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).
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.
A family of structurally related collagens that form the characteristic collagen fibril bundles seen in CONNECTIVE TISSUE.
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.
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.
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.
A fibrillar collagen found predominantly in CARTILAGE and vitreous humor. It consists of three identical alpha1(II) chains.
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.
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.
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)
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.
A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.
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.
A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.
A fibrillar collagen found primarily in interstitial CARTILAGE. Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens.
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.
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 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.
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.
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.
A non-fibrillar collagen found primarily in terminally differentiated hypertrophic CHONDROCYTES. It is a homotrimer of three identical alpha1(X) subunits.
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).
The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
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.
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.
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.
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.
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.
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.
Tissue that supports and binds other tissues. It consists of CONNECTIVE TISSUE CELLS embedded in a large amount of EXTRACELLULAR MATRIX.
Glycoproteins which have a very high polysaccharide content.
Enzymes that catalyze the degradation of collagen by acting on the peptide bonds.
Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.
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.
A family of structurally-related short-chain collagens that do not form large fibril bundles.
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.
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.
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 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.
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 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.
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.
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.
Reagent used as an intermediate in the manufacture of beta-alanine and pantothenic acid.
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.
Adherence of cells to surfaces or to other cells.
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.
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 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.
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.
Polymorphic cells that form cartilage.
Restoration of integrity to traumatized tissue.
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 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.
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.
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 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.
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.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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)
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.
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.
Basic glycoprotein members of the SERPIN SUPERFAMILY that function as COLLAGEN-specific MOLECULAR CHAPERONES in the ENDOPLASMIC RETICULUM.
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.
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)
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.
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.
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.
The lamellated connective tissue constituting the thickest layer of the cornea between the Bowman and Descemet membranes.
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.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The process whereby PLATELETS adhere to something other than platelets, e.g., COLLAGEN; BASEMENT MEMBRANE; MICROFIBRILS; or other "foreign" surfaces.
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 in which a polyacrylamide gel is used as the diffusion medium.
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 (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.
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.
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.
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.
A family of zinc-dependent metalloendopeptidases that is involved in the degradation of EXTRACELLULAR MATRIX components.
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.
Elements of limited time intervals, contributing to particular results or situations.
A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain.
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.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
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.
An integrin alpha subunit that binds COLLAGEN and LAMININ though its I domain. It combines with INTEGRIN BETA1 to form the heterodimer INTEGRIN ALPHA1BETA1.
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.
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.
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.
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.
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.
The area between the EPIPHYSIS and the DIAPHYSIS within which bone growth occurs.
Methods for maintaining or growing CELLS in vitro.
Process by which organic tissue becomes hardened by the physiologic deposit of calcium salts.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
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.
Established cell cultures that have the potential to propagate indefinitely.
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.
The properties, processes, and behavior of biological systems under the action of mechanical forces.
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.
Connective tissue comprised chiefly of elastic fibers. Elastic fibers have two components: ELASTIN and MICROFIBRILS.
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.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
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.
Proteins prepared by recombinant DNA technology.
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.
Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.
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.
Synthetic or natural materials, other than DRUGS, that are used to replace or repair any body TISSUES or bodily function.
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)
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.
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.
A member of the MATRIX METALLOPROTEINASES that cleaves triple-helical COLLAGEN types I, II, and III.
Surface glycoproteins on platelets which have a key role in hemostasis and thrombosis such as platelet adhesion and aggregation. Many of these are receptors.
A class of enzymes that catalyzes the degradation of gelatin by acting on the peptide bonds. EC 3.4.24.-.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
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.
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.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
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.
Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.
The rate dynamics in chemical or physical systems.
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.
Components of the extracellular matrix consisting primarily of fibrillin. They are essential for the integrity of elastic fibers.
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).
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.
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.
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.
The process of bone formation. Histogenesis of bone including ossification.
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.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
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.
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.
Extracellular substance of bone tissue consisting of COLLAGEN fibers, ground substance, and inorganic crystalline minerals and salts.
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)
An endopeptidase that is structurally similar to MATRIX METALLOPROTEINASE 2. It degrades GELATIN types I and V; COLLAGEN TYPE IV; and COLLAGEN TYPE V.
Shiny, flexible bands of fibrous tissue connecting together articular extremities of bones. They are pliant, tough, and inextensile.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
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.
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.
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.
Bone-forming cells which secrete an EXTRACELLULAR MATRIX. HYDROXYAPATITE crystals are then deposited into the matrix to form bone.
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.
Resistance and recovery from distortion of shape.
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.
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.
A group of cells that includes FIBROBLASTS, cartilage cells, ADIPOCYTES, smooth muscle cells, and bone cells.
The fibrous tissue that replaces normal tissue during the process of WOUND HEALING.
Angiostatic proteins that are formed from proteolytic cleavage of COLLAGEN TYPE XVIII.
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.
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.
Proteoglycans consisting of proteins linked to one or more CHONDROITIN SULFATE-containing oligosaccharide chains.
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).
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.
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.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
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)
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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).
A fibrous cord that connects the muscles in the back of the calf to the HEEL BONE.
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.
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.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
The relationship between the dose of an administered drug and the response of the organism to the drug.
The sum of the weight of all the atoms in a molecule.
Experimentally induced chronic injuries to the parenchymal cells in the liver to achieve a model for LIVER CIRRHOSIS.
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.
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.
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.
One or more layers of EPITHELIAL CELLS, supported by the basal lamina, which covers the inner or outer surfaces of the body.
Perisinusoidal cells of the liver, located in the space of Disse between HEPATOCYTES and sinusoidal endothelial cells.
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.
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.
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).
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Antibodies produced by a single clone of cells.
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.
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.
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)
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.
The main trunk of the systemic arteries.
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.
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.
The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.
Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)
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.
Peptides composed of between two and twelve amino acids.
Endogenous tissue constituents that have the ability to interact with AUTOANTIBODIES and cause an immune response.
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 complex of related glycopeptide antibiotics from Streptomyces verticillus consisting of bleomycin A2 and B2. It inhibits DNA metabolism and is used as an antineoplastic, especially for solid tumors.

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)

There are many different types of collagen diseases, each with its own set of symptoms and characteristics. Some common examples include:

* Osteogenesis imperfecta (OI): A genetic disorder that affects the development of bones and connective tissue, leading to fragile bones, joint deformities, and other complications.
* Ehlers-Danlos syndrome (EDS): A group of genetic disorders that affect the production and structure of collagen, leading to loose joints, bruising, and other symptoms.
* Marfan syndrome: A genetic disorder that affects the body's connective tissue, particularly the heart, blood vessels, and joints. It can cause tall stature, long limbs, and cardiovascular problems.
* Cutis laxa: A rare genetic disorder that affects the production of collagen in the skin, leading to loose, wrinkled skin and other complications.
* Pseudoxanthoma elasticum (PXE): A genetic disorder that affects the elastic tissue in the skin, leading to mineral deposits and changes in the skin's texture and color.

Collagen diseases can be caused by a variety of factors, including genetics, environmental exposures, and autoimmune disorders. Treatment for these conditions can vary depending on the specific type and severity of the disease, but may include medication, physical therapy, and surgery.

Fibrosis can occur in response to a variety of stimuli, including inflammation, infection, injury, or chronic stress. It is a natural healing process that helps to restore tissue function and structure after damage or trauma. However, excessive fibrosis can lead to the loss of tissue function and organ dysfunction.

There are many different types of fibrosis, including:

* Cardiac fibrosis: the accumulation of scar tissue in the heart muscle or walls, leading to decreased heart function and potentially life-threatening complications.
* Pulmonary fibrosis: the accumulation of scar tissue in the lungs, leading to decreased lung function and difficulty breathing.
* Hepatic fibrosis: the accumulation of scar tissue in the liver, leading to decreased liver function and potentially life-threatening complications.
* Neurofibromatosis: a genetic disorder characterized by the growth of benign tumors (neurofibromas) made up of fibrous connective tissue.
* Desmoid tumors: rare, slow-growing tumors that are made up of fibrous connective tissue and can occur in various parts of the body.

Fibrosis can be diagnosed through a variety of methods, including:

* Biopsy: the removal of a small sample of tissue for examination under a microscope.
* Imaging tests: such as X-rays, CT scans, or MRI scans to visualize the accumulation of scar tissue.
* Blood tests: to assess liver function or detect specific proteins or enzymes that are elevated in response to fibrosis.

There is currently no cure for fibrosis, but various treatments can help manage the symptoms and slow the progression of the condition. These may include:

* Medications: such as corticosteroids, immunosuppressants, or chemotherapy to reduce inflammation and slow down the growth of scar tissue.
* Lifestyle modifications: such as quitting smoking, exercising regularly, and maintaining a healthy diet to improve overall health and reduce the progression of fibrosis.
* Surgery: in some cases, surgical removal of the affected tissue or organ may be necessary.

It is important to note that fibrosis can progress over time, leading to further scarring and potentially life-threatening complications. Regular monitoring and follow-up with a healthcare professional are crucial to managing the condition and detecting any changes or progression early on.

1. Bone fractures: The most common symptom of OI is an increased risk of fractures, which can occur with minimal trauma or even without any apparent cause.
2. Dental problems: People with OI may have poorly formed teeth, tooth decay, and gum disease.
3. Short stature: Many individuals with OI are short in stature, due to the effects of chronic fractures and pain on growth and development.
4. Muscle weakness: Some people with OI may experience muscle weakness, particularly in the limbs.
5. Joint problems: OI can cause issues with joint mobility and stability, leading to arthritis and other degenerative conditions.
6. Scoliosis: Curvature of the spine is common in people with OI, which can lead to back pain and respiratory problems.
7. Blue sclerae: A distinctive feature of OI is the presence of blue-colored sclerae (the white part of the eye).
8. Other symptoms: Some people with OI may experience hearing loss, vision problems, and delayed development.

There are several types of OI, each caused by a mutation in a specific gene. The most common forms of OI are type I, type II, and type III. Type I is the mildest form and type III is the most severe. There is no cure for OI, but treatment focuses on managing symptoms and preventing complications. This may include:

1. Bracing and orthotics: To support weakened bones and improve posture.
2. Physical therapy: To maintain muscle strength and flexibility.
3. Pain management: To reduce the risk of chronic pain and improve quality of life.
4. Dental care: Regular dental check-ups and appropriate treatment to prevent tooth decay and gum disease.
5. Respiratory care: To manage breathing problems and prevent respiratory infections.
6. Monitoring for hearing loss: Regular hearing tests to detect any hearing loss and provide appropriate intervention.
7. Early intervention: To help children with OI develop skills and abilities to their full potential.
8. Genetic counseling: For families with a history of OI, to understand the risks and implications for future pregnancies.

It's important for people with OI to work closely with their healthcare provider to manage their condition and prevent complications. With proper care and support, many people with OI can lead active and fulfilling lives.

1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.

2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.

3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.

4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.

5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.

6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.

7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.

8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.

9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.

10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.

There are several types of pulmonary fibrosis, including:

1. Idiopathic pulmonary fibrosis (IPF): This is the most common and severe form of the disease, with no known cause or risk factors. It is characterized by a rapid decline in lung function and poor prognosis.
2. Connective tissue disease-associated pulmonary fibrosis: This type is associated with conditions such as rheumatoid arthritis, systemic lupus erythematosus, and scleroderma.
3. Drug-induced pulmonary fibrosis: Certain medications, such as amiodarone and nitrofurantoin, can cause lung damage and scarring.
4. Radiation-induced pulmonary fibrosis: Exposure to high doses of radiation, especially in childhood, can increase the risk of developing pulmonary fibrosis later in life.
5. Environmental exposures: Exposure to pollutants such as silica, asbestos, and coal dust can increase the risk of developing pulmonary fibrosis.

Symptoms of pulmonary fibrosis include shortness of breath, coughing, and fatigue. The disease can be diagnosed through a combination of imaging tests such as chest X-rays, computed tomography (CT) scans, and magnetic resonance imaging (MRI), as well as lung biopsy.

Treatment options for pulmonary fibrosis are limited and vary depending on the underlying cause of the disease. Medications such as pirfenidone and nintedanib can help slow the progression of the disease, while lung transplantation may be an option for advanced cases.

Keloids can be caused by a variety of factors, including:

* Trauma or injury to the skin, such as cuts, burns, or bites
* Surgery or other medical procedures
* Piercings or tattoos
* Skin conditions like acne or chickenpox

Keloids can appear in different shapes and sizes, and may be:

* Red or purple in color
* Raised and irregularly shaped
* Soft and rubbery to the touch
* Itchy or painful

There is no cure for keloids, but there are several treatment options available, including:

* Steroid injections to reduce inflammation and flatten the scar tissue
* Silicone gel or sheeting to help flatten and soften the scar
* Surgery to remove the keloid and repair the underlying tissue
* Laser therapy to reduce the size and color of the keloid

It's important to note that while these treatments can help improve the appearance of keloids, they may not completely eliminate them. In some cases, keloids may return after treatment.

These animal models allow researchers to study the underlying causes of arthritis, test new treatments and therapies, and evaluate their effectiveness in a controlled environment before moving to human clinical trials. Experimental arthritis models are used to investigate various aspects of the disease, including its pathophysiology, immunogenicity, and potential therapeutic targets.

Some common experimental arthritis models include:

1. Collagen-induced arthritis (CIA): This model is induced in mice by immunizing them with type II collagen, which leads to an autoimmune response and inflammation in the joints.
2. Rheumatoid arthritis (RA) models: These models are developed by transferring cells from RA patients into immunodeficient mice, which then develop arthritis-like symptoms.
3. Osteoarthritis (OA) models: These models are induced in animals by subjecting them to joint injury or overuse, which leads to degenerative changes in the joints and bone.
4. Psoriatic arthritis (PsA) models: These models are developed by inducing psoriasis in mice, which then develop arthritis-like symptoms.

Experimental arthritis models have contributed significantly to our understanding of the disease and have helped to identify potential therapeutic targets for the treatment of arthritis. However, it is important to note that these models are not perfect representations of human arthritis and should be used as tools to complement, rather than replace, human clinical trials.

Symptoms of hereditary nephritis may include blood in the urine, proteinuria (excess protein in the urine), edema (swelling), high blood pressure, and kidney failure. The disorder can be diagnosed through blood tests, such as a viral load or genetic testing, and imaging studies, such as ultrasound or CT scans.

There is no cure for hereditary nephritis, but treatment options are available to manage the symptoms and slow the progression of the disease. Treatment may include medications to control blood pressure, reduce proteinuria, and prevent further kidney damage. In severe cases, dialysis or a kidney transplant may be necessary.

The exact cause of osteoarthritis is not known, but it is thought to be due to a combination of factors such as genetics, wear and tear on joints over time, and injuries or trauma to the joint. Osteoarthritis can affect any joint in the body, but it most commonly affects the hands, knees, hips, and spine.

The symptoms of osteoarthritis can vary depending on the severity of the condition and which joint is affected. Common symptoms include:

* Pain or tenderness in the joint
* Stiffness, especially after periods of rest or inactivity
* Limited mobility or loss of flexibility
* Grating or crackling sensations when the joint is moved
* Swelling or redness in the affected joint
* Muscle weakness or wasting

There is no cure for osteoarthritis, but there are several treatment options available to manage the symptoms and slow the progression of the disease. These include:

* Pain relief medications such as acetaminophen or nonsteroidal anti-inflammatory drugs (NSAIDs)
* Physical therapy to improve mobility and strength
* Lifestyle modifications such as weight loss, regular exercise, and avoiding activities that exacerbate the condition
* Bracing or orthotics to support the affected joint
* Corticosteroid injections or hyaluronic acid injections to reduce inflammation and improve joint function
* Joint replacement surgery in severe cases where other treatments have failed.

Early diagnosis and treatment of osteoarthritis can help manage symptoms, slow the progression of the disease, and improve quality of life for individuals with this condition.

Osteoarthritis (OA) is a degenerative condition that occurs when the cartilage that cushions the joints breaks down over time, causing the bones to rub together. It is the most common form of arthritis and typically affects older adults.

Rheumatoid arthritis (RA) is an autoimmune condition that occurs when the body's immune system attacks the lining of the joints, leading to inflammation and pain. It can affect anyone, regardless of age, and is typically seen in women.

Other types of arthritis include psoriatic arthritis, gouty arthritis, and lupus-related arthritis. Treatment for arthritis depends on the type and severity of the condition, but can include medications such as pain relievers, anti-inflammatory drugs, and disease-modifying anti-rheumatic drugs (DMARDs). Physical therapy and lifestyle changes, such as exercise and weight loss, can also be helpful. In severe cases, surgery may be necessary to repair or replace damaged joints.

Arthritis is a leading cause of disability worldwide, affecting over 50 million adults in the United States alone. It can have a significant impact on a person's quality of life, making everyday activities such as walking, dressing, and grooming difficult and painful. Early diagnosis and treatment are important to help manage symptoms and slow the progression of the disease.

There are two main types of systemic scleroderma: diffuse cutaneous systemic sclerosis (DCSS) and limited cutaneous systemic sclerosis (LCSS). DCSS is characterized by skin thickening and scar formation over the trunk, arms, and legs, while LCSS is characterized by skin tightening and patches of scaly skin on the hands and face.

The symptoms of systemic scleroderma can include:

* Skin hardening and tightening
* Fatigue
* Joint pain and stiffness
* Muscle weakness
* Swallowing difficulties
* Heartburn and acid reflux
* Shortness of breath
* Raynaud's phenomenon (pale or blue-colored fingers and toes in response to cold temperatures or stress)

The exact cause of systemic scleroderma is not known, but it is believed to involve a combination of genetic and environmental factors. Treatment options for systemic scleroderma include medications to manage symptoms such as pain, stiffness, and swallowing difficulties, as well as physical therapy and lifestyle modifications to improve quality of life.

In summary, systemic scleroderma is a chronic autoimmune disease that affects multiple systems in the body, causing skin hardening and thickening, fatigue, joint pain, and other symptoms. While there is no cure for systemic scleroderma, treatment options are available to manage symptoms and improve quality of life.

Cicatrix is a term used to describe the scar tissue that forms after an injury or surgery. It is made up of collagen fibers and other cells, and its formation is a natural part of the healing process. The cicatrix can be either hypertrophic (raised) or atrophic (depressed), depending on the severity of the original wound.

The cicatrix serves several important functions in the healing process, including:

1. Protection: The cicatrix helps to protect the underlying tissue from further injury and provides a barrier against infection.
2. Strength: The collagen fibers in the cicatrix give the scar tissue strength and flexibility, allowing it to withstand stress and strain.
3. Support: The cicatrix provides support to the surrounding tissue, helping to maintain the shape of the affected area.
4. Cosmetic appearance: The appearance of the cicatrix can affect the cosmetic outcome of a wound or surgical incision. Hypertrophic scars are typically red and raised, while atrophic scars are depressed and may be less noticeable.

While the formation of cicatrix is a normal part of the healing process, there are some conditions that can affect its development or appearance. For example, keloid scars are raised, thick scars that can form as a result of an overactive immune response to injury. Acne scars can also be difficult to treat and may leave a lasting impression on the skin.

In conclusion, cicatrix is an important part of the healing process after an injury or surgery. It provides protection, strength, support, and can affect the cosmetic appearance of the affected area. Understanding the formation and functions of cicatrix can help medical professionals to better manage wound healing and improve patient outcomes.

The hallmark symptom of EBD is the formation of large, painful blisters that can arise spontaneously or after minor trauma. These blisters can become infected and leave scars, leading to significant disability and reduced quality of life. In addition to skin blistering, individuals with EBD may experience other symptoms such as scarring alopecia, conjunctivitis, and difficulty swallowing.

The diagnosis of EBD is based on clinical findings, family history, and laboratory tests including genetic analysis. Treatment for the condition typically involves wound care and pain management, and may also involve physical therapy to maintain joint mobility and prevent contractures. In severe cases, surgery may be necessary to release tension on the skin or to repair damaged tissue.

Overall, EBD is a rare and debilitating condition that can have a significant impact on an individual's quality of life. With proper management and support, however, many individuals with EBD are able to lead active and fulfilling lives despite their challenges.

The term "experimental" refers to the fact that this type of cirrhosis is typically induced in animals through the use of certain chemicals, toxins, or viruses, rather than occurring naturally in humans. The goal of studying experimental liver cirrhosis is to gain a better understanding of the underlying mechanisms and to develop new treatments for this condition.

Some examples of how experimental liver cirrhosis may be induced include:

* Administering certain chemicals or toxins, such as carbon tetrachloride or thioacetamide, to animals in order to damage the liver and trigger the formation of nodules and fibrosis.
* Infecting animals with viruses that can cause liver damage and inflammation, such as hepatitis B or C virus.
* Using genetic models to study the role of specific genes in the development of liver cirrhosis.

Experimental liver cirrhosis is often studied in laboratory animals, such as mice, rats, and pigs, using a range of techniques including histology, biochemistry, and molecular biology. The studies may focus on various aspects of the disease, such as the mechanisms of inflammation and fibrosis, the role of specific cell types or signaling pathways, and the efficacy of potential therapeutic agents.

The hallmark of anti-GBM disease is the presence of circulating anti-GBM antibodies and immune complexes, which are deposited in the glomeruli and lung alveoli, leading to inflammation and tissue damage. The disease can progress rapidly and lead to ESRD if left untreated.

The symptoms of anti-GBM disease vary depending on the severity of the disease and may include:

* Hematuria (blood in urine)
* Proteinuria (excess protein in urine)
* Reduced kidney function
* Fatigue
* Weight loss
* Shortness of breath
* Cough

The diagnosis of anti-GBM disease is based on a combination of clinical findings, laboratory tests, and kidney biopsy. Laboratory tests may include:

* Detection of anti-GBM antibodies in the blood
* Presence of immune complexes in the urine or lung tissue
* Abnormal liver enzymes
* Low complement levels

Treatment of anti-GBM disease typically involves a combination of steroids, immunosuppressive medications, and plasmapheresis (a process that removes harmful antibodies from the blood). In severe cases, kidney transplantation may be necessary. The prognosis for anti-GBM disease is generally poor, with a five-year survival rate of approximately 50%.

During ventricular remodeling, the heart muscle becomes thicker and less flexible, leading to a decrease in the heart's ability to fill with blood and pump it out to the body. This can lead to shortness of breath, fatigue, and swelling in the legs and feet.

Ventricular remodeling is a natural response to injury, but it can also be exacerbated by factors such as high blood pressure, diabetes, and obesity. Treatment for ventricular remodeling typically involves medications and lifestyle changes, such as exercise and a healthy diet, to help manage symptoms and slow the progression of the condition. In some cases, surgery or other procedures may be necessary to repair or replace damaged heart tissue.

The process of ventricular remodeling is complex and involves multiple cellular and molecular mechanisms. It is thought to be driven by a variety of factors, including changes in gene expression, inflammation, and the activity of various signaling pathways.

Overall, ventricular remodeling is an important condition that can have significant consequences for patients with heart disease. Understanding its causes and mechanisms is crucial for developing effective treatments and improving outcomes for those affected by this condition.

The condition can be caused by a variety of factors, including excessive alcohol consumption, viral hepatitis, non-alcoholic fatty liver disease, and certain medications. It can also be a complication of other diseases such as hemochromatosis and Wilson's disease.

The symptoms of liver cirrhosis can vary depending on the severity of the disease, but may include fatigue, loss of appetite, nausea, abdominal swelling, and pain in the upper right side of the abdomen. As the disease progresses, it can lead to complications such as esophageal varices, ascites, and liver failure, which can be life-threatening.

There is no cure for liver cirrhosis, but treatment options are available to manage the symptoms and slow the progression of the disease. These may include medications to control swelling and pain, dietary changes, and in severe cases, liver transplantation. In some cases, a liver transplant may be necessary if the disease has caused significant damage and there is no other option to save the patient's life.

In conclusion, liver cirrhosis is a serious and potentially life-threatening condition that can cause significant damage to the liver and lead to complications such as liver failure. It is important for individuals to be aware of the risk factors and symptoms of the disease in order to seek medical attention if they suspect they may have liver cirrhosis. With proper treatment and management, it is possible to slow the progression of the disease and improve the patient's quality of life.

There are several types of hypertrophy, including:

1. Muscle hypertrophy: The enlargement of muscle fibers due to increased protein synthesis and cell growth, often seen in individuals who engage in resistance training exercises.
2. Cardiac hypertrophy: The enlargement of the heart due to an increase in cardiac workload, often seen in individuals with high blood pressure or other cardiovascular conditions.
3. Adipose tissue hypertrophy: The excessive growth of fat cells, often seen in individuals who are obese or have insulin resistance.
4. Neurological hypertrophy: The enlargement of neural structures such as brain or spinal cord due to an increase in the number of neurons or glial cells, often seen in individuals with neurodegenerative diseases such as Alzheimer's or Parkinson's.
5. Hepatic hypertrophy: The enlargement of the liver due to an increase in the number of liver cells, often seen in individuals with liver disease or cirrhosis.
6. Renal hypertrophy: The enlargement of the kidneys due to an increase in blood flow and filtration, often seen in individuals with kidney disease or hypertension.
7. Ovarian hypertrophy: The enlargement of the ovaries due to an increase in the number of follicles or hormonal imbalances, often seen in individuals with polycystic ovary syndrome (PCOS).

Hypertrophy can be diagnosed through various medical tests such as imaging studies (e.g., CT scans, MRI), biopsies, and blood tests. Treatment options for hypertrophy depend on the underlying cause and may include medications, lifestyle changes, and surgery.

In conclusion, hypertrophy is a growth or enlargement of cells, tissues, or organs in response to an excessive stimulus. It can occur in various parts of the body, including the brain, liver, kidneys, heart, muscles, and ovaries. Understanding the underlying causes and diagnosis of hypertrophy is crucial for effective treatment and management of related health conditions.

The symptoms of EBA can vary in severity and may include:

* Blisters and sores on the skin and mucous membranes
* Skin thickening and scarring
* Pain and discomfort
* Infection and inflammation

The exact cause of EBA is not known, but it is believed to be an autoimmune response, where the body's immune system mistakenly attacks its own tissues. Genetic factors may also play a role in the development of EBA.

There is no cure for EBA, but treatment options include:

* Immunosuppressive medications to reduce inflammation and suppress the immune system
* Topical and oral medications to manage pain and prevent infection
* Wound care and debridement to promote healing and reduce scarring
* Phototherapy to reduce inflammation and promote healing

The diagnosis of EBA is based on a combination of clinical findings, laboratory tests, and skin biopsy. Laboratory tests may include:

* Immunofluorescence to detect the presence of autoantibodies against the basement membrane zone
* Direct immunofluorescence to detect the presence of autoantibodies on the skin
* Indirect immunofluorescence to detect the presence of autoantibodies in the blood

The prognosis for EBA is generally poor, with a high risk of complications and a significant impact on quality of life. However, with appropriate treatment, some patients may experience improved symptoms and reduced inflammation. Early diagnosis and aggressive treatment are important to improve outcomes in patients with EBA.

There are several subtypes of localized scleroderma, including:

* Linear morphea: This is the most common form of localized scleroderma and appears as a linear or polylinear band of hardened skin on the arms, legs, or torso.
* Plaque morphea: This type of scleroderma causes flat, disk-shaped patches of thickened skin that can be red, purple, or brown.
* Guttate morphea: This form of localized scleroderma is characterized by numerous small, drop-like lesions on the arms, legs, or torso.

The exact cause of localized scleroderma is not known, but it is believed to be an autoimmune disorder that triggers the immune system to attack healthy tissue in the skin. The condition can be diagnosed through a combination of physical examination, medical history, and diagnostic tests such as biopsies or imaging studies.

Treatment for localized scleroderma typically involves topical medications, such as corticosteroids or immunosuppressants, to reduce inflammation and slow the progression of the disease. In some cases, phototherapy or physical therapy may also be recommended to improve symptoms and prevent complications.

While there is no cure for localized scleroderma, early diagnosis and appropriate treatment can help manage the condition and improve quality of life for those affected.

While there is no cure for keratoconus, there are several treatment options available to help manage the condition. These include eyeglasses or contact lenses, specialized contact lenses called rigid gas permeable (RGP) lenses, and corneal transplantation in severe cases. Other treatments that may be recommended include phototherapeutic keratectomy (PTK), which involves removing damaged tissue from the cornea using a laser, or intacs, which are tiny plastic inserts that are placed into the cornea to flatten it and improve vision.

Keratoconus is relatively rare, affecting about 1 in every 2,000 people worldwide. However, it is more common in certain groups of people, such as those with a family history of the condition or those who have certain medical conditions, such as Down syndrome or sickle cell anemia. It typically affects both eyes, although one eye may be more severely affected than the other.

While there is no known cause for keratoconus, researchers believe that it may be linked to genetics, environmental factors, or a combination of both. The condition usually begins in adolescence or early adulthood and can progress over several years. In some cases, keratoconus can also be associated with other eye conditions, such as cataracts, glaucoma, or retinal detachment.

There are several symptoms of RA, including:

1. Joint pain and stiffness, especially in the hands and feet
2. Swollen and warm joints
3. Redness and tenderness in the affected areas
4. Fatigue, fever, and loss of appetite
5. Loss of range of motion in the affected joints
6. Firm bumps of tissue under the skin (rheumatoid nodules)

RA can be diagnosed through a combination of physical examination, medical history, blood tests, and imaging studies such as X-rays or ultrasound. Treatment typically involves a combination of medications, including nonsteroidal anti-inflammatory drugs (NSAIDs), disease-modifying anti-rheumatic drugs (DMARDs), and biologic agents. Lifestyle modifications such as exercise and physical therapy can also be helpful in managing symptoms and improving quality of life.

There is no cure for RA, but early diagnosis and aggressive treatment can help to slow the progression of the disease and reduce symptoms. With proper management, many people with RA are able to lead active and fulfilling lives.

Blisters are caused by friction or rubbing against a surface, which causes the top layer of skin to separate from the underlying layer. This separation creates a space that fills with fluid, forming a blister. Blisters can also be caused by burns, chemical exposure, or other types of injury.

There are different types of blisters, including:

1. Friction blisters: These are the most common type of blister and are caused by friction or rubbing against a surface. They are often seen on the hands, feet, and buttocks.
2. Burn blisters: These are caused by burns and can be more severe than friction blisters.
3. Chemical blisters: These are caused by exposure to chemicals and can be very painful.
4. Blisters caused by medical conditions: Certain medical conditions, such as epidermolysis bullosa (a genetic disorder that affects the skin), can cause blisters to form easily.

Blisters can be treated in several ways, depending on their size and location. Small blisters may not require treatment and can heal on their own within a few days. Larger blisters may need to be drained and covered with a bandage to prevent infection. In severe cases, surgical intervention may be necessary.

Preventing blisters is key to avoiding the discomfort and pain they can cause. To prevent blisters, it is important to:

1. Wear properly fitting shoes and clothing to reduce friction.
2. Use lubricating creams or powders to reduce friction.
3. Take regular breaks to rest and allow the skin to recover.
4. Avoid using harsh chemicals or detergents that can cause irritation.
5. Keep the affected area clean and dry to prevent infection.

In conclusion, blisters are a common and uncomfortable condition that can be caused by a variety of factors. While they can be treated and managed, prevention is key to avoiding the discomfort and pain they can cause. By taking steps to prevent blisters and seeking medical attention if they do occur, individuals can reduce their risk of developing this uncomfortable condition.

There are several factors that can contribute to bone resorption, including:

1. Hormonal changes: Hormones such as parathyroid hormone (PTH) and calcitonin can regulate bone resorption. Imbalances in these hormones can lead to excessive bone resorption.
2. Aging: As we age, our bones undergo remodeling more frequently, leading to increased bone resorption.
3. Nutrient deficiencies: Deficiencies in calcium, vitamin D, and other nutrients can impair bone health and lead to excessive bone resorption.
4. Inflammation: Chronic inflammation can increase bone resorption, leading to bone loss and weakening.
5. Genetics: Some genetic disorders can affect bone metabolism and lead to abnormal bone resorption.
6. Medications: Certain medications, such as glucocorticoids and anticonvulsants, can increase bone resorption.
7. Diseases: Conditions such as osteoporosis, Paget's disease of bone, and bone cancer can lead to abnormal bone resorption.

Bone resorption can be diagnosed through a range of tests, including:

1. Bone mineral density (BMD) testing: This test measures the density of bone in specific areas of the body. Low BMD can indicate bone loss and excessive bone resorption.
2. X-rays and imaging studies: These tests can help identify abnormal bone growth or other signs of bone resorption.
3. Blood tests: Blood tests can measure levels of certain hormones and nutrients that are involved in bone metabolism.
4. Bone biopsy: A bone biopsy can provide a direct view of the bone tissue and help diagnose conditions such as Paget's disease or bone cancer.

Treatment for bone resorption depends on the underlying cause and may include:

1. Medications: Bisphosphonates, hormone therapy, and other medications can help slow or stop bone resorption.
2. Diet and exercise: A healthy diet rich in calcium and vitamin D, along with regular exercise, can help maintain strong bones.
3. Physical therapy: In some cases, physical therapy may be recommended to improve bone strength and mobility.
4. Surgery: In severe cases of bone resorption, surgery may be necessary to repair or replace damaged bone tissue.

The exact cause of endomyocardial fibrosis is not known, but it is believed to be related to inflammation and scarring within the heart. The condition is more common in men than women, and typically affects people between the ages of 20 and 50. Symptoms of endomyocardial fibrosis can include shortness of breath, fatigue, swelling in the legs and feet, and chest pain.

There is no cure for endomyocardial fibrosis, but treatment options may include medications to manage symptoms, surgery to repair or replace damaged heart tissue, and lifestyle changes such as a healthy diet and regular exercise. In severe cases, heart transplantation may be necessary. Early diagnosis and treatment can help slow the progression of the condition and improve quality of life for those affected.

Some common types of cartilage diseases include:

1. Osteoarthritis: A degenerative condition that causes the breakdown of joint cartilage and bone damage.
2. Rheumatoid arthritis: An autoimmune disease that causes inflammation and pain in the joints, including the cartilage.
3. Cartilage tears: Tears in the cartilage of a joint can cause pain, stiffness, and limited mobility.
4. Cartilage thinning: A condition where the cartilage becomes thinner over time, leading to joint pain and stiffness.
5. Chondrocalcinosis: A condition where calcium deposits form in the cartilage, causing pain and stiffness in the affected joint.
6. Chondromalacia patellae: A condition where the cartilage on the underside of the kneecap deteriorates, leading to pain and instability in the knee joint.
7. Osteochondritis dissecans: A condition where a piece of cartilage and bone becomes detached from the joint surface, causing pain and stiffness.
8. Paget's disease of bone: A condition where the bones become enlarged and deformed due to abnormal bone growth, which can affect the cartilage.
9. Bone spurs: Bony outgrowths that can form in response to injury or inflammation, and can cause pain and limited mobility.
10. Avascular necrosis: A condition where the blood supply to a bone is disrupted, leading to bone death and cartilage damage.

These are just a few examples of cartilage diseases. There are many other conditions that can affect the cartilage in different parts of the body. Treatment options for cartilage diseases vary depending on the specific condition and its severity, but may include medication, physical therapy, or surgery.

There are several types of tendon injuries, including:

1. Tendinitis: Inflammation of a tendon, often caused by repetitive strain or overuse.
2. Tendon rupture: A complete tear of a tendon, which can be caused by trauma or degenerative conditions such as rotator cuff tears in the shoulder.
3. Tendon strain: A stretch or tear of a tendon, often caused by acute injury or overuse.
4. Tendon avulsion: A condition where a tendon is pulled away from its attachment point on a bone.

Symptoms of tendon injuries can include pain, swelling, redness, and limited mobility in the affected area. Treatment options depend on the severity of the injury and may include rest, physical therapy, medication, or surgery. Preventive measures such as proper warm-up and cool-down exercises, stretching, and using appropriate equipment can help reduce the risk of tendon injuries.

There are several types of EB, classified based on the severity of symptoms and the age of onset. The most severe form, EB simplex, is the most common and affects approximately 1 in 20,000 to 1 in 50,000 births. Other forms of EB include junctional EB, dystrophic EB, and Kindler syndrome.

Symptoms of EB typically appear within the first few weeks of life and may include:

* Blisters and sores on the skin and mucous membranes
* Skin that is thin and fragile, with a characteristic "velvety" texture
* Delayed healing of wounds and scars
* Increased risk of infection
* Poor wound closure

Treatment for EB is focused on managing symptoms and preventing complications. This may include:

* Wound care and dressing changes
* Antibiotics to prevent infection
* Pain management
* Physical therapy to maintain joint mobility and prevent deformities
* Phototherapy to promote healing

There is currently no cure for EB, but researchers are working to develop new treatments and gene therapies to improve the lives of those affected by the condition. With proper management and support, however, many people with EB can lead active and fulfilling lives.

The cause of Dupuytren contracture is not fully understood, but it is believed to be related to genetic factors and may be more common in people of Northern European ancestry. Other risk factors include a family history of the condition, alcoholism, diabetes, and liver or kidney disease.

The symptoms of Dupuytren contracture can progress slowly over time, with the fingers gradually becoming more bent and rigid. In some cases, the contracture can become severe enough to interfere with hand function and daily activities. Treatment options for Dupuytren contracture include physical therapy, splints, and surgery.

Surgery is often recommended for people with severe contractures or those who have significant difficulty with hand function. The goal of surgery is to release the contracted tissue and restore normal hand movement. However, surgery is not always successful, and recurrence of the contracture is common.

In addition to surgery, other treatment options for Dupuytren contracture include:

* Physical therapy to improve hand function and range of motion
* Splints to help straighten the fingers
* Injections of enzymes or other medications to dissolve the contracted tissue
* Radiofrequency ablation to heat and shrink the contractured tissue

It is important to note that Dupuytren contracture is a chronic condition, meaning it cannot be cured and will require ongoing treatment and monitoring. With proper treatment and management, however, many people with Dupuytren contracture are able to maintain functional use of their hands and improve their quality of life.

There are several ways to prevent and treat scurvy, including:

* Eating foods rich in vitamin C, such as citrus fruits, leafy greens, and bell peppers.
* Taking vitamin C supplements.
* Increasing the intake of other nutrients that help the body absorb vitamin C, such as calcium and potassium.
* Avoiding foods and drinks that are high in oxalic acid, which can interfere with the absorption of vitamin C.

The discovery of scurvy and its treatment have had a significant impact on the history of medicine and nutrition. It led to the discovery of other essential nutrients and the development of modern nutrition science.

A rare autoimmune disorder characterized by inflammation and damage to cartilage and connective tissue throughout the body, often leading to arthritis, skin rashes, and other symptoms. The condition is often triggered by infections or exposure to certain medications, and can be difficult to diagnose due to its diverse range of symptoms. Treatment typically involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing: A rare autoimmune disorder affecting cartilage and connective tissue throughout the body, often causing arthritis and skin rashes. The condition is difficult to diagnose due to its diverse range of symptoms, but treatment involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body. The condition can cause a wide range of symptoms, including arthritis, skin rashes, and inflammation in various organs and joints. It is often triggered by infections or exposure to certain medications, and can be difficult to diagnose due to its diverse range of symptoms. Treatment typically involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, causing arthritis, skin rashes, and other symptoms. Treatment involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder characterized by inflammation and damage to cartilage and connective tissue throughout the body, often leading to arthritis, skin rashes, and other symptoms. Treatment typically involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, causing arthritis, skin rashes, and other symptoms. Treatment involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves immunosuppressive medications and surgery to repair damaged tissue.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves immunosuppressive medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment usually involves immunosuppressive medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves immunosuppressive medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary to treat severe cases of the disorder.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves a combination of medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary to treat severe cases of the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves a combination of medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary to treat severe cases of the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves a combination of medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary to treat severe cases of the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment typically involves a combination of medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary to treat severe cases of the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In some cases, bone marrow transplantation may be necessary to treat severe cases of the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis, relapsing is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to arthritis, skin rashes, and other symptoms. Treatment often involves a combination of medications and surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to treat the disorder effectively.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis and skin rashes. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that affects cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Polychondritis is a rare autoimmune disorder that can cause inflammation in cartilage and connective tissue throughout the body, leading to symptoms such as arthritis, skin rashes, and other symptoms. Treatment typically involves medications to reduce inflammation and suppress the immune system, as well as surgery to repair damaged tissue. In severe cases, bone marrow transplantation may be necessary to effectively treat the disorder.

Treatment for ureteral obstruction depends on the underlying cause and may include medications, endoscopic procedures, or surgery. In some cases, a temporary drainage catheter may be placed in the ureter to help relieve symptoms until the blockage can be fully treated.

Ureteral obstruction can be acute or chronic, and may occur in adults or children. It is important to seek medical attention if symptoms persist or worsen over time, as untreated ureteral obstruction can lead to complications such as kidney damage or sepsis.

Causes of Ureteral Obstruction:

Ureteral obstruction can be caused by a variety of factors, including:

1. Kidney stones: Small, hard mineral deposits that form in the urine and can block the flow of urine through the ureters.
2. Tumors: Cancerous or non-cancerous growths that can block the ureters.
3. Scar tissue: Scarring from previous surgeries or injuries can cause narrowing or blockages in the ureters.
4. Prostate enlargement: In men, an enlarged prostate gland can press on the urethra and ureters, causing blockages.
5. Bladder neck obstruction: A condition where the bladder neck is narrow or blocked, preventing urine from flowing through the urethra.
6. Trauma: Injuries to the ureters or bladder can cause blockages.
7. Inflammation: Inflammation in the ureters or kidneys can cause swelling and blockages.
8. Congenital conditions: Some people may be born with abnormalities that cause blockages in the urinary tract.
9. Neurological disorders: Conditions such as multiple sclerosis, Parkinson's disease, or spinal cord injuries can affect the nerves that control the bladder and ureters, leading to blockages.
10. Medications: Certain medications, such as certain antibiotics and chemotherapy drugs, can cause damage to the ureters and lead to blockages.

Airway remodeling is a complex process that involves changes in the structure and function of the airways, as well as an immune response. It is characterized by the following features:

* Airway wall thickening and inflammation
* Increased mucus production
* Narrowing of the airway lumina due to smooth muscle hypertrophy and fibrosis
* Increased airway resistance and decreased lung function.

Airway remodeling is a hallmark of asthma and COPD, and it can lead to exacerbations and poor disease control if left untreated. The exact mechanisms driving airway remodeling are not fully understood, but it is believed that a combination of genetic and environmental factors contribute to its development.

There are several techniques used to assess airway remodeling in patients with respiratory diseases, including:

* Quantitative computed tomography (QCT) - This technique allows for the measurement of airway wall thickness and luminal area.
* Magnetic resonance imaging (MRI) - MRI can provide information on airway size and shape, as well as tissue composition.
* Bronchoscopy with biopsy - This procedure allows for the examination of airway tissue and the assessment of inflammation and fibrosis.

There are several treatments available for airway remodeling in patients with respiratory diseases, including:

* Medications such as bronchodilators, corticosteroids, and anti-inflammatory drugs
* Pulmonary rehabilitation - This includes exercises and education to help improve lung function and overall health.
* Lung transplantation - In severe cases of airway remodeling that do not respond to other treatments, lung transplantation may be considered.

It is important for patients with respiratory diseases to work closely with their healthcare provider to monitor their condition and adjust their treatment plan as needed. With appropriate management, many patients with airway remodeling can experience improved lung function and quality of life.

Example sentences:

1. The patient developed a foreign-body reaction after receiving a defective hip implant, resulting in severe pain and swelling.
2. The transplanted liver was rejected by the recipient's immune system, causing a foreign-body reaction that led to its failure.
3. The use of a certain drug was associated with a high risk of foreign-body reactions, leading to its withdrawal from the market.

Disease progression can be classified into several types based on the pattern of worsening:

1. Chronic progressive disease: In this type, the disease worsens steadily over time, with a gradual increase in symptoms and decline in function. Examples include rheumatoid arthritis, osteoarthritis, and Parkinson's disease.
2. Acute progressive disease: This type of disease worsens rapidly over a short period, often followed by periods of stability. Examples include sepsis, acute myocardial infarction (heart attack), and stroke.
3. Cyclical disease: In this type, the disease follows a cycle of worsening and improvement, with periodic exacerbations and remissions. Examples include multiple sclerosis, lupus, and rheumatoid arthritis.
4. Recurrent disease: This type is characterized by episodes of worsening followed by periods of recovery. Examples include migraine headaches, asthma, and appendicitis.
5. Catastrophic disease: In this type, the disease progresses rapidly and unpredictably, with a poor prognosis. Examples include cancer, AIDS, and organ failure.

Disease progression can be influenced by various factors, including:

1. Genetics: Some diseases are inherited and may have a predetermined course of progression.
2. Lifestyle: Factors such as smoking, lack of exercise, and poor diet can contribute to disease progression.
3. Environmental factors: Exposure to toxins, allergens, and other environmental stressors can influence disease progression.
4. Medical treatment: The effectiveness of medical treatment can impact disease progression, either by slowing or halting the disease process or by causing unintended side effects.
5. Co-morbidities: The presence of multiple diseases or conditions can interact and affect each other's progression.

Understanding the type and factors influencing disease progression is essential for developing effective treatment plans and improving patient outcomes.

There are several types of thrombosis, including:

1. Deep vein thrombosis (DVT): A clot forms in the deep veins of the legs, which can cause swelling, pain, and skin discoloration.
2. Pulmonary embolism (PE): A clot breaks loose from another location in the body and travels to the lungs, where it can cause shortness of breath, chest pain, and coughing up blood.
3. Cerebral thrombosis: A clot forms in the brain, which can cause stroke or mini-stroke symptoms such as weakness, numbness, or difficulty speaking.
4. Coronary thrombosis: A clot forms in the coronary arteries, which supply blood to the heart muscle, leading to a heart attack.
5. Renal thrombosis: A clot forms in the kidneys, which can cause kidney damage or failure.

The symptoms of thrombosis can vary depending on the location and size of the clot. Some common symptoms include:

1. Swelling or redness in the affected limb
2. Pain or tenderness in the affected area
3. Warmth or discoloration of the skin
4. Shortness of breath or chest pain if the clot has traveled to the lungs
5. Weakness, numbness, or difficulty speaking if the clot has formed in the brain
6. Rapid heart rate or irregular heartbeat
7. Feeling of anxiety or panic

Treatment for thrombosis usually involves medications to dissolve the clot and prevent new ones from forming. In some cases, surgery may be necessary to remove the clot or repair the damaged blood vessel. Prevention measures include maintaining a healthy weight, exercising regularly, avoiding long periods of immobility, and managing chronic conditions such as high blood pressure and diabetes.

Medical Term: Cardiomegaly

Definition: An abnormal enlargement of the heart.

Symptoms: Difficulty breathing, shortness of breath, fatigue, swelling of legs and feet, chest pain, and palpitations.

Causes: Hypertension, cardiac valve disease, myocardial infarction (heart attack), congenital heart defects, and other conditions that affect the heart muscle or cardiovascular system.

Diagnosis: Physical examination, electrocardiogram (ECG), chest x-ray, echocardiography, and other diagnostic tests as necessary.

Treatment: Medications such as diuretics, vasodilators, and beta blockers, lifestyle changes such as exercise and diet modifications, surgery or other interventions in severe cases.

Note: Cardiomegaly is a serious medical condition that requires prompt diagnosis and treatment to prevent complications such as heart failure and death. If you suspect you or someone else may have cardiomegaly, seek medical attention immediately.

The risk of developing osteoarthritis of the knee increases with age, obesity, and previous knee injuries or surgery. Symptoms of knee OA can include:

* Pain and stiffness in the knee, especially after activity or extended periods of standing or sitting
* Swelling and redness in the knee
* Difficulty moving the knee through its full range of motion
* Crunching or grinding sensations when the knee is bent or straightened
* Instability or a feeling that the knee may give way

Treatment for knee OA typically includes a combination of medication, physical therapy, and lifestyle modifications. Medications such as pain relievers, anti-inflammatory drugs, and corticosteroids can help manage symptoms, while physical therapy can improve joint mobility and strength. Lifestyle modifications, such as weight loss, regular exercise, and avoiding activities that exacerbate the condition, can also help slow the progression of the disease. In severe cases, surgery may be necessary to repair or replace the damaged joint.

With type I collagen and possibly all fibrillar collagens, if not all collagens, each triple-helix associates into a right- ... The synthesis of collagen occurs inside and outside of the cell. The formation of collagen which results in fibrillary collagen ... Multiple collagen fibrils form into collagen fibers. Collagen may be attached to cell membranes via several types of protein, ... of the collagen in the human body is type I collagen. However, as of 2011, 28 types of human collagen have been identified, ...
Collagen, type I, alpha 1 Collagen, type II, alpha 1 Collagen, type III, alpha 1 Collagen, type IV, alpha 1 Collagen, type V, ... alpha 1 Collagen, type VI, alpha 1 Collagen, type VII, alpha 1 Collagen, type VIII, alpha 1 Collagen, type IX, alpha 1 Collagen ... collagen (type I, II, VI, X collagen fibrils) and proteoglycans. The ratio and the proportion of collagen play an important ... The targeted cells can process the α- chain peptides to form triple helix collagen, and replenish the collagen in the targeted ...
When collagen is lost in large amounts, it may cause wrinkles to emerge. Tobacco use can also result in slow collagen healing. ... Most collagen belongs to types 1, 2 and 3. Collagen consists mainly of amino acids and can be mostly found in tendons, muscles ... The use of tobacco can cause damage to the skin's collagen layer. It can cause the skin around the lips to lose collagen when ... Research shows that type 1 collagen reduces in amount when exposed to UV light because of the dilapidation of the collagen. ...
... is a term previously used to describe systemic autoimmune diseases (e.g., rheumatoid arthritis, systemic lupus ... ISBN 0-8027-0449-2. Collagen disease entry in the public domain NCI Dictionary of Cancer Terms This article incorporates public ... "collagen disease" was coined by Dr. Alvin F. Coburn in 1932, on his quest to discover streptococcal infection as the cause for ... but now is thought to be more appropriate for diseases associated with defects in collagen, which is a component of the ...
... (Fibril Associated Collagens with Interrupted Triple helices) is a type of collagen which is also a proteoglycan ... Triple helix Collagen helix GO term: FACIT collagen[permanent dead link] "FACIT - Collagens which are proteoglycnas". Archived ... FACIT collagens include collagen types IX, XII, XIV, XIX, and XXI. COL22A1 is also included in this class. ... Tuckwell D (2002). "Identification and analysis of collagen alpha 1(XXI), a novel member of the FACIT collagen family". Matrix ...
Binds fibril-forming collagens, collagen of types I, II, III and X. A specific binding site in collagen II has been identified ... It preferentially binds collagens IV, VI and type XIII collagen, but also fibril-forming collagens. Specific binding sites in ... A ligand of Lair-1 receptor is type XVII transmembrane collagen, it binds type I and III collagen as well. Collagen binding ... It binds fibril-forming collagens and primarily type IV collagen, but also collagen of types I, VI, VIII. It is expressed ...
Collagen folded into a triple helix is known as tropocollagen. Collagen triple helices are often bundled into fibrils which ... The rise of the collagen helix (superhelix) is 2.9 Å (0.29 nm) per residue. The center of the collagen triple helix is very ... including type I collagen. In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the ... the collagen triple helix or type-2 helix is the main secondary structure of various types of fibrous collagen, ...
Role of Collagen VI in Knee Function Studies have revealed that the mutation or deletion of genes encoding for collagen VI can ... Collagen VI (ColVI) is a type of collagen primarily associated with the extracellular matrix of skeletal muscle. ColVI ... Lampe AK, Flanigan KM, Bushby KM, Hicks D (August 9, 2012). "Collagen VI-Related Dystrophies". Collagen Type VI-Related ... Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen. J. Biol. Chem. 272, 26522-26529. ...
Collagen is denatured by heating in the presence of SDS prior to loading the gel. The collagen bands are visualized through CHP ... Collagen is the main component of the extracellular matrix (ECM). The collagen superfamily consists of 28 different types of ... The binding does not depend on a specific sequence or epitope on collagen, enabling CHPs to target denatured collagen chains of ... However, changes of collagen homeostasis are associated with numerous diseases and pathological conditions. Excessive collagen ...
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 ...
Type I collagen Collagen, type III, alpha 1 Park KS, Park MJ, Cho ML, Kwok SK, Ju JH, Ko HJ, Park SH, Kim HY (2009). "Type II ... Type II collagen is organised into fibrils. This fibrillar network of collagen allows the cartilage to entrap the proteoglycan ... Collagen+type+II at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with short description ... Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by ...
... (CIA) is a condition induced in mice (or rats) to study rheumatoid arthritis. CIA is induced in mice ... Williams, RO (2004). Collagen-induced arthritis as a model for rheumatoid arthritis. Methods Mol Med. Vol. 98. pp. 207-16. doi: ... Arthritis in mice induced by a single immunisation with collagen v t e (Articles with short description, Short description ... Brand, DD; Latham, KA; Rosloniec, EF (2007). "Collagen-induced arthritis". Nat Protoc. 2 (5): 1269-75. doi:10.1038/nprot. ...
... is the protein predicted to be encoded by COL27A1. It was first described by Dr. James M. Pace and his ... It is related to the fibrillar collagens: type II, type XI, and type XXIV. Current research suggests that it is made by ... v t e (Articles lacking sources from December 2009, All articles lacking sources, Collagens, All stub articles, Protein stubs) ...
... is a type of collagen which can be cleaved to form endostatin. The endostatin is from the c terminus end of ... which codes for production of type XVIII collagen. It is speculated that the mutation of type XVIII collagen that occurs in ... When type XVIII collagen is mutated at the COL18A1 gene, exon 2 in the sequence is skipped, which results in production of an ... The collagen XVIII is located within the basement membrane, and plays a major role in the integrity of the structure of the ...
April 2012). "Collagen induction therapy for the treatment of upper lip wrinkles". J Dermatolog Treat. 23 (2): 144-52. doi: ... Collagen induction therapy (CIT), also known as microneedling, dermarolling, or skin needling, is a cosmetic procedure that ... PRP is derived from the patient's own blood and may contain growth factors that increase collagen production. It can be applied ... Abuaf OK, Yildiz H, Baloglu H, Bilgili ME, Simsek HA, Dogan B (December 2016). "Histologic Evidence of New Collagen Formulation ...
Collagen Type II collagen Collagen, type I, alpha 1 Collagen, type I, alpha 2 Collagen, type III, alpha 1 Ting, Kay R. (2016 ... Type I collagen is the most abundant collagen of the human body. It forms large, eosinophilic fibers known as collagen fibers. ... The cross-links result in the formation of very strong mature type I collagen fiber. See Collagen, type I, alpha 1#Clinical ... to make a molecule of type I pro-collagen. These triple-stranded, rope-like pro-collagen molecules must be processed by enzymes ...
... is a form of fibrillar collagen associated with classical Ehlers-Danlos syndrome. It is found within the dermal ... "Type V collagen controls the initiation of collagen fibril assembly". J. Biol. Chem. 279 (51): 53331-7. doi:10.1074/jbc. ... Collagen+Type+V at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (CS1 errors: missing periodical, ... Autoimmunity against type V collagen is associated with lung transplant failure. COL5A1, COL5A2, COL5A3 Wenstrup RJ, Florer JB ...
The collagen gel contraction assay is a type of wound contraction. It is performed using the dermal equivalent model, which ... consists of dermal fibroblasts seeded into a collagen gel. Macrophages restrain contraction of an in vitro wound healing model ...
Collagen alpha-2(IV) chain is a protein that in humans is encoded by the COL4A2 gene. This gene encodes one of the six subunits ... "Entrez Gene: COL4A2 collagen, type IV, alpha 2". Hinek A (1995). "Nature and the multiple functions of the 67-kD elastin-/ ... Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another ... Pöschl E, Pollner R, Kühn K (1988). "The genes for the alpha 1(IV) and alpha 2(IV) chains of human basement membrane collagen ...
This gene encodes one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in ... Type-I collagen Collagen GRCh38: Ensembl release 89: ENSG00000164692 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, ... "Entrez Gene: COL1A2 collagen, type I, alpha 2". Byers PH, Wallis GA, Willing MC (1991). "Osteogenesis imperfecta: translation ...
The COL11A1 gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a ... collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene ... "Entrez Gene: COL11A1 collagen, type XI, alpha 1". GeneReviews/NCBI/NIH/UW entry on Stickler Syndrome Yoshioka H, Ramirez F ( ... Collagen alpha-1(XI) chain is a protein that in humans is encoded by the COL11A1 gene. ...
Collagen XVII is a transmembrane protein, like collagen XIII, XXIII and XXV. Collagen XVII is a structural component of ... The C-terminus of collagen XVII binds to laminin 5, and correct integration of laminin 5 into the matrix requires collagen XVII ... Mutations in the human collagen XVII gene, COL17A1, lead to the absence or structural alterations and mutations of collagen ... Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a- ...
Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. ... This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. ... "Entrez Gene: COL9A3 collagen, type IX, alpha 3". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ... Collagen alpha-3(IX) chain is a protein that in humans is encoded by the COL9A3 gene. ...
Collagen alpha-1(XXI) chain is a protein that in humans is encoded by the COL21A1 gene. The protein is an extracellular matrix ... "COL21A1 collagen, type XXI, alpha 1". Entrez Gene: COL21A1. United States National Center for Biotechnology Information. Chou ... MY, Li HC (March 2002). "Genomic organization and characterization of the human type XXI collagen (COL21A1) gene". Genomics. 79 ...
Collagen XXIII shows structural homology with collagen XIII and collagen XXV . Apart from having the characteristic structure ... The molecule of collagen XXIII can be found either in membrane-bond form or in shed form. Type XXIII collagen is expressed in ... "Entrez Gene: COL23A1 collagen, type XXIII, alpha 1". Banyard J, Bao L, Zetter BR (June 2003). "Type XXIII collagen, a new ... Collagen XXIII is a type II transmembrane protein and the fourth in the subfamily of non-fibrillar transmembranous collagens. ...
This gene encodes one of the two alpha chains of type VIII collagen. The gene product is a short chain collagen and a major ... "Entrez Gene: COL8A1 collagen, type VIII, alpha 1". Shuttleworth CA (1998). "Type VIII collagen". Int. J. Biochem. Cell Biol. 29 ... Plenz GA, Deng MC, Robenek H, Völker W (2003). "Vascular collagens: spotlight on the role of type VIII collagen in ... The type VIII collagen fibril can be either a homo- or a heterotrimer. Alternatively spliced transcript variants encoding the ...
Collagen alpha-1(VI) chain is a protein that in humans is encoded by the COL6A1 gene. The collagens are a superfamily of ... Collagen VI is a major structural component of microfibrils. The basic structural unit of collagen VI is a heterotrimer of the ... "Entrez Gene: COL6A1 collagen, type VI, alpha 1". Bertini E, Pepe G (2002). "Collagen type VI and related disorders: Bethlem ... "Further characterization of the three polypeptide chains of bovine and human short-chain collagen (intima collagen)". Eur. J. ...
Collagen XIII belongs to the transmembranous subfamily of collagens, like collagen XVII, XXIII and XXV. GRCh38: Ensembl release ... Like other collagens, collagen XIII is a trimer; it is not known whether this trimer is composed of one or more than one alpha ... Latvanlehto A, Snellman A, Tu H, Pihlajaniemi T (2003). "Type XIII collagen and some other transmembrane collagens contain two ... Unlike most of the collagens, which are secreted into the extracellular matrix, collagen XIII contains a transmembrane domain ...
This gene encodes the alpha chain of type XV collagen, a member of the FACIT collagen family (fibril-associated collagens with ... Changes of collagen XV can be known to lead to cancer-like behavior in tissues. The loss of collagen XV would no longer provide ... Type XV collagen is known to be a tumor suppressor that can be used to understand tumor cells environment. Type XV collagen ... "Epitope-defined monoclonal antibodies against multiplexin collagens demonstrate that type XV and XVIII collagens are expressed ...
Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have ... This gene encodes one of the three alpha chains of type IX collagen, a collagen component of hyaline cartilage. ... "Entrez Gene: COL9A1 collagen, type IX, alpha 1". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ... Collagen alpha-1(IX) chain is a protein that in humans is encoded by the COL9A1 gene. ...
... News - 02 April 2020 - Communication TNW Collagen is the glue that holds our bodies together. It can ... Collagen networks take different forms depending on a tissues function. In this image you can see collagen purified from human ... "Weve been doing fundamental research into collagen for some time now and asked ourselves: what makes collagen networks so ... In addition to the fact that collagen networks are more flexible than collagen fibers, the networks have another advantage: ...
Collagen is a protein found widely in almost all cells of animals, and scientifically can be used to learn much about an ... Bone collagen of fish shows individual history of migration and feeding habits Peer-Reviewed Publication Research Institute for ... Bone collagen of fish shows individual history of migration and feeding habits. Research Institute for Humanity and Nature ... Then, carbon and nitrogen stable isotopes of collagen in their vertebral centrum were analyzed chronologically. A non-linear ...
Drug information for Ramosu Collagen Ampoule 200 by RaMoSu. Includes: facts, uses, warnings and directions. ... FISH SKIN COLLAGEN, SOLUBLE (FISH SKIN COLLAGEN, SOLUBLE) FISH SKIN COLLAGEN, SOLUBLE. 100 g in 100 mL. ... Ramosu Collagen Ampoule 200. Dosage form: liquid. Ingredients: FISH SKIN COLLAGEN, SOLUBLE 100g in 100mL. Labeler: RaMoSu. NDC ...
But what can hydrolyzed collagen really do for you? ... Many products contain hydrolyzed collagen, and there are a lot ... Collagen is the most abundant protein in your body, while gelatin is a degraded form of collagen. This article reviews collagen ... Because joint cartilage contains collagen, and joint pain often comes from collagen loss, its thought that collagen can reduce ... But what can hydrolyzed collagen really do for you?. Collagen is a protein found in the body of all animals, including humans. ...
SHG microscopy can be used to quantitate collagen after nerve repair via fiber alignment. Given that the development of neuroma ... characterized by disorganized collagen and sprouting axons. Collagen deposition during wound healing can be intrinsically ... Quantification of Collagen Organization after Nerve Repair Plast Reconstr Surg Glob Open. 2017 Dec 11;5(12):e1586. doi: 10.1097 ... Quantitatively, collagen fibers were more aligned in the control nerves (mean alignment 0.754, SE 0.055) than in the repairs ( ...
Buy Collagen , luxury hair care, skincare and cosmetics at HQHair.com, with Free Delivery. ... What Are Myvitamins Collagen Capsules?. Myvitamins Collagen is a hydrolysed form of collagen that is expertly formulated to ... What Are Myvitamins Collagen Capsules?. Myvitamins Collagen is a hydrolysed form of collagen that is expertly formulated to ... Why Use Myvitamins Collagen Capsules?. Collagen is like the glue that holds us together. It makes up our skin, bones, cartilage ...
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PRNewswire/ -- Collagen Matrix, Inc., a leader in regenerative medicine and a global manufacturer of collagen and mineral based ... About Collagen Matrix. Collagen Matrix, Inc., founded in 1997, delivers a full line of the highest-quality collagen and mineral ... Greg joins the Collagen Matrix executive team as an accomplished medical device executive with over 30 years of extensive ... Prior to joining Collagen Matrix, Greg held various Research and Development roles with LifeNet Health, NovaBone Products, ...
... hydrolyzed collagen) are made by breaking down collagen proteins into small pieces. They are commonly used for aging skin and ... Denatured Collagen, Hydrolised Collagen, Hydrolysed Collagen, Hydrolyzed Collagen, Hydrolyzed Collagen Protein, Marine Collagen ... Collagen peptides are very small pieces of protein from animal collagen. Collagen is one of the materials that makes up ... Collagen peptides are made by breaking down whole collagen proteins into smaller pieces. When taken by mouth, collagen peptides ...
Peter Thomas Roth FIRMx Collagen Serum is a face serum packed with 7 forms of Collagen and collagen-supporting ingredients to ... Marine Collagen, Plant Collagen and Hydrolyzed Collagen help improve the look of fine lines, wrinkles, firmness and elasticity ... Marine Collagen, Plant Collagen and Hydrolyzed Collagen - Help improve the look of fine lines, wrinkles, firmness and ... Peter Thomas Roth FIRMx Collagen Serum is a face serum packed with 7 forms of Collagen and collagen-supporting ingredients to ...
Rabbit polyclonal Collagen IV antibody. Validated in WB, IP, ELISA, IHC, ICC/IF and tested in Mouse, Rat, Hamster, Cow, Dog, ... Negligible cross-reactivity with Type I, II, III, V or VI collagens. Non-specific cross reaction of anti-collagen antibodies ... Full length native protein (purified) corresponding to Collagen IV. Collagen Type IV from human and bovine placenta. The ... Belongs to the type IV collagen family.. Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain. ...
A fibrous protein that is the chief constituent of the bodys connective tissues,...
BuyELEMIS Pro-Collagen Rose Cleansing Balm 100 g.online with Dermstore. We have a great range ofproducts available. ... ELEMIS Pro-Collagen Rose Cleansing Balm 100 g.. A facial cleansing balm that removes impurities, moisturizes and nourishes skin ... ELEMIS Pro-Collagen Rose Cleansing Balm 100 g.. A facial cleansing balm that removes impurities, moisturizes and nourishes skin ... Pro-Collagen Rose Cleansing Balm from ELEMIS purifies and moisturizes the skin helping to promote a smooth and glowing ...
Heres what the science says about top collagen-rich foods to include in your diet. ... What can collagen rich foods do for your body? ... Think: collagen water, collagen lattes and collagen smoothies. ... 10 Collagen-Rich Foods To Add to Your Diet. Eating collagen-rich foods can help your body make more of its own collagen. Heres ... But what is hydrolyzed collagen? Its a supplement form of collagen-aka smaller collagen molecules, called peptides, that have ...
... offers 10g collagen per serving. Rich in bovine collagen & good fats, nourish the body from the inside. ... What is collagen and why do we need it?. The most abundant protein in the body, collagen is the thing that holds our skin, ... Bovine collagen creamer benefits. Choosing Dose and Co collagen creamer is an easy, balanced way to supplement your diet with ... Keto-friendly, each serving of Dose & Cos bovine collagen protein powder creamer contains 10g of high quality collagen. ...
Jennifer Aniston has been named the face and the new chief creative officer of collagen brand Vital Proteins. ... shell be building greater awareness around the benefits of collagen and how it fits into her everyday life. "Collagen is the ... Collagen is the bodys most abundant protein. It helps support hair, skin, nail, bone and joint health, making it a nice fit ... Now, shes here to explain how this whole ingestible collagen thing works. Today, Vital Proteins welcomed Aniston on board as ...
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Collagen has become ubiquitous, perhaps even a poster child, for broad health and wellness as the audience for this exciting ... Related tags Collagen Beauty from within Bone health Joint health Collagen has become ubiquitous, perhaps even a poster child, ... Collagen: Going beyond skin deep By Len Monheit, Executive Director, Collagen Stewardship Alliance 20-Dec-2021. - Last updated ... Weve seen growth in organic claims around bovine collagen, and companies in the marine collagen space continue to look towards ...
... and nutritional contents for Ultra collagen type 1 &3 and over 2,000,000 other foods at MyFitnessPal ...
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My Daily Collagen™ is suitable for people who follow paleo and keto diets. Its also sugar-free, fat-free and GMO-free. ... Yes! My Daily Collagen™ is suitable for people who follow paleo and keto diets. Its also sugar-free, fat-free and GMO-free.. ...
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Collagen network remodelling and left ventricular function in constrictive pericarditis. Message subject: (Your Name) has ...
Adding collagen to your diet can be as simple a swirling a few scoops into your morning coffee. Thats not the only way: Here, ... As we get older, our natural collagen levels start depleting, which is why so many people are turning to collagen supplements ... Adding a collagen powder to your diet can be as simple as swirling a few scoops into your morning coffee. (It dissolves into ... Collagen powder supplements are proteins that have been broken down into peptides, or short chains of amino acids, that can be ...
Collagen Peptides Powder information including description from Now, supplement facts, and suggested use. Order online for ... Collagen Peptides Powder Description from Now Collagen peptides from types 1 and 3 bovine collagen are well-known for their ... Studies indicate that hydrolyzed collagen may help to support strong bones and healthy joints as well as skin smoothness and ... As the most abundant protein in mammals, collagen makes up about 30% of the bodys protein. ...
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Nourish your beauty from the inside with Beauty Shield Collagen Gummies. This unique blend of collagen, Astaxanthin, Vitamin C ... Home / Monthly Specials / August Monthly Specials / Collagen Gummy Beauty Shield Enlarge Image. Email to a Friend NeoCell. ... Beauty Shield Collagen Gummies promote even skin tone, and improve skin texture and hydration with Astaxanthin. Enjoy these ...
  • A 2018 study in postmenopausal women found that treatment with 5 grams of collagen peptides per day for a year increased bone mineral density and improved markers indicating increased bone formation and reduced bone degradation. (healthline.com)
  • One 2018 study involving 64 participants found that treatment with 1 gram of collagen peptides for 12 weeks significantly reduced wrinkling, and improved hydration and elasticity of the skin compared with a placebo group. (healthline.com)
  • Collagen peptides are very small pieces of protein from animal collagen. (medlineplus.gov)
  • Collagen peptides are made by breaking down whole collagen proteins into smaller pieces. (medlineplus.gov)
  • When taken by mouth, collagen peptides seem to build up in the skin and cartilage. (medlineplus.gov)
  • Collagen peptides are used for aging skin and osteoarthritis. (medlineplus.gov)
  • Don't confuse collagen peptides with collagen type I (native), collagen type II (native), or gelatin. (medlineplus.gov)
  • Taking collagen peptides by mouth seems to improve skin hydration and skin elasticity in older people. (medlineplus.gov)
  • Taking collagen peptides by mouth might slightly relieve pain and improve joint function in people with knee osteoarthritis. (medlineplus.gov)
  • There is interest in using collagen peptides for a number of other purposes, but there isn't enough reliable information to say whether it might be helpful. (medlineplus.gov)
  • Collagen peptides are possibly safe. (medlineplus.gov)
  • Collagen peptides have been safely used in doses up to 10 grams daily for up to 5 months. (medlineplus.gov)
  • There isn't enough reliable information to know if collagen peptides are safe to use when pregnant or breast-feeding. (medlineplus.gov)
  • Collagen peptides have most often been used by adults in doses of 2.5-10 grams daily for up to 6 months. (medlineplus.gov)
  • Miyanaga M, Uchiyama T, Motoyama A, Ochiai N, Ueda O, Ogo M. Oral Supplementation of Collagen Peptides Improves Skin Hydration by Increasing the Natural Moisturizing Factor Content in the Stratum Corneum: A Randomized, Double-Blind, Placebo-Controlled Clinical Trial. (medlineplus.gov)
  • Oral Intake of Enzymatically Decomposed AP Collagen Peptides Improves Skin Moisture and Ceramide and Natural Moisturizing Factor Contents in the Stratum Corneum. (medlineplus.gov)
  • It promises to be a day-in-the-life look at the A-lister's wellness routine, which includes some cardio, lots of natural light, and her favorite VP products, including the famed, fan-favorite Collagen Peptides that you can mix into anything your heart desires. (thecut.com)
  • On the combination formula side, we are also seeing formulas of collagen peptides alongside these boosters - a formulation strategy we expect to continue - especially in supplements and liquid shots. (cosmeticsdesign.com)
  • Collagen can't be used in its whole form, so it must be broken down into smaller pieces, known as peptides. (prohealth.com)
  • It contains our proprietary Collagen Peptides, which includes a patented collagen ingredient backed by two published, double-blind clinical studies. (fredmeyer.com)
  • It contains type 1 porcine collagen, which is essential to the skin and bones. (hqhair.com)
  • Interestingly, porcine collagen closely resembles human collagen, which is why it's often used in healthcare settings for skin, wound and tendon repair and reinforcement. (eatingwell.com)
  • Objective: to assess the efficacy of porcine collagen matrix (CM) in root coverage (RC) and increase of keratinized gingiva width (KGW) around teeth and implants. (bvsalud.org)
  • Keto-friendly, each serving of Dose & Co's bovine collagen protein powder creamer contains 10g of high quality collagen. (hollandandbarrett.com)
  • Choosing Dose and Co collagen creamer is an easy, balanced way to supplement your diet with vital bovine collagen supplies. (hollandandbarrett.com)
  • We've seen growth in organic claims around bovine collagen, and companies in the marine collagen space continue to look towards certifications such as MSC as a way to differentiate on a quality and ethical level - and support loyal consumers' values at the same time. (cosmeticsdesign.com)
  • Grassfed, Pasture-Raised Bovine Collagen from Brazil and Argentina which includes Types I and III and is good for reducing bone and joint pain, helping restore gut health, supporting healthy muscle growth and improving skin quality. (prohealth.com)
  • Wild Caught Marine Collagen which includes Types I and III and is good for keeping the skin and tissues healthy by improving elasticity. (prohealth.com)
  • In some places, for example in the skin, collagen proteins form fibrous networks that are very elastic. (tudelft.nl)
  • Your skin is made up of collagen proteins, so it makes sense that collagen supplements can heal it. (healthline.com)
  • Non-specific cross reaction of anti-collagen antibodies with other human serum proteins or non-collagen extracellular matrix proteins is negligible. (abcam.com)
  • Immunoaffinity chromatography using immobilized antigens followed by extensive cross-adsorption against other collagens, human serum proteins and non-collagen extracellular matrix proteins to remove any unwanted specificities. (abcam.com)
  • Today, Vital Proteins welcomed Aniston on board as the collagen brand's new chief creative officer and star of their new campaign. (thecut.com)
  • Collagen is the glue that holds our bodies together. (tudelft.nl)
  • Collagen is like the glue that holds us together. (hqhair.com)
  • Collagen is the glue that holds everything together. (thecut.com)
  • Some research has shown that taking collagen supplements may benefit the skin by reducing certain markers of aging. (healthline.com)
  • In this image you can see collagen purified from human cartilage (left), cowhide (middle) and a rat's tail (right). (tudelft.nl)
  • Because joint cartilage contains collagen, and joint pain often comes from collagen loss, it's thought that collagen can reduce joint pain. (healthline.com)
  • When middle-aged women (39 to 59 years) took oral collagen supplements made from chicken cartilage, they improved their fine lines, wrinkles, crow's feet and skin elasticity, according to a 2019 study in Alternative Therapies in Health and Medicine . (eatingwell.com)
  • Collagen is one of the materials that makes up cartilage, bone, and skin. (medlineplus.gov)
  • In addition to the fact that collagen networks are more flexible than collagen fibers, the networks have another advantage: they can withstand greater forces before they break down. (tudelft.nl)
  • Collagen fibers, such as those in tendons, can be stretched only about twenty percent before they tear," says Koenderink. (tudelft.nl)
  • This study explores the essential role collagen fibers may play in muscle contracture in GMC. (bvsalud.org)
  • Compared with normal muscle tissue , contracture -affected tissue tended to have more type III collagen and form shorter fibers. (bvsalud.org)
  • 2009). A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort. (healthline.com)
  • Collagen has become ubiquitous, perhaps even a poster child, for broad health and wellness as the audience for this exciting ingredient has continued to expand in recent years. (cosmeticsdesign.com)
  • Lastly, and related to but slightly separate from this active environment is the position of collagen in next generation sports nutrition, both as a protein source, but also as a functional structural ingredient. (cosmeticsdesign.com)
  • This presents an interesting challenge and opportunity for an ingredient that is clearly an animal product, since collagen is a structural animal protein, not naturally found in any plants. (cosmeticsdesign.com)
  • In 2022, expect the communication on both ingredient and brand differentiation strategies to heat up significantly, and the vegetarian collagen dialogue will not go away. (cosmeticsdesign.com)
  • Collagen Matrix, Inc., founded in 1997, delivers a full line of the highest-quality collagen and mineral based medical devices that support the body's natural ability to regenerate. (prnewswire.com)
  • Collagen is the body's most abundant protein. (thecut.com)
  • By 60 years old, over half your body's collagen has been depleted. (prohealth.com)
  • In a 2019 study published in Alternative Therapies In Health and Medicine , where participants consumed collagen supplements regularly, researchers reported successful anti-aging benefits including reduced fine lines, wrinkles and crow's feet. (eatingwell.com)
  • 2 grams of pro-collagen to support quality collagen production (which is especially important after age 60). (prohealth.com)
  • Peter Thomas Roth FIRMx Collagen Serum is a face serum packed with 7 forms of Collagen and collagen-supporting ingredients to help skin appear firmer and smoother. (ulta.com)
  • This collagen formula is enhanced with clinically-studied ingredients like Vitamin C and probiotics for added support for your healthy immune system, gut health and digestion. (target.com)
  • Multi Collagen Protein is more than just collagen - it's real results you can see and feel, from ingredients you can trust. (target.com)
  • The Food and Drug Administration (FDA) has also approved the use of collagen implants to smooth wrinkles and treat acne scars. (healthline.com)
  • Smoking and tanning can also damage your natural collagen levels, resulting in prematurely aging skin with deeper, more noticeable wrinkles. (hollandandbarrett.com)
  • Decreased collagen production can cause numerous age-related effects including, wrinkles, shrinking and weak muscles, stiff joints and tendons, joint pain, weakening bones, limited joint mobility, gut imbalances and reduced blood flow. (prohealth.com)
  • Eggshell Membrane Collagen which includes Types I, V and X and is good for reducing joint pain and stiffness, helping support joint mobility, improving skin quality to decrease wrinkles and fine lines, and supporting a healthy gut. (prohealth.com)
  • Many products contain hydrolyzed collagen, and there are a lot of supplements on the market. (healthline.com)
  • However, keep in mind that most studies showing joint pain improvement with collagen consumption have used high-dose collagen hydrolysate supplements. (healthline.com)
  • Although our natural levels decline as we age, supplements can help to restore the amount of collagen in our body. (hqhair.com)
  • Legit benefits aside, the reality is that regular collagen supplements aren't for everyone. (eatingwell.com)
  • Unlike most collagen supplements that focus on skin health, our Longevity Collagen was formulated to support your total health as you age. (prohealth.com)
  • With an expert formulation, our Collagen Capsules can help to boost your levels to support the health of your skin and joints. (hqhair.com)
  • With that said, here are the 10 best collagen-rich foods to add to your eating pattern to boost your intake. (eatingwell.com)
  • Restore your skin's natural moisture and boost collagen production with this invigorating, leave-on energy gel. (theorganicpharmacy.com)
  • 365 mg of Collagen Boost Complex which includes 250 mgs of hyaluronic acid to help lubricate joints to fight against joint pain and stiffness. (prohealth.com)
  • Collagen is everywhere in our body, and although it is naturally very elastic, there are limits to that elasticity. (tudelft.nl)
  • Chicken Collagen which includes Type II and is good for reducing joint pain, supporting gut health and improving skin elasticity and appearance. (prohealth.com)
  • The most abundant protein in the body, collagen is the thing that holds our skin, ligaments, muscles, bones and tendons together. (hollandandbarrett.com)
  • Collagen is the most abundant protein your body makes. (prohealth.com)
  • Studies show that hydrolyzed collagen (or collagen hydrolysate) can help strengthen your joints and help with pain caused by conditions like osteoarthritis. (healthline.com)
  • Prokopová A, Pavlacková J, Mokrejs P, Gál R. Collagen Hydrolysate Prepared from Chicken By-Product as a Functional Polymer in Cosmetic Formulation. (medlineplus.gov)
  • Fibrosis and intercellular collagen connections from four weeks of muscle strains. (cdc.gov)
  • polymers, and the progress recently made concerning resistance to hydrolytic collagen degradation. (bvsalud.org)
  • In contrast to normally repairable muscle defects, fibroblasts in non-repairable defects were shown to downregulate collagen -related pathways at the early and late stages of tissue repair. (bvsalud.org)
  • Study findings include the suggestion that the collagen secretion function of fibroblasts and collagen pattern might influence the muscle repair ability and be further involved in the GMC pathogenic process. (bvsalud.org)
  • Correlation between ageing and collagen gel contractility of human fibroblasts. (bvsalud.org)
  • Scientists at the Research Institute for Humanity and Nature (RIHN) and Japan Fisheries Research and Education Agency (FRA), Japan, prove this point for Japanese flounder by measuring isotope ratios in vertebral-bone collagen. (eurekalert.org)
  • Greg joins the Collagen Matrix executive team as an accomplished medical device executive with over 30 years of extensive experience designing, developing and commercializing medical devices for the regeneration of bone and soft tissues. (prnewswire.com)
  • And if you're looking for more collagen type I (the type of collagen that plays a big role in skin, hair and nail health), then beef bone broth is a worthy go-to because it's a great source of collagen type I. Make your own with our Beef Bone Broth recipe . (eatingwell.com)
  • They contain both type I and type III collagens - those found in skin, bones, organs and tendons, plus those found most usually in bone marrow. (hollandandbarrett.com)
  • The next obvious benefit area is the continued development of the bone and joint health market, and the essential role collagen and related science will play. (cosmeticsdesign.com)
  • viscosity, reduced red cell deformability, The main objectives of this study were abnormal red cell adhesive properties, en- to assess platelet aggregation patterns and dothelial intimal proliferation, bone marrow levels of PC, PS and AT III in SCA patients or fat embolism and a chronic hypercoagula- in the steady state and in vaso-occlusive ble state [6]. (who.int)
  • Greg's experience and knowledge will strengthen our executive team and I look forward to expanding our product pipeline across the various technology platforms that underlie Collagen Matrix," said Bart J. Doedens , CEO of Collagen Matrix Inc. (prnewswire.com)
  • Prior to joining Collagen Matrix, Greg held various Research and Development roles with LifeNet Health, NovaBone Products, Integra LifeSciences, Dentsply and Orthovita specializing in products for dentistry, sports medicine, orthopaedics/spine, and neurosurgery along with plastic and reconstructive surgery applications. (prnewswire.com)
  • More information about Collagen Matrix can be found at www.CollagenMatrix.com . (prnewswire.com)
  • Instead, collagen in the skin, as in many other places, forms disorderly networks that are enormously flexible and can move with the forces they are subjected to. (tudelft.nl)
  • There are other claims that collagen can be used in skin creams to improve skin structure, but they aren't backed up by research. (healthline.com)
  • 1. Vitamin C contributes to normal collagen formation for the normal function of skin. (hqhair.com)
  • Pro-Collagen Rose Cleansing Balm from ELEMIS purifies and moisturizes the skin helping to promote a smooth and glowing complexion. (dermstore.com)
  • Even if younger-looking skin or joint pain relief isn't of interest to you, collagen should still be on your radar: we start to lose collagen in our mid-20s, and after the age of 40, our bodies lose about 1 percent of collagen each year according to a 2019 review published in Molecules . (eatingwell.com)
  • Not unlike other animal sources of collagen, fish collagen is concentrated in the bones, skin and scales. (eatingwell.com)
  • Effects of hydrolyzed collagen supplementation on skin aging: a systematic review and meta-analysis. (medlineplus.gov)
  • The Organic Pharmacy's Collagen Mask is like Spanx for the skin, a lifting base layer that makes everything that comes after look better. (theorganicpharmacy.com)
  • The potent, high-performing formula is comprised of St. John's Wort, Rose Hip, Alpha Lipoic Acid, DMAE and MSM to restore moisture, stimulate and invigorate, making this Collagen Mask a must-have for all skin types. (theorganicpharmacy.com)
  • With Multi Collagen Protein, you don't have to choose between benefits for your hair, skin, nails, joints and gut - each serving brings you ten types of collagen from four real food sources to provide a broad spectrum of benefits. (target.com)
  • Collagen Candy™ is a premier formula for helping skin maintain healthy, spring-like bounce. (fredmeyer.com)
  • Collagen is a protein found widely in almost all cells of animals, and scientifically can be used to learn much about an animal's life history including human being in the present or in the past. (eurekalert.org)
  • Collagen is a protein found in the body of all animals, including humans. (healthline.com)
  • It's unclear whether simply increasing your dietary intake of collagen-rich foods, such as tough cuts of meat, would have the same effect. (healthline.com)
  • Usually found in meat, fish and dairy based foods, not getting enough dietary collagen, or eating a diet high in refined carbohydrates and sugars, can damage or reduce your supply of collagen too. (hollandandbarrett.com)
  • Collagen Type IV from human and bovine placenta. (abcam.com)
  • Source is the first obvious differentiator that is a determiner of type of collagen, base of science and consumer value proposition. (cosmeticsdesign.com)
  • Pathological testing and type III collagen testing were used in contracture tissue studies. (bvsalud.org)
  • Recurrent GMC patients seemed to have a higher type III collagen ratio (P (bvsalud.org)
  • Endostatin is derived from the noncollagenous domain 1 (NC1) at the C-terminus of collagen type XVIII. (who.int)
  • In preparations obtained from animals which received intratracheal injections of crocidolite dust, the ratio was elevated, indicating that tissue reaction to asbestos dust apparently commences with stimulation of collagen biosynthesis. (cdc.gov)
  • The researchers confined the collagen thus created between two plates, moving the upper one back and forth to exert forces on the tissue. (tudelft.nl)
  • My Daily Collagen ™ is suitable for people who follow paleo and keto diets. (losethebackpain.com)
  • To find out what makes networks of collagen so strong, the researchers ordered ready-made collagen molecules, which are commercially available. (tudelft.nl)
  • By imaging the inside of the collagen with an electron microscope, and using computer simulations of fibre networks made by the researchers in Wageningen, the team discovered what made some networks stronger than others: the average number of connections at the intersections in the network. (tudelft.nl)
  • In retrospect, the researchers' findings are easy to explain: if there are too many connections, collagen networks becomes stiff. (tudelft.nl)
  • We've been doing fundamental research into collagen for some time now and asked ourselves: what makes collagen networks so strong, and what determines the limit of that strength," says cell biophysics expert Gijsje Koenderink from TU Delft. (tudelft.nl)
  • The pattern of collagen production may contribute to the gluteal muscle contracture pathogenic process. (bvsalud.org)
  • The purpose of this study was to develop a protocol for SHG imaging of nerves and to assess whether collagen alignment can be quantified after nerve repair. (nih.gov)
  • Myvitamins Collagen is a hydrolysed form of collagen that is expertly formulated to support our natural levels. (hqhair.com)
  • Collagen has also been found to help with improving joint functionality and joint pain according to a 2021 review published in Amino Acids . (eatingwell.com)
  • The effectiveness of products depends on how the collagen is made and how the body uses it. (healthline.com)
  • The FDA has recalled several products containing hydrolyzed collagen because manufacturers have made false claims about what they can do. (healthline.com)
  • Dose & Co have done it, with this delicious caramel flavoured collagen coffee creamer, made with sustainably sourced bovine collagens. (hollandandbarrett.com)
  • Under the right conditions, namely a low temperature and a low (acid) pH value, collagen molecules can be dissolved. (tudelft.nl)
  • As active consumers also change their lifestyles to take better care of themselves to age better, formulations with several different types of substantiated collagen products are proliferating on store shelves. (cosmeticsdesign.com)
  • as the latter, she'll be building greater awareness around the benefits of collagen and how it fits into her everyday life. (thecut.com)
  • Eating collagen-rich foods can help your body make more of its own collagen. (eatingwell.com)
  • Known for its high bioavailability, bovine collagens are the most easily absorbed and digested by the human body. (hollandandbarrett.com)
  • Starting around 35 years of age, your body slowly begins to produce less collagen. (prohealth.com)
  • The collagen your body does make is also lower in quality compared to when you were younger. (prohealth.com)
  • More research is needed to determine if other sources of collagen in other forms help too. (healthline.com)
  • Bovine-aka cattle-is one of the top sources of collagen on the market. (eatingwell.com)
  • Create a beautiful canvas with this super light leave on gel mask, that boosts collagen production, lifts, tightens and brightens. (theorganicpharmacy.com)
  • Women have a significant reduction in collagen production after menopause. (prohealth.com)
  • It includes clinically supported doses of key components that tackle all aspects of age-related, low-collagen production. (prohealth.com)
  • While research is still in the early stages, a 2010 study showed that hydrolyzed collagen may play a role in preventing and treating osteoporosis. (healthline.com)
  • This includes seeing collagen as a protein source in functional foods and drinks too, where it's favorable stability and characteristics make it an interesting and easy addition to drinks and bars. (cosmeticsdesign.com)
  • Consumers increasingly cite source and value concerns as reasons they choose collagen products. (cosmeticsdesign.com)
  • While some biotechs are doing a wonderful job of developing non-animal sourced bio-identical collagen, these products are not yet on the market - and even when they are, will likely be at the super-premium end of the market. (cosmeticsdesign.com)