  • There are many types of collagen and collagen products available on the market. (howstuffworks.com)
  • Over 90% of the collagen in the human body, however, is type I. So far, 28 types of collagen have been identified and described. (wikipedia.org)
  • This is called staggering and in the fibrillar collagens, the molecules are staggered from each other by about 67 nm (a unit that is referred to as 'D' and changes depending upon the hydration state of the aggregate). (news-medical.net)
  • When the receptors are bound by the correct combination of signal molecules (called fibroblast growth factors, or FGFs), the fibroblast begins the production of collagen. (nuskin.com)
  • Preparation contains native collagen molecules with a small amount of nicked or shortened sequences due to pepsin treatment. (corning.com)
  • Disclosed is an artificial membrane comprising a product made by cross-linking molecules of interpenetrating denatured collagen coupled at their lysine epsilon amino groups with a coupler through carbonyl groups, sulfonyl groups, or combination thereof on the coupler wherein non-coupled lysine epsilon. (google.com)
  • Disclosed is an artificial membrane comprising a product made by cross-linking molecules of interpenetrating denatured collagen coupled at their lysine epsilon amino groups with a coupler through carbonyl groups, sulfonyl groups, or combination thereof on the coupler wherein non-coupled lysine epsilon amino groups are bonded to a modifier wherein the modifier is a carbonyl sulfonyl, carbamoyl, or β-malic acid group. (google.com)
  • 13. An artificial membrane comprising a product made by cross-linking molecules of interpenetrating denatured collagen coupled at their lysine epsilon amino groups with a coupler through carbonyl groups, sulfonyl groups, or combination thereof on the coupler. (google.com)
  • It is designed with Tri- Collagen Complex, a unique formulation of three collagen molecules working in synergy to penetrate the deeper layers of the skin. (thefreedictionary.com)
  • Cosmetic lotions that claim to increase collagen levels are unlikely to do so, as collagen molecules are too large to be absorbed through the skin. (medicalnewstoday.com)
  • If you want to attach these molecules to collagen, you don't have to cook it or use harsh chemicals. (newswise.com)
  • Collagen molecules are too large to permeate the skin, so any cream applied to the face containing collagen is of limited effectiveness. (reference.com)
  • What is meant by staggered ends in collagen molecules? (madsci.org)
  • Covalent cross-links hold many collagen molecules side by side, forming fibres.The ends of the parallel molecules are staggered.If they were not, there would be a weak spot running right across the collagen fibre.What is the meaning of staggered ends here? (madsci.org)
  • Miniature scaffolds made from collagen - the 'glue' that holds our bodies together - are being used to heal damaged joints, and could be used to develop new cancer therapies or help repair the heart after a heart attack. (cam.ac.uk)
  • Some disorders classified as collagen vascular disease affect your joints, skin, blood vessels, or other vital organs. (healthline.com)
  • If you have a collagen vascular disease, your immune system causes inflammation in your collagen and nearby joints. (healthline.com)
  • Collagen can take years off your face, keep your joints strong and improve overall health. (livestrong.com)
  • Scientists say that the collagen in bone broth is poorly absorbed in the body and, therefore, doesn't reach your skin and joints. (livestrong.com)
  • I have been taking the Vital collagen for a few months, and my joints feel better, and I've also noticed great differences in my hair, skin, and nails. (gnc.com)
  • This disruption leads to a variety of disorders such as scurvy-a disease where the body cannot produce collagen and, as a result, essentially falls apart as these support structures (collagen) deteriorate. (nuskin.com)
  • Vascular endothelial growth factor (VEGF) was loaded on mesoporous silica nanoparticle (MSN), which was then incorporated within a type I collagen sponge, to produce collagen/MSN/VEGF (CMV) scaffold. (mendeley.com)
  • BioCell Collagen might increase levels of collagen in the skin. (webmd.com)
  • Even though your body may not produce the same levels of collagen as it once did, stimulating your collagen production has the potential to reverse some signs of aging. (howstuffworks.com)
  • Soy consumption can increase in the amount of collagen in your skin. (wikihow.com)
  • Hence, it is crucial that we consume the right amount of collagen to maintain younger-looking skin while delaying the aging process. (hubpages.com)
  • So you end up with a compromise - long enough to get a good amount of collagen but short enough to keep the flavor intact. (cheftalk.com)
  • The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. (wikipedia.org)
  • Collagen fibers provide your muscles with the strength and structure needed to move and function throughout the day. (livestrong.com)
  • Collagen fibers not only make up your skeletal muscle fibers, but they also make up your smooth muscles (such as those in the bladder and reproductive system) and your cardiac (heart) muscles. (livestrong.com)
  • Rice University researchers have delivered a scientific one-two punch with a pair of papers that detail how synthetic collagen fibers self-assemble via their sticky ends. (eurekalert.org)
  • The collagen fibers of the invention and hemostatic fabrics formed thereof optionally include hemostatic agents and/or other therapeutic agents, to further promote hemostasis and wound healing. (google.es)
  • 2. A sterile surgical collagen product having a felt- or fleece-like structure with open, communicating voids between the fibers, as obtained by the method according to claim 1. (google.com.au)
  • Collagen is injected via a tiny needle just below the skin's surface to help fill up areas that are depressed or, in the case of lips, too thin. (bellaonline.com)
  • Despite what packages may say, creams containing collagen work on the skin's surface only and cannot reverse the effects of collagen loss, which occurs deep in the skin's layers. (howstuffworks.com)
  • I am looking for an antibody specific for human collagen 1 and/or collagen 3 for measuring collagen contents in supernatants of fibroblast cultures with an ELISA. (bio.net)
  • CosmoDerm and CosmoPlast are bioengineered human collagen products that are used for similar indications as Zyderm and Zyplast but have the advantage of not requiring a skin test prior to the first treatment. (medicinenet.com)
  • Most medical collagen is derived from cattle or pigs, but more expensive human collagen is available from cadavers, placentas and aborted fetuses. (happi.com)
  • Both bovine and human collagen products are biodegradable and temporary. (howstuffworks.com)
  • Collagen creams will probably do the most harm to your wallet, not your face. (ehow.co.uk)
  • Skin care therapist Julia March also recommends both eating your collagen and using creams. (huffingtonpost.com)
  • From collagen supplements and anti-aging creams to hair masks and shampoos, there are thousands of options available. (livestrong.com)
  • Read on to find out about collagen boosting creams. (howstuffworks.com)
  • The body naturally produces the collagen that it needs, but this production is gradually disrupted as part of the natural ageing process. (google.com)
  • This means that a woman has naturally lost almost half of the collagen from her skin by the age of 50. (google.com)
  • Reserveage Nutrition's Plant-Based Support Collagen Builder features naturally derived silica from bamboo and natural vitamin C from Indian Gooseberries (Amia extract) to deliver co-nutrients for collagen production. (thefreedictionary.com)
  • Because it is non-toxic, dissolves naturally over time and rarely triggers rejection, collagen is commonly used in cosmetics, drug delivery systems and biocompatible coatings. (newswise.com)
  • Hair and nails also naturally contain large amounts of collagen. (wisegeek.com)
  • Various skin care products are promoted in the market, but the most effective way to protect and enhance the beauty of the skin and hair is to eat a nutritionally balanced and wholesome diet that includes foods that can boost your collagen naturally. (medindia.net)
  • In the face of these supplements not having the desired effect, skincare expert Cherry Woods says our best option is to coax our skin into producing collagen naturally . (netdoctor.co.uk)
  • As with most essential elements though, natural sources are always best, and it is preferable to boost collagen production through increased amino acid intake in the diet. (wisegeek.com)
  • Skincare products containing antioxidants and collagen-boosting components may increase collagen in your skin, but more research is needed. (wikihow.com)
  • Drawing on natural resources, whilst working with the latest technology, Elemis strive to create the latest innovations in skincare from their Pro Collagen Collection and Tri-Enzyme range. (asos.com)
  • Packed together as bundles, fibrous bands of collagen serve as the main support system of the dermis, the deepest layer of skin. (newbeauty.com)
  • Collagen is further packed into fibrillar collagen types with hexagional or quasi hexagonal shapes. (news-medical.net)
  • Ultimately, I show that this single amino acid guides the assembly of the C-propeptides of all the fibrillar collagens. (mit.edu)
  • The physical characteristics are nearly identical to our existing Collagen Peptide Powder and the Grass-Fed version is only a little over 10% more in price. (constantcontact.com)
  • As an added bonus, we will be happy to update your current Collagen Peptide Powder label to the new Grass-Fed at no charge! (constantcontact.com)
  • Please note that Vitalabs will no longer be stocking our regular Collagen Peptide Powder due to the ever increasing demand and popularity of the Grass-Fed Collagen. (constantcontact.com)
  • A further commercially available collagen product consists of a light flocculent powder which, though haemostatically active, is difficult to apply in depth into a wound and which has the disadvantage of being washed away by strong diffuse bleedings. (google.com.au)
  • Increased glomerular and mesangial deposition of collagen IV occurs in diabetic nephropathy and increased urinary levels are associated with the extent of renal injury. (wikipedia.org)
  • Type III collagen is found in the walls of arteries and other hollow organs and usually occurs in the same fibril with type I collagen. (news-medical.net)
  • Collagen occurs in many places throughout the body. (wikipedia.org)
  • Gradual calcium deposition within collagen occurs as a natural function of aging. (wikipedia.org)
  • Epidermolysis bullosa acquisita involves an autoimmune reaction to this form of collagen. (wikipedia.org)
  • Your blood vessels or the lining of your heart may become inflamed if you have this form of collagen vascular disease. (healthline.com)
  • Temporal arteritis, or giant cell arteritis, is another form of collagen vascular disease. (healthline.com)
  • However, if you don't have joint problems, you might want to opt for collagen hydrolysate or collagen peptide supplements instead. (howstuffworks.com)
  • Several small studies suggest collagen hydrolysate may reduce pain associated with osteoarthritis. (consumerlab.com)
  • This was also the first time I had heard "collagen" referenced in the health world without any reference to needles or fillers - in fact, there were more stats thrown around about athletes and runners. (popsugar.com)
  • Below you will find a detailed explanation of how collagen works, followed by a list of other injectable fillers your doctor may recommend. (medicinenet.com)
  • It seems like she's had that problem fixed with a little facelift, facial fillers, and lip collagen. (awfulplasticsurgery.com)
  • Collagen helps to give strength to various structures of the body and also protects structures like the skin by preventing absorption and spreading of pathogenic substances, environmental toxins, micro - organisms and cancerous cells. (news-medical.net)
  • The collagen (derived from cow hide ) is injected just beneath the skin where the body accepts it as its own, and allows it to fill the wrinkle or heal the scar. (everything2.com)
  • Without collagen your body cannot repair itself normally, so tooth loss and bruising (among many other things) occur. (everything2.com)
  • If it weren't for collagen, the body would literally fall apart. (nuskin.com)
  • Certain nutrients can help your body to produce more collagen, so make sure that you are including a good balance of vitamins and minerals. (wikihow.com)
  • Consuming these foods can help your body optimize its collagen production. (wikihow.com)
  • It is important that your skin and body remain hydrated if you are trying to increase your collagen production. (wikihow.com)
  • Eat plenty of foods rich in vitamin C. Vitamin C is important for collagen production in the body. (wikihow.com)
  • Collagen supplements may help boost collagen in your body. (wikihow.com)
  • Collagen from fish can be quickly absorbed by the body. (wikihow.com)
  • These supplements are made from egg shell membranes and can help your body build collagen. (wikihow.com)
  • Our body continuously makes new collagen, but the process begins to slow down after about age 30. (cnn.com)
  • Although collagen is the best known filler, there are many other substances doctors can use to plump up your skin, including fat from your own body and synthetic materials. (medicinenet.com)
  • Zyderm and Zyplast collagen are placed just beneath the skin, in the dermis where the body readily accepts it as its own. (medicinenet.com)
  • Autologen is an injection of your own collagen, extracted from another place on your body. (medicinenet.com)
  • Collagen provides these body structures with the ability to withstand forces that stretch or lengthen them. (thefreedictionary.com)
  • Collagen functions several different ways in your body. (livestrong.com)
  • Collagen makes up the walls of the veins, arteries and capillaries of the body. (livestrong.com)
  • Collagen is a building block of the body. (ehow.co.uk)
  • In this thesis, I report a series of studies targeted at elucidating mechanisms of proteostasis for collagen type-1, the most abundant collagen in the human body. (mit.edu)
  • Endogenous collagen is natural collagen, synthesized by the body. (medicalnewstoday.com)
  • The collagens in the human body are strong and flexible. (medicalnewstoday.com)
  • Some collagens act as protective coverings for delicate organs in the body, such as the kidneys. (medicalnewstoday.com)
  • With this process," Yu said, "we can make the collagen that's already found in the human body behave in new ways, including some ways that are not found in nature. (newswise.com)
  • Because the collagen solution contains water it is quickly absorbed into the body. (bellaonline.com)
  • Needless to say, if you want to preserve and conserve the wellspring of youth in your body, you're going to need to utilize a combo of goodies that contain collagen and products that boost its production to keep you looking and feeling youthful. (usmagazine.com)
  • When combined with strength training, collagen supplements may increase muscle strength and improve body composition. (livestrong.com)
  • Super Collagen contains clinically studied BioActive NeoCell Collagen which supports healthy collagen formation throughout the body. (ebay.ca)
  • Find out more about collagen and its role in the body. (medicalnewstoday.com)
  • Research from the Indian Dermatology Online Journal suggests that vitamin C also plays an important role in protecting the skin and creating more collagen in the body. (medicalnewstoday.com)
  • We hypothesized that taking dietary supplements such as resveratrol and collagen could enhance skin and body satisfaction. (prweb.com)
  • Lower doses are not enough to show a significant improvement in the skin texture, while consumption over 5000mg collagen is excess collagen and will be drained from the body. (hubpages.com)
  • Eviva Collagen Elixir is a new beverage that is being touted for the many benefits it can offer the body, inside and out. (trendhunter.com)
  • However, as we age, the production of collagen levels in our body decreases. (advocare.com)
  • Synthetic collagen will remain in the body for a longer period than biodegradable collagen. (howstuffworks.com)
  • The longer you simmer the more collagen (body) you get but the flavor gets muddied. (cheftalk.com)
  • The hair and scalp serum is formulated with a unique, hair-plumping delivery system that effectively penetrates the scalp's epidermis with Type 1 collagen (the most abundant collagen in the human body) and a proprietary blend. (newbeauty.com)
  • Collagen also provides important function in your blood vessels. (livestrong.com)
  • The ganglion cell axons (red), astrocytes (green), and blood vessels (blue) are labeled using SMI-32, GFAP, and Collagen IV antibodies respectively. (utah.edu)
  • Anti- GFP (green) and anti- Collagen IV (blue) which were used to determine numbers of astrocytes and relative locations in relation to blood vessels. (utah.edu)
  • With age, collagen production slows and the cells structures weaken. (news-medical.net)
  • With age, collagen levels drop off due to a decrease in production and an increase in degradation. (nuskin.com)
  • Cruciferous vegetables contain sulfur, which is important for collagen production. (wikihow.com)
  • Isoflavone-rich soy products can increase your collagen production. (wikihow.com)
  • Staying hydrated will support collagen production. (wikihow.com)
  • Collagen production declines with age and exposure to factors such as smoking and UV light. (medicalnewstoday.com)
  • By the age of 60 years, a considerable decline in collagen production is normal. (medicalnewstoday.com)
  • The beauty benefits of avocado oil are increased collagen production, improved skin moisturization and better scalp health. (reference.com)
  • In general, eating lots of veggies and a variety of fruits will enhance collagen production," Petrucci says. (huffingtonpost.com)
  • Shop these nine products to elevate your collagen production and boost your beauty. (usmagazine.com)
  • An interesting study observed that daily intake of tomatoes increases the production of procollagen, the soluble precursor of collagen. (medindia.net)
  • A deficiency of vitamin C is linked to poor production of collagen, which leads to fragile skin, brittle nails and corkscrew hair. (medindia.net)
  • Rona- Care ASC III is said to be an effective amplifier of collagen III production because it sends cytokines to enhance fibroblast activity. (happi.com)
  • The breakthrough product not only claims to restore collagen, but also boost its production in your scalp and give your hair it's healthy, natural sheen back. (newbeauty.com)
  • Consistent use of the product not only replenishes lost collagen (after the age of 25, your body's ability to reproduce collagen is diminished), but boosts future collage production, making it an ideal product for all age groups and all hair types," says Teeluck. (newbeauty.com)
  • We think some of the duration from Restylane is due to this new collagen production,' Wang says. (scientificamerican.com)
  • We thought we could do this,' Wang says, 'but we were surprised at the robust level of production of collagen. (scientificamerican.com)
  • The strength at 6X supports the physiological functions of collagen, as the homeopathic biological substrate acts as supporter of the endogenous production of collagen. (drugs.com)
  • However, collagen production decreases with age, which causes weaker connections. (netdoctor.co.uk)
  • However, according to the October 2008 issue of Archives of Dermatological Research , it was said that consuming collagen may increase the body's overall production of collagen, thus promoting skin health. (netdoctor.co.uk)
  • Reduce sugar intake diet to limit the glycation process and step up your Vitamin C intake, which will assist in stimulating collagen production. (netdoctor.co.uk)
  • Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. (wikipedia.org)
  • Several recent studies suggest that disturbances of the collagen texture and the extracellular matrix (ECM) metabolism are major factors leading to the onset of diverticular disease. (springer.com)
  • Fish type I collagen is an effective material as a biodegradable scaffold or spacer replicating the natural extracellular matrix, which serves to spatially organize cells, providing them with environmental signals and directing site-specific cellular regulation. (hindawi.com)
  • Collagen VI is an important component of the extracellular matrix which forms a microfibrillar network that is found in close association with the cell and surrounding basement membrane. (nih.gov)
  • A regular intake of this fruit or its oil increases the content of soluble collagen in the skin. (medindia.net)
  • Bone broth liquids and powders derived from beef or chicken can also be a good source of collagen, though there isn't much evidence of skin or joint benefits, according to Dr. Patricia Farris, a dermatologist and fellow of the American Academy of Dermatology. (cnn.com)
  • Are Collagen and Bone Broth The Keys to Youthful Skin? (huffingtonpost.com)
  • But bone broth and collagen supplements are more effective, because they strengthen your skin from the inside. (huffingtonpost.com)
  • There are plenty of foods and herbs rich in collagen, from egg whites and bone broth to spirulina. (livestrong.com)
  • Bone broth has emerged as one of the best natural sources of collagen. (livestrong.com)
  • Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina . (wikipedia.org)
  • Where is collagen found? (news-medical.net)
  • The reason for this is because the collagen found in these products is not geared to be absorbed by the skin, and instead remains on the s. (articlealley.com)
  • Because collagen is a type of material found in our bodies, it readily binds with cellular components to promote optimum healing, creating a latticework for cells to grow on. (webwire.com)
  • In addition, collagen XVII has been found to be present in the central nervous system, thus offering an explanation for the statistical association between bullous pemphigoid, in which autoimmunity is directed against dermal collagen XVII, and neurological diseases. (hindawi.com)
  • Several forms of commercially-produced liquid collagen are found in beauty products and nutritional supplements. (wisegeek.com)
  • I've found collagen C pomegranate liquid in a local health store, and I agree that some kind of flavoring is going to be essential. (wisegeek.com)
  • A branded form of undenatured type II collagen, UC-II , has been found to improve knee stiffness and/or pain. (consumerlab.com)
  • Understanding the structure and function of collagen will help you better know how to maintain a healthy, youthful appearance. (nuskin.com)
  • The best way to maintain a healthy, youthful looking appearance is to protect the healthy collagen you currently have and to prevent future collagen degradation. (nuskin.com)
  • Collagen Peptide is easily absorbed to maintain youthful skin for longer. (ebay.ca)
  • Collagen cream is thought to be a good way to improve and keep your youthful appearance. (hubpages.com)
  • Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix . (wikipedia.org)
  • Peptide-binding assays indicate that the binding is primarily driven by stereo-selective triple-helical hybridization between monomeric CMPs of high triple-helical propensity and denatured collagen strands. (pnas.org)
  • In 2016, edible collagen has been the darling of beauty editors, its benefits touted in publications from Allure to Vogue. (spafinder.com)
  • Hsp47 transiently associates with procollagen and is involved in collagen processing and/or secretion under normal conditions. (nih.gov)