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.
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 scleroprotein fibril consisting mostly of type III collagen. Reticulin fibrils are extremely thin, with a diameter of between 0.5 and 2 um. They are involved in maintaining the structural integrity in a variety of organs.
The process whereby PLATELETS adhere to something other than platelets, e.g., COLLAGEN; BASEMENT MEMBRANE; MICROFIBRILS; or other "foreign" surfaces.
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).
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.
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 found predominantly in CARTILAGE and vitreous humor. It consists of three identical alpha1(II) chains.
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.
Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
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.
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 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.
A family of structurally related collagens that form the characteristic collagen fibril bundles seen in CONNECTIVE TISSUE.
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 primarily in interstitial CARTILAGE. Collagen type XI is heterotrimer containing alpha1(XI), alpha2(XI) and alpha3(XI) subunits.
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 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 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.
A non-fibrillar collagen found primarily in terminally differentiated hypertrophic CHONDROCYTES. It is a homotrimer of three identical alpha1(X) subunits.
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 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.
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.
An autosomal recessively inherited disorder characterized by the accumulation of intermediate-density lipoprotein (IDL or broad-beta-lipoprotein). IDL has a CHOLESTEROL to TRIGLYCERIDES ratio greater than that of VERY-LOW-DENSITY LIPOPROTEINS. This disorder is due to mutation of APOLIPOPROTEINS E, a receptor-binding component of VLDL and CHYLOMICRONS, resulting in their reduced clearance and high plasma levels of both cholesterol and triglycerides.
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)
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.
Glycoproteins which have a very high polysaccharide content.
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.
A fibril-associated collagen usually found crosslinked to the surface of COLLAGEN TYPE II fibrils. It is a heterotrimer containing alpha1(IX), alpha2(IX) and alpha3(IX) subunits.
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 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.
Proteins found in any species of bacterium.
Polymorphic cells that form cartilage.
The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
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.
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.
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.
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.
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.
Adherence of cells to surfaces or to other cells.
Insect members of the superfamily Apoidea, found almost everywhere, particularly on flowers. About 3500 species occur in North America. They differ from most WASPS in that their young are fed honey and pollen rather than animal food.
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.
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.

Dipyridamole inhibits TGF-beta-induced collagen gene expression in human peritoneal mesothelial cells. (1/504)

BACKGROUND: Peritoneal matrix accumulation is characteristic of peritoneal fibrosis (PF). Continuous ambulatory peritoneal dialysis (CAPD) patients who had persistent transforming growth factor-beta (TGF-beta) in their drained effluent had an increased risk of PF. We previously reported that TGF-beta stimulates the expression of types I and III collagen mRNA in cultured human peritoneal mesangial cells (HPMCs), which may predispose them to develop PF. Pharmacological interventions to attenuate TGF-beta-stimulated matrix accumulation in HPMC may have therapeutic potential for the treatment of PF. The SMAD family and the extracellular signal-regulated protein kinase (ERK1/2, p44/p42) pathways have been shown to participate in TGF-beta signaling. Our current study identified these signal pathways in HPMCs and investigated the molecular mechanisms involved in the inhibitory effects of dipyridamole on TGF-beta-induced collagen gene expression in HPMCs. METHODS: HPMCs were cultured from human omentum by an enzyme digestion METHOD: Expression of collagen alpha1(I) mRNA was determined by Northern blotting. The SMAD proteins and the ERK1/2 activity were determined by Western blotting. RESULTS: TGF-beta-stimulated collagen alpha1(I) mRNA expression of HPMC was inhibited by dipyridamole in a dose-dependent manner. Smad2 and ERK1/2 were activated in response to TGF-beta; however, TGF-beta had little effect on the protein expression of Smad4. The addition of PD98059, which blocked activation of ERK1/2, suppressed TGF-beta-induced collagen alpha1(I) mRNA expression in a dose-dependent manner. At a concentration that inhibited collagen gene expression (17 microg/mL), dipyridamole suppressed ERK1/2 activation by TGF-beta. In contrast, the same concentration of dipyridamole had no effect on TGF-beta-induced activation of Smad2. CONCLUSION: Dipyridamole inhibits TGF-beta-induced collagen gene expression in HPMC through modulation of the ERK pathway. Our study of dipyridamole may provide therapeutic basis for clinical applications in the prevention of PF.  (+info)

Haploinsufficiency for one COL3A1 allele of type III procollagen results in a phenotype similar to the vascular form of Ehlers-Danlos syndrome, Ehlers-Danlos syndrome type IV. (2/504)

Mutations in the COL3A1 gene that encodes the chains of type III procollagen result in the vascular form of Ehlers-Danlos syndrome (EDS), EDS type IV, if they alter the sequence in the triple-helical domain. Although other fibrillar collagen-gene mutations that lead to allele instability or failure to incorporate proalpha-chains into trimers-and that thus reduce the amount of mature molecules produced-result in clinically apparent phenotypes, no such mutations have been identified in COL3A1. Furthermore, mice heterozygous for Col3a1 "null" alleles have no identified phenotype. We have now found three frameshift mutations (1832delAA, 413delC, and 555delT) that lead to premature termination codons (PTCs) in exons 27, 6, and 9, respectively, and to allele-product instability. The mRNA from each mutant allele was transcribed efficiently but rapidly degraded, presumably by the mechanisms of nonsense-mediated decay. In a fourth patient, we identified a point mutation, in the final exon, that resulted in a PTC (4294C-->T [Arg1432Ter]). In this last instance, the mRNA was stable but led to synthesis of a truncated protein that was not incorporated into mature type III procollagen molecules. In all probands, the presenting feature was vascular aneurysm or rupture. Thus, in contrast to mutations in genes that encode the dominant protein of a tissue (e.g., COL1A1 and COL2A1), in which "null" mutations result in phenotypes milder than those caused by mutations that alter protein sequence, the phenotypes produced by these mutations in COL3A1 overlap with those of the vascular form of EDS. This suggests that the major effect of many of these dominant mutations in the "minor" collagen genes may be expressed through protein deficiency rather than through incorporation of structurally altered molecules into fibrils.  (+info)

Cardiac remodeling after long term norepinephrine treatment in rats. (3/504)

OBJECTIVE: In this study we have tested the hypothesis that degradation of collagen by matrix metalloproteinase 2 (MMP-2) precedes the deposition of extracellular matrix (ECM) after long term norepinephrine (NE) treatment. METHODS: Female Sprague-Dawley rats received continuous i.v. infusion of NE (0.1 mg/kg.h) for 1, 2, 3, 4 and 14 days. Heart function and weight as well as expression of cardiac colligin and of collagen I and III were examined. Furthermore, we have assessed the degradation pathway of collagen by measuring the mRNA and activity of myocardial MMP-2 and tissue inhibitor of metalloproteinase 2 (TIMP-2) as well as the protein level of TIMP-2. RESULTS: NE induced hypertrophy predominantly of the left ventricle (LV) in a time-dependent manner. It increased the mRNAs of colligin, collagen I and III, and of MMP-2 and TIMP-2 as well as MMP-2 activity in two phases: In the initial phase, at 3 and 4 days, the mRNA of colligin and of collagen I and III was elevated predominantly in the LV, MMP-2 and TIMP-2 mRNA, as well as TIMP-2 protein and MMP-activity were increased in both ventricles. The second phase, after 14 days, was characterized by a less pronounced increase in colligin, collagen I and III and in MMP-2 activity which occurred exclusively in the LV. Finally, long-term treatment with NE induced a 37% increase in interstitial fibrosis which was shown to occur exclusively in the LV after 14 days. CONCLUSION: NE treatment induced fibrosis exclusively in the LV which was associated with hypertrophy predominantly of the LV. The elevated MMP-2 activity seems to be necessary for the ECM to adapt to the enlargement of myocytes and to reduce overproduction of collagen.  (+info)

Biophysical characterization of the C-propeptide trimer from human procollagen III reveals a tri-lobed structure. (4/504)

Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix components involved in feedback inhibition, mineralization, cell growth arrest, and chemotaxis. At present, three-dimensional structural information for the C-propeptides, which would help to understand the underlying molecular mechanisms, is lacking. Here we have carried out a biophysical study of the recombinant C-propeptide trimer from human procollagen III using laser light scattering, analytical ultracentrifugation, and small angle x-ray scattering. The results show that the trimer is an elongated molecule, which by modeling of the x-ray scattering data appears to be cruciform in shape with three large lobes and one minor lobe. We speculate that each of the major lobes corresponds to one of the three component polypeptide chains, which come together in a junction region to connect to the rest of the procollagen molecule.  (+info)

Role of protein kinase C-delta in the regulation of collagen gene expression in scleroderma fibroblasts. (5/504)

Working with cultured dermal fibroblasts derived from control individuals and patients with systemic sclerosis (SSc), we have examined the effects of protein kinase C-delta (PKC-delta) on type I collagen biosynthesis and steady-state levels of COL1A1 and COL3A1 mRNAs. Rottlerin, a specific inhibitor of PKC-delta, exerted a powerful, dose-dependent inhibition of type I and type III collagen gene expression in normal and SSc cells. Optimal rottlerin concentrations caused a 70-90% inhibition of type I collagen production, a >80% reduction in COL1A1 mRNA, and a >70% reduction in COL3A1 mRNA in both cell types. In vitro nuclear transcription assays and transient transfections with COL1A1 promoter deletion constructs demonstrated that rottlerin profoundly reduced COL1A1 transcription and that this effect required a 129-bp promoter region encompassing nucleotides -804 to -675. This COL1A1 segment imparted rottlerin sensitivity to a heterologous promoter. Cotransfections of COL1A1 promoter constructs with a dominant-negative PKC-delta expression plasmid showed that suppression of this kinase silenced COL1A1 promoter activity. The results indicate that PKC-delta participates in the upregulation of collagen gene transcription in SSc and suggest that treatment with PKC-delta inhibitors could suppress fibrosis in this disease.  (+info)

Interstitial collagens I, III, and VI sequester and modulate the multifunctional cytokine oncostatin M. (6/504)

The binding of certain growth factors and cytokines to components of the extracellular matrix can regulate their local availability and modulate their biological activities. We show that oncostatin M (OSM), a profibrogenic cytokine and modulator of cancer cell proliferation, specifically binds to collagen types I, III, IV, and VI, immobilized on polystyrene or nitrocellulose. Single collagen chains inhibit these interactions in a dose-dependent manner. Cross-inhibition experiments of collagen-derived peptides point to a limited set of OSM-binding collagenous consensus sequences. Furthermore, this interaction is found for OSM but not for other interleukin-6 type cytokines. OSM binding to collagens is saturable, with dissociation constants around 10(-8) m and estimated molar ratios of 1-3 molecules of OSM bound to one molecule of triple helical collagen. Furthermore, collagen-bound OSM is biologically active and able to inhibit proliferation of A375 melanoma cells. We conclude that abundant interstitial collagens dictate the spatial pattern of bioavailable OSM. This interaction could be exploited for devising collagenous peptide-antagonists that modulate OSM bioactivity in tumor growth and fibrotic disorders like rheumatoid arthritis and hepatic fibrosis.  (+info)

Adenosine regulates the IL-1 beta-induced cellular functions of human gingival fibroblasts. (7/504)

In this study we examined the influence of adenosine on the cellular functions of human gingival fibroblasts (HGF), such as the production of inflammatory cytokines and extracellular matrices (ECM), and the expression and function of adhesion molecules. Concerning the expression of adenosine receptors, RT-PCR analysis revealed that HGF expressed adenosine receptor A1, A2a and A2b, but not A3 mRNA. Ligation of adenosine receptors by adenosine or its related analogue, 2-chloroadenosine (2-CADO), N(6)-cyclopentyladenosine (CPA) or CGS21680 synergistically increased IL-1beta-induced IL-6 and IL-8 production. In terms of ECM expression, adenosine and the adenosine receptor agonists, 2-CADO and CPA, enhanced constitutive and IL-1beta-induced expression of hyaluronate synthase mRNA, but not the mRNA levels of other ECM, such as collagen type I, III and fibronectin. Moreover, the adherence of IL-1beta-stimulated HGF to activated lymphocytes was also inhibited by adenosine, which is in part explained by the fact that adenosine down-regulated the IL-1beta-induced expression of ICAM-1 on HGF. These results provide new evidence for the possible involvement of adenosine in the regulation of inflammatory responses in periodontal tissues.  (+info)

Mast cell chymase inhibits smooth muscle cell growth and collagen expression in vitro: transforming growth factor-beta1-dependent and -independent effects. (8/504)

In the vulnerable areas of fibrous caps of advanced atherosclerotic lesions, chymase-containing mast cells are present. In such areas, the numbers of smooth muscle cells (SMCs) and the content of collagen are reduced. In this in vitro study, we found that the addition of chymase, isolated and purified from rat serosal mast cells, to cultured rat aortic SMCs of the synthetic phenotype (s-SMCs) inhibited their proliferation by blocking the G(0)/G(1)-->S transition in the cell cycle. Rat chymase and recombinant human chymase inhibited the expression of collagen type I and type III mRNA in s-SMCs and in human coronary arterial SMCs. The growth-inhibitory effect of chymase was partially reversed by addition to the culture medium of an antibody capable of neutralizing the activity of transforming growth factor-beta1 (TGF-beta1). Immunocytochemistry showed that the s-SMCs expressed and synthesized extracellular matrix-associated TGF-beta1. On exposure to mast cell chymase, the extracellular matrix-associated latent TGF-beta1 was released and activated, as demonstrated by immunoblotting and by an ELISA with TGF-beta1 type II receptor for capture. When added to s-SMCs, such chymase-released TGF-beta1 was capable of inhibiting their growth. In contrast, the inhibitory effect of chymase on collagen synthesis by s-SMCs did not depend on TGF-beta1. Taken together, the findings support the hypothesis that chymase released from activated mast cells in atherosclerotic plaques contributes to cap remodeling.  (+info)

Collagen Type III, also known as Collagen III Alpha 1 (COL3A1), is a type of collagen that is found in various connective tissues throughout the body. It is a fibrillar collagen that is produced by fibroblasts and is a major component of reticular fibers, which provide structural support to organs such as the liver, spleen, and lymph nodes. Collagen Type III is also found in the walls of blood vessels, the skin, and the intestinal tract.

Mutations in the COL3A1 gene can lead to a rare genetic disorder called Ehlers-Danlos syndrome type IV, which is characterized by fragile and elastic skin, easy bruising, and spontaneous rupture of blood vessels. Collagen Type III has been studied for its potential role in various other medical conditions, including fibrosis, cancer, and cardiovascular disease.

Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.

Collagen Type I is the most abundant form of collagen in the human body, found in various connective tissues such as tendons, ligaments, skin, and bones. It is a structural protein that provides strength and integrity to these tissues. Collagen Type I is composed of three alpha chains, two alpha-1(I) chains, and one alpha-2(I) chain, arranged in a triple helix structure. This type of collagen is often used in medical research and clinical applications, such as tissue engineering and regenerative medicine, due to its excellent mechanical properties and biocompatibility.

Reticulin is a type of protein fiber that forms part of the extracellular matrix in various connective tissues in the body. It is composed of collagenous and non-collagenous proteins, and it has a reticular or network-like structure when viewed under a microscope. In histology (the study of the microscopic structure of tissues), reticulin fibers are often stained to help identify certain types of cells or structures.

In particular, reticulin fibers are often found in close association with certain types of cells, such as hematopoietic stem cells and neurons. They provide structural support and help regulate the function of these cells. In addition, reticulin fibers play a role in the immune response, wound healing, and tissue repair.

Abnormal accumulations of reticulin fibers can be seen in various disease states, such as fibrosis (excessive scarring) and certain types of cancer. For example, increased reticulin fibers are often found in the liver in patients with cirrhosis, a condition characterized by extensive scarring and damage to the liver. Similarly, abnormal reticulin fiber deposition is seen in some forms of lymphoma, a type of cancer that affects the lymphatic system.

Platelet adhesiveness refers to the ability of platelets, which are small blood cells that help your body form clots to prevent excessive bleeding, to stick to other cells or surfaces. This process is crucial in hemostasis, the process of stopping bleeding after injury to a blood vessel.

When the endothelium (the lining of blood vessels) is damaged, subendothelial structures are exposed, which can trigger platelet adhesion. Platelets then change shape and release chemical signals that cause other platelets to clump together, forming a platelet plug. This plug helps to seal the damaged vessel and prevent further bleeding.

Platelet adhesiveness is influenced by several factors, including the presence of von Willebrand factor (vWF), a protein in the blood that helps platelets bind to damaged vessels, and the expression of glycoprotein receptors on the surface of platelets. Abnormalities in platelet adhesiveness can lead to bleeding disorders or thrombotic conditions.

Extracellular matrix (ECM) proteins are a group of structural and functional molecules that provide support, organization, and regulation to the cells in tissues and organs. The ECM is composed of a complex network of proteins, glycoproteins, and carbohydrates that are secreted by the cells and deposited outside of them.

ECM proteins can be classified into several categories based on their structure and function, including:

1. Collagens: These are the most abundant ECM proteins and provide strength and stability to tissues. They form fibrils that can withstand high tensile forces.
2. Proteoglycans: These are complex molecules made up of a core protein and one or more glycosaminoglycan (GAG) chains. The GAG chains attract water, making proteoglycans important for maintaining tissue hydration and resilience.
3. Elastin: This is an elastic protein that allows tissues to stretch and recoil, such as in the lungs and blood vessels.
4. Fibronectins: These are large glycoproteins that bind to cells and ECM components, providing adhesion, migration, and signaling functions.
5. Laminins: These are large proteins found in basement membranes, which provide structural support for epithelial and endothelial cells.
6. Tenascins: These are large glycoproteins that modulate cell adhesion and migration, and regulate ECM assembly and remodeling.

Together, these ECM proteins create a microenvironment that influences cell behavior, differentiation, and function. Dysregulation of ECM proteins has been implicated in various diseases, including fibrosis, cancer, and degenerative disorders.

Fibronectin is a high molecular weight glycoprotein that is found in many tissues and body fluids, including plasma, connective tissue, and the extracellular matrix. It is composed of two similar subunits that are held together by disulfide bonds. Fibronectin plays an important role in cell adhesion, migration, and differentiation by binding to various cell surface receptors, such as integrins, and other extracellular matrix components, such as collagen and heparan sulfate proteoglycans.

Fibronectin has several isoforms that are produced by alternative splicing of a single gene transcript. These isoforms differ in their biological activities and can be found in different tissues and developmental stages. Fibronectin is involved in various physiological processes, such as wound healing, tissue repair, and embryonic development, and has been implicated in several pathological conditions, including fibrosis, tumor metastasis, and thrombosis.

Collagen Type IV is a type of collagen that forms the structural basis of basement membranes, which are thin, sheet-like structures that separate and support cells in many types of tissues. It is a major component of the basement membrane's extracellular matrix and provides strength and flexibility to this structure. Collagen Type IV is composed of three chains that form a distinctive, mesh-like structure. Mutations in the genes encoding Collagen Type IV can lead to a variety of inherited disorders affecting the kidneys, eyes, and ears.

Collagen Type II is a specific type of collagen that is a major component of the extracellular matrix in articular cartilage, which is the connective tissue that covers and protects the ends of bones in joints. It is also found in other tissues such as the vitreous humor of the eye and the inner ear.

Collagen Type II is a triple helix molecule composed of three polypeptide chains that contain a high proportion of the amino acids proline and hydroxyproline. This type of collagen provides structural support and elasticity to tissues, and it also plays a role in the regulation of cell behavior and signaling.

Collagen Type II is a target for autoimmune responses in conditions such as rheumatoid arthritis, where the immune system mistakenly attacks the body's own collagen, leading to joint inflammation and damage. It is also a common component of various dietary supplements and therapies used to support joint health and treat osteoarthritis.

The extracellular matrix (ECM) is a complex network of biomolecules that provides structural and biochemical support to cells in tissues and organs. It is composed of various proteins, glycoproteins, and polysaccharides, such as collagens, elastin, fibronectin, laminin, and proteoglycans. The ECM plays crucial roles in maintaining tissue architecture, regulating cell behavior, and facilitating communication between cells. It provides a scaffold for cell attachment, migration, and differentiation, and helps to maintain the structural integrity of tissues by resisting mechanical stresses. Additionally, the ECM contains various growth factors, cytokines, and chemokines that can influence cellular processes such as proliferation, survival, and differentiation. Overall, the extracellular matrix is essential for the normal functioning of tissues and organs, and its dysregulation can contribute to various pathological conditions, including fibrosis, cancer, and degenerative diseases.

Fibrosis is a pathological process characterized by the excessive accumulation and/or altered deposition of extracellular matrix components, particularly collagen, in various tissues and organs. This results in the formation of fibrous scar tissue that can impair organ function and structure. Fibrosis can occur as a result of chronic inflammation, tissue injury, or abnormal repair mechanisms, and it is a common feature of many diseases, including liver cirrhosis, lung fibrosis, heart failure, and kidney disease.

In medical terms, fibrosis is defined as:

"The process of producing scar tissue (consisting of collagen) in response to injury or chronic inflammation in normal connective tissue. This can lead to the thickening and stiffening of affected tissues and organs, impairing their function."

Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.

Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.

In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.

Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Collagen Type V is a specific type of collagen, which is a protein that provides structure and strength to connective tissues in the body. Collagen Type V is found in various tissues, including the cornea, blood vessels, and hair. It plays a crucial role in the formation of collagen fibers and helps regulate the diameter of collagen fibrils. Mutations in the genes that encode for Collagen Type V can lead to various connective tissue disorders, such as Ehlers-Danlos syndrome and osteogenesis imperfecta.

Fibrillar collagens are a type of collagen that form rope-like fibrils in the extracellular matrix of connective tissues. They are composed of three polypeptide chains, called alpha chains, which are coiled together in a triple helix structure. The most common types of fibrillar collagens are Type I, II, III, V, and XI. These collagens provide strength and support to tissues such as tendons, ligaments, skin, and bones. They also play important roles in the regulation of cell behavior and tissue development. Mutations in genes encoding fibrillar collagens can lead to a variety of connective tissue disorders, including osteogenesis imperfecta, Ehlers-Danlos syndrome, and Marfan syndrome.

Collagen Type VI is a type of collagen that is widely expressed in various tissues, including skeletal muscle, skin, and blood vessels. It is a major component of the extracellular matrix and plays important roles in maintaining tissue structure and function. Collagen Type VI forms microfilaments that provide structural support to the basement membrane and regulate cell-matrix interactions. Mutations in the genes encoding collagen Type VI can lead to several inherited connective tissue disorders, such as Bethlem myopathy and Ullrich congenital muscular dystrophy.

Collagen type XI is a fibrillar collagen that is found in the extracellular matrix of various tissues, including cartilage and the eye. It is a homotrimer made up of three identical alpha 1(XI) chains or a heterotrimer composed of two alpha 1(XI) chains and one alpha 2(XI) chain. Collagen type XI is closely associated with collagen type II fibrils and plays a role in regulating the diameter and organization of these fibrils. Mutations in the genes encoding collagen type XI can lead to skeletal disorders such as stiff skin syndrome and fibrodysplasia ossificans progressiva.

Collagen receptors are a type of cell surface receptor that bind to collagen molecules, which are the most abundant proteins in the extracellular matrix (ECM) of connective tissues. These receptors play important roles in various biological processes, including cell adhesion, migration, differentiation, and survival.

Collagen receptors can be classified into two major groups: integrins and discoidin domain receptors (DDRs). Integrins are heterodimeric transmembrane proteins that consist of an alpha and a beta subunit. They bind to collagens via their arginine-glycine-aspartic acid (RGD) motif, which is located in the triple-helical domain of collagen molecules. Integrins mediate cell-collagen interactions by clustering and forming focal adhesions, which are large protein complexes that connect the ECM to the cytoskeleton.

DDRs are receptor tyrosine kinases (RTKs) that contain a discoidin domain in their extracellular region, which is responsible for collagen binding. DDRs bind to collagens via their non-RGD motifs and induce intracellular signaling pathways that regulate cell behavior.

Abnormalities in collagen receptor function have been implicated in various diseases, including fibrosis, cancer, and inflammation. Therefore, understanding the structure and function of collagen receptors is crucial for developing novel therapeutic strategies to treat these conditions.

Procollagen is the precursor protein of collagen, which is a major structural protein in the extracellular matrix of various connective tissues, such as tendons, ligaments, skin, and bones. Procollagen is synthesized inside the cell (in the rough endoplasmic reticulum) and then processed by enzymes to remove specific segments, resulting in the formation of tropocollagen, which are the basic units of collagen fibrils.

Procollagen consists of three polypeptide chains (two alpha-1 and one alpha-2 chain), each containing a central triple-helical domain flanked by non-helical regions at both ends. These non-helical regions, called propeptides, are cleaved off during the processing of procollagen to tropocollagen, allowing the individual collagen molecules to align and form fibrils through covalent cross-linking.

Abnormalities in procollagen synthesis or processing can lead to various connective tissue disorders, such as osteogenesis imperfecta (brittle bone disease) and Ehlers-Danlos syndrome (a group of disorders characterized by joint hypermobility, skin hyperextensibility, and tissue fragility).

Collagen type XVIII is a type of collagen that is found in the basement membrane, which is a thin layer of extracellular matrix that separates and supports epithelial and endothelial cells. It is a heterotrimeric protein composed of three different chains, alpha1(XVIII), alpha2(XVIII), and alpha3(XVIII). Collagen XVIII is thought to play a role in the maintenance and organization of the basement membrane, as well as in cell adhesion and migration. It also contains a number of distinct domains that are involved in various biological processes, including angiogenesis, tissue repair, and tumor growth. Mutations in the gene that encodes collagen XVIII have been associated with eye diseases such as Knobloch syndrome and familial exudative vitreoretinopathy.

Hydroxyproline is not a medical term per se, but it is a significant component in the medical field, particularly in the study of connective tissues and collagen. Here's a scientific definition:

Hydroxyproline is a modified amino acid that is formed by the post-translational modification of the amino acid proline in collagen and some other proteins. This process involves the addition of a hydroxyl group (-OH) to the proline residue, which alters its chemical properties and contributes to the stability and structure of collagen fibers. Collagen is the most abundant protein in the human body and is a crucial component of connective tissues such as tendons, ligaments, skin, and bones. The presence and quantity of hydroxyproline can serve as a marker for collagen turnover and degradation, making it relevant to various medical and research contexts, including the study of diseases affecting connective tissues like osteoarthritis, rheumatoid arthritis, and Ehlers-Danlos syndrome.

Cartilage is a type of connective tissue that is found throughout the body in various forms. It is made up of specialized cells called chondrocytes, which are embedded in a firm, flexible matrix composed of collagen fibers and proteoglycans. This unique structure gives cartilage its characteristic properties of being both strong and flexible.

There are three main types of cartilage in the human body: hyaline cartilage, elastic cartilage, and fibrocartilage.

1. Hyaline cartilage is the most common type and is found in areas such as the articular surfaces of bones (where they meet to form joints), the nose, trachea, and larynx. It has a smooth, glassy appearance and provides a smooth, lubricated surface for joint movement.
2. Elastic cartilage contains more elastin fibers than hyaline cartilage, which gives it greater flexibility and resilience. It is found in structures such as the external ear and parts of the larynx and epiglottis.
3. Fibrocartilage has a higher proportion of collagen fibers and fewer chondrocytes than hyaline or elastic cartilage. It is found in areas that require high tensile strength, such as the intervertebral discs, menisci (found in joints like the knee), and the pubic symphysis.

Cartilage plays a crucial role in supporting and protecting various structures within the body, allowing for smooth movement and providing a cushion between bones to absorb shock and prevent wear and tear. However, cartilage has limited capacity for self-repair and regeneration, making damage or degeneration of cartilage tissue a significant concern in conditions such as osteoarthritis.

Collagen type X is a specific type of collagen that is primarily found in the hypertrophic zone of mature cartilage, which is located near the site of bone formation during endochondral ossification. It plays a crucial role in the mineralization process of the cartilage matrix and is essential for the formation of healthy bones. Collagen type X is composed of three identical alpha chains that form a triple helix structure, and it is synthesized by chondrocytes, which are the specialized cells found in cartilage tissue. Mutations in the gene that encodes collagen type X have been associated with certain skeletal disorders, such as Schmid metaphyseal chondrodysplasia.

Collagen type XII is a type of collagen that is found in the extracellular matrix of various tissues, including tendons, ligaments, and skin. It is a fibril-associated collagen that is closely associated with collagens type I and III. Collagen type XII has been shown to play a role in regulating the organization and diameter of collagen fibrils. Mutations in the gene for collagen type XII have been associated with certain types of muscular dystrophy and Bethlem myopathy, which are genetic disorders that affect muscle strength and tone. Additionally, it has been suggested to play a role in the development of osteoarthritis.

The basement membrane is a thin, specialized layer of extracellular matrix that provides structural support and separates epithelial cells (which line the outer surfaces of organs and blood vessels) from connective tissue. It is composed of two main layers: the basal lamina, which is produced by the epithelial cells, and the reticular lamina, which is produced by the connective tissue. The basement membrane plays important roles in cell adhesion, migration, differentiation, and survival.

The basal lamina is composed mainly of type IV collagen, laminins, nidogens, and proteoglycans, while the reticular lamina contains type III collagen, fibronectin, and other matrix proteins. The basement membrane also contains a variety of growth factors and cytokines that can influence cell behavior.

Defects in the composition or organization of the basement membrane can lead to various diseases, including kidney disease, eye disease, and skin blistering disorders.

Laminin is a family of proteins that are an essential component of the basement membrane, which is a specialized type of extracellular matrix. Laminins are large trimeric molecules composed of three different chains: α, β, and γ. There are five different α chains, three different β chains, and three different γ chains that can combine to form at least 15 different laminin isoforms.

Laminins play a crucial role in maintaining the structure and integrity of basement membranes by interacting with other components of the extracellular matrix, such as collagen IV, and cell surface receptors, such as integrins. They are involved in various biological processes, including cell adhesion, differentiation, migration, and survival.

Laminin dysfunction has been implicated in several human diseases, including cancer, diabetic nephropathy, and muscular dystrophy.

Hyperlipoproteinemia Type III, also known as Broad Beta Disease or Remnant Hyperlipidemia, is a genetic disorder characterized by an increased level of chylomicron remnants and intermediate-density lipoproteins (IDL) in the blood. This results in elevated levels of both low-density lipoprotein (LDL), or "bad" cholesterol, and triglycerides, and decreased levels of high-density lipoprotein (HDL), or "good" cholesterol. The condition can lead to premature atherosclerosis and an increased risk for cardiovascular disease. It is caused by mutations in the APOE gene, which encodes the apolipoprotein E protein, leading to abnormal clearance of lipoproteins from the blood.

Collagen diseases, also known as collagen disorders or connective tissue diseases, refer to a group of medical conditions that affect the body's connective tissues. These tissues provide support and structure for various organs and systems in the body, including the skin, joints, muscles, and blood vessels.

Collagen is a major component of connective tissues, and it plays a crucial role in maintaining their strength and elasticity. In collagen diseases, the body's immune system mistakenly attacks healthy collagen, leading to inflammation, pain, and damage to the affected tissues.

There are several types of collagen diseases, including:

1. Systemic Lupus Erythematosus (SLE): This is a chronic autoimmune disease that can affect various organs and systems in the body, including the skin, joints, kidneys, heart, and lungs.
2. Rheumatoid Arthritis (RA): This is a chronic inflammatory disease that primarily affects the joints, causing pain, swelling, and stiffness.
3. Scleroderma: This is a rare autoimmune disorder that causes thickening and hardening of the skin and connective tissues, leading to restricted movement and organ damage.
4. Dermatomyositis: This is an inflammatory muscle disease that can also affect the skin, causing rashes and weakness.
5. Mixed Connective Tissue Disease (MCTD): This is a rare autoimmune disorder that combines symptoms of several collagen diseases, including SLE, RA, scleroderma, and dermatomyositis.

The exact cause of collagen diseases is not fully understood, but they are believed to be related to genetic, environmental, and hormonal factors. Treatment typically involves a combination of medications, lifestyle changes, and physical therapy to manage symptoms and prevent complications.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Proteoglycans are complex, highly negatively charged macromolecules that are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains. They are a major component of the extracellular matrix (ECM) and play crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and maintenance of tissue structure and function.

The GAG chains, which can vary in length and composition, are long, unbranched polysaccharides that are composed of repeating disaccharide units containing a hexuronic acid (either glucuronic or iduronic acid) and a hexosamine (either N-acetylglucosamine or N-acetylgalactosamine). These GAG chains can be sulfated to varying degrees, which contributes to the negative charge of proteoglycans.

Proteoglycans are classified into four major groups based on their core protein structure and GAG composition: heparan sulfate/heparin proteoglycans, chondroitin/dermatan sulfate proteoglycans, keratan sulfate proteoglycans, and hyaluronan-binding proteoglycans. Each group has distinct functions and is found in specific tissues and cell types.

In summary, proteoglycans are complex macromolecules composed of a core protein and one or more GAG chains that play important roles in the ECM and various biological processes, including cell signaling, growth factor regulation, and tissue structure maintenance.

Decorin is a small proteoglycan, a type of protein with a attached sugar chain, that is found in the extracellular matrix of connective tissues in the body. It is composed of a core protein and one or more glycosaminoglycan (GAG) chains, specifically dermatan sulfate. Decorin plays important roles in the organization and biomechanical properties of collagen fibrils, regulation of cell proliferation and migration, and modulation of growth factor activity. It has been studied for its potential role in various physiological and pathological processes, including wound healing, fibrosis, and cancer.

Collagen type IX is a type of collagen that is found in the extracellular matrix, particularly in the cartilage and vitreous humor of the eye. It is a heterotrimeric protein made up of three alpha chains (alpha1, alpha2, and alpha3), which are encoded by different genes (COL9A1, COL9A2, and COL9A3). Collagen type IX is thought to play a role in the organization and stability of collagen fibrils, as well as in the interaction between collagen and other extracellular matrix components. It has been implicated in various connective tissue disorders, such as Stickler syndrome and Marshall syndrome.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Articular cartilage is the smooth, white tissue that covers the ends of bones where they come together to form joints. It provides a cushion between bones and allows for smooth movement by reducing friction. Articular cartilage also absorbs shock and distributes loads evenly across the joint, protecting the bones from damage. It is avascular, meaning it does not have its own blood supply, and relies on the surrounding synovial fluid for nutrients. Over time, articular cartilage can wear down or become damaged due to injury or disease, leading to conditions such as osteoarthritis.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Chondrocytes are the specialized cells that produce and maintain the extracellular matrix of cartilage tissue. They are responsible for synthesizing and secreting the collagen fibers, proteoglycans, and other components that give cartilage its unique properties, such as elasticity, resiliency, and resistance to compression. Chondrocytes are located within lacunae, or small cavities, in the cartilage matrix, and they receive nutrients and oxygen through diffusion from the surrounding tissue fluid. They are capable of adapting to changes in mechanical stress by modulating the production and organization of the extracellular matrix, which allows cartilage to withstand various loads and maintain its structural integrity. Chondrocytes play a crucial role in the development, maintenance, and repair of cartilaginous tissues throughout the body, including articular cartilage, costal cartilage, and growth plate cartilage.

In medical terms, the skin is the largest organ of the human body. It consists of two main layers: the epidermis (outer layer) and dermis (inner layer), as well as accessory structures like hair follicles, sweat glands, and oil glands. The skin plays a crucial role in protecting us from external factors such as bacteria, viruses, and environmental hazards, while also regulating body temperature and enabling the sense of touch.

Microbial collagenase is not a medical term per se, but it does refer to an enzyme that is used in various medical and research contexts. Collagenases are a group of enzymes that break down collagen, a structural protein found in connective tissues such as skin, tendons, and ligaments. Microbial collagenase is a type of collagenase that is produced by certain bacteria, such as Clostridium histolyticum.

In medical terms, microbial collagenase is used in various therapeutic and research applications, including:

1. Wound healing: Microbial collagenase can be used to break down and remove necrotic tissue from wounds, which can help promote healing and prevent infection.
2. Dental applications: Collagenases have been used in periodontal therapy to remove calculus and improve the effectiveness of root planing and scaling procedures.
3. Research: Microbial collagenase is a valuable tool for researchers studying the structure and function of collagen and other extracellular matrix proteins. It can be used to digest tissue samples, allowing scientists to study the individual components of the extracellular matrix.

It's important to note that while microbial collagenase has many useful applications, it must be used with care, as excessive or improper use can damage healthy tissues and cause adverse effects.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

A tendon is the strong, flexible band of tissue that connects muscle to bone. It helps transfer the force produced by the muscle to allow various movements of our body parts. Tendons are made up of collagen fibers arranged in parallel bundles and have a poor blood supply, making them prone to injuries and slow to heal. Examples include the Achilles tendon, which connects the calf muscle to the heel bone, and the patellar tendon, which connects the kneecap to the shinbone.

Pepsin A is defined as a digestive enzyme that is primarily secreted by the chief cells in the stomach's fundic glands. It plays a crucial role in protein catabolism, helping to break down food proteins into smaller peptides during the digestive process. Pepsin A has an optimal pH range of 1.5-2.5 for its enzymatic activity and is activated from its inactive precursor, pepsinogen, upon exposure to acidic conditions in the stomach.

Collagen type VIII is a less common type of collagen that is found in the eyes, specifically in the basement membrane of the cornea and the blood vessels of the eye. It is a network-forming collagen and is believed to play a role in maintaining the structural integrity and stability of these tissues. Mutations in the genes encoding for collagen type VIII have been associated with certain eye disorders, such as Fuchs' endothelial corneal dystrophy.

Here is a medical definition from the US National Library of Medicine:

"Collagen, type VIII, alpha-1 (COL8A1) is a gene that provides instructions for making one component of a type VIII collagen protein called collagen VIII alpha-1 chain. Collagen proteins are important building blocks for many tissues in the body, including tendons, ligaments, and the cornea, which is the clear outer covering of the eye.

Collagen VIII is found in the basement membrane, a thin layer of protein that surrounds many types of cells and helps to anchor them to surrounding tissue. In the eye, collagen VIII is produced by cells called endothelial cells, which line the inside surface of the cornea. Collagen VIII forms networks with other proteins that help maintain the structural integrity and stability of the cornea.

Mutations in the COL8A1 gene can cause Fuchs' endothelial corneal dystrophy, a progressive eye disorder characterized by the gradual clouding of the cornea." ()

Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.

"Bees" are not a medical term, as they refer to various flying insects belonging to the Apidae family in the Apoidea superfamily. They are known for their role in pollination and honey production. If you're looking for medical definitions or information, please provide relevant terms.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Tropocollagen is the fundamental unit of collagen, a protein that provides strength and structure to various tissues in the body. It is composed of three polypeptide chains coiled together in a triple helix structure. These chains are rich in the amino acids proline and hydroxyproline, which contribute to the stability of the helical structure. Tropocollagen molecules can further assemble into larger fibrils and fibers, providing tensile strength to tissues such as tendons, ligaments, and skin.

This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. Mutations ... "Entrez Gene: COL9A3 collagen, type IX, alpha 3". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
... type III collagen is also an important regulator of the diameter of type I and II collagen fibrils. Type III collagen is also ... Type III collagen could also be important in several other human diseases. Increased amounts of type III collagen are found in ... Type III collagen is one of the fibrillar collagens whose proteins have a long, inflexible, triple-helical domain. Type III ... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ...
... related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type ... Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in ... type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This ... "Entrez Gene: COL5A3 collagen, type V, alpha 3". van der Rest M, Garrone R (1991). "Collagen family of proteins". FASEB J. 5 (13 ...
This protein is an alpha chain of type VI collagen that aids in microfibril formation. As part of type VI collagen, this ... one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The alpha 3 ... both Bethlem myopathy and autosomal recessive UCMD patients are heterozygous for mutations in the three type VI collagen alpha ... "Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen". American Journal of Human ...
2003). "Type-IV collagen related diseases". J. Nephrol. 16 (2): 314-6. PMID 12768082. Torra R, Tazón-Vega B, Ars E, Ballarín J ... Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits; ... Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another ... "Entrez Gene: COL4A3 collagen, type IV, alpha 3 (Goodpasture antigen)". Hinek A (1995). "Nature and the multiple functions of ...
A ligand of Lair-1 receptor is type XVII transmembrane collagen, it binds type I and III collagen as well. Collagen binding ... Binds fibril-forming collagens, collagen of types I, II, III and X. A specific binding site in collagen II has been identified ... It binds fibril-forming collagens and primarily type IV collagen, but also collagen of types I, VI, VIII. It is expressed ... It preferentially binds collagens IV, VI and type XIII collagen, but also fibril-forming collagens. Specific binding sites in ...
This step is absent when synthesizing type III, a type of fibrillar collagen. Formation of the collagen fibril: lysyl oxidase, ... of the collagen in the human body is type I collagen. However, as of 2011, 28 types of human collagen have been identified, ... The number of types shows collagen's diverse functionality. Fibrillar (Type I, II, III, V, XI) Non-fibrillar FACIT (Fibril ... Type XIII, XVII) Microfibril forming (Type VI) Anchoring fibrils (Type VII) The five most common types are: Type I: skin, ...
Various types of collagens have individual roles and structures. Most collagen belongs to types 1, 2, and 3. Collagen consists ... Collagen loss is the gradual decrease of levels of collagen in the body. Collagen is the main structural protein found in the ... When collagen is lost in large amounts, it may cause wrinkles to emerge. Tobacco use can also result in slow collagen healing. ... When an individual consumes excessive amounts of sugar, the glycation process converts collagen into an unstable type 1, which ...
... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... Ehlers-Danlos type IV is most attributed to abnormalities in the reticular fibers (collagen Type III). Ehlers-Danlos syndrome, ... Ehlers-Danlos type IV is most attributed to abnormalities in the reticular fibers (collagen Type III). Without the ... Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene. ...
... type III procollagen, type IV collagen, laminin, tissue inhibitor of metalloproteinase, or prolyl hydroxylase?". Alcoholism: ... Tight collagen helix The most common collagen is type I collagen which makes up 90% of all collagen. It is found in all dermal ... show that the collagen hybridizing peptide probes can be used across species and collagen types (including type IV 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- ...
The collagen XVIII has three different isoforms. While each of the isoforms has the same C-terminus end, they have a varying ... Type XVIII collagen is a type of collagen which can be cleaved to form endostatin. The endostatin is from the c terminus end of ... This type of mutation particularly affects only one isoform of type XVIII collagen - the short isoform type, while the medium ... which codes for production of type XVIII collagen. It is speculated that the mutation of type XVIII collagen that occurs in ...
... this form of Ehlers Danlos is due to the mutation that produces less chains from the three chains that make up Type V Collagen ... Type V collagen is a part of the family of collagen proteins consisting of Collagen I- Collagen XXVIII. Collagen proteins are ... type V collagen preproprotein, CO5A1_HUMAN, and collagen type V alpha. Type V collagen can also be abbreviated to COLV or ... Type V collagen is a part of the Extracellular Matrix (ECM). Collagen V is gene expression modulated by TGF-β. Type V collagen ...
Type IV collagen is the major structural component of basement membranes, which contains two or three COL4A1 proteins. Thus, ... COL4A1 belongs to the type IV collagen family and contains three domains: a short N-terminal domain, a long triple-helical 7S ... It is ubiquitously expressed in many tissues and cell types. COL4A1 is a subunit of the type IV collagen and plays a role in ... "Chromosomal assignments of the genes coding for human types II, III, and IV collagen: a dispersed gene family". Proceedings of ...
"Duplication of type IV collagen COOH-terminal repeats and species-specific expression of alpha 1(IV) and alpha 2(IV) collagen ... "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 ... This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. The C- ...
Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a- ... It encodes the alpha chain of type XVII collagen. Collagen XVII is a transmembrane protein, like collagen XIII, XXIII and XXV. ... which in turn causes a type of osteogenesis imperfecta. Collagen, type XVII, alpha 1 has been shown to interact with Keratin 18 ... 2015). "Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial recurrent erosion dystrophy (ERED)". Hum. Mutat. ...
"COL21A1 collagen, type XXI, alpha 1". Entrez Gene: COL21A1. United States National Center for Biotechnology Information. Chou ... "Genomic organization and characterization of the human type XXI collagen (COL21A1) gene". Genomics. 79 (3): 395-401. doi: ... Collagen alpha-1(XXI) chain is a protein that in humans is encoded by the COL21A1 gene. The protein is an extracellular matrix ...
1987). "Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones". Eur. J. Biochem ... "Entrez Gene: COL6A1 collagen, type VI, alpha 1". Bertini E, Pepe G (2002). "Collagen type VI and related disorders: Bethlem ... "Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen". J. Biol. Chem. 272 (42): 26522-9 ... 1988). "Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen". Am. J. Hum. Genet. ...
Pihlajaniemi T, Tamminen M (1990). "The alpha 1 chain of type XIII collagen consists of three collagenous and four ... Latvanlehto A, Snellman A, Tu H, Pihlajaniemi T (2003). "Type XIII collagen and some other transmembrane collagens contain two ... Collagen XIII belongs to the transmembranous subfamily of collagens, like collagen XVII, XXIII and XXV. GRCh38: Ensembl release ... 2002). "The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and ...
Type XV collagen is known to be a tumor suppressor that can be used to understand tumor cells environment. Type XV collagen ... This gene encodes the alpha chain of type XV collagen, a member of the FACIT collagen family (fibril-associated collagens with ... "Epitope-defined monoclonal antibodies against multiplexin collagens demonstrate that type XV and XVIII collagens are expressed ... Hägg PM, Hägg PO, Peltonen S, Autio-Harmainen H, Pihlajaniemi T (June 1997). "Location of type XV collagen in human tissues and ...
This gene encodes one of the three alpha chains of type IX collagen, a collagen component of hyaline cartilage. Type IX ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have shown ... "Entrez Gene: COL9A1 collagen, type IX, alpha 1". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
Type XXVII collagen is related to the "fibrillar" class of collagens and may play a role in development of the skeleton. ... COL27A1 is a type XXVII collagen. It was discovered by James Pace. This gene appears to be turned on in cartilage, the eye, and ... Fibrillar collagens, such as COL27A1, compose one of the most ancient families of extracellular matrix molecules. They form ... Collagen alpha-1 (XXVII) chain (COL27A1) is a protein that in humans is encoded by the COL27A1 gene. ...
Three transcript variants have been identified for this gene. ARUP COL4A5 gene variant database LOVD Alport gene variant ... of type IV collagen in synovial capillaries by immunohistochemistry using a monoclonal antibody against human type IV collagen ... Collagen Type-IV collagen Alport syndrome GRCh38: Ensembl release 89: ENSG00000188153 - Ensembl, May 2017 GRCm38: Ensembl ... "Entrez Gene: COL4A5 collagen, type IV, alpha 5 (Alport syndrome)". Lemmink HH, Schröder CH, Monnens LA, Smeets HJ (1997). "The ...
This gene encodes the alpha chain of type XIX collagen, a member of the FACIT collagen family (fibril-associated collagens with ... other members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve ... collagen (COL12A1), alpha 1(IX) collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-q13". Genomics ... "Entrez Gene: COL19A1 collagen, type XIX, alpha 1". Yoshioka H, Zhang H, Ramirez F, et al. (1992). "Synteny between the loci for ...
2006). "The elongated first fibronectin type III domain of collagen XIV is an inducer of quiescence and differentiation in ... "Entrez Gene: COL14A1 collagen, type XIV, alpha 1 (undulin)". "COL14A1 - Collagen alpha-1(XIV) chain precursor - Homo sapiens ( ... 2005). "Collagen types XII and XIV are present in basement membrane zones during human embryonic development". J. Mol. Histol. ... Tono-Oka S, Tanase S, Miike T, Tanaka H (1996). "Transient expression of collagen type XIV during muscle development and its ...
This gene encodes one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective ... "Entrez Gene: COL6A2 collagen, type VI, alpha 2". "COLLAGEN, TYPE VI, ALPHA-2; COL6A2". www.omim.org. Retrieved 2023-10-13. ... "Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen". J. Biol. Chem. 272 (42): 26522-9 ... 1987). "Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones". Eur. J. Biochem ...
Greenspan DS, Lee ST, Lee BS, Hoffman GG (1992). "Homology between alpha 2(V) and alpha 1(III) collagen promoters and evidence ... related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type ... Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in ... type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This ...
... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... Type XI collagen also helps maintain the spacing and diameter of type II collagen fibrils. Type II collagen is an important ... Instead, another type of collagen chain replaces pro-alpha2(XI) to form type XI collagen in the vitreous of the eye. COL11A2 ... The COL11A2 gene produces one component of this type of collagen, called the pro-alpha2(XI) chain. Type XI collagen adds ...
... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... Unlike type VIII collagen, the other short chain collagen, type X collagen is a homotrimer. Type X collagen has a short triple ... "Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gene to chromosome 10". Eur. J. ... to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between ...
Seyer JM, Kang AH (1989). "Covalent structure of collagen: amino acid sequence of three cyanogen bromide-derived peptides from ... related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type ... Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in ... type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This ...
This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. This chain ... "Entrez Gene: COL9A2 collagen, type IX, alpha 2". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. Mutations ... "Entrez Gene: COL9A3 collagen, type IX, alpha 3". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
Blue cells = expressed in wild-type.. Gray triangles = other expression annotations only. (e.g. absence of expression or data ...
Find your collagen supplements today at ProHealth Longevity. ... Decreased collagen production can cause numerous age-related ... What Types of Collagen Are Included in Longevity Collagen Peptides? ProHealths Longevity Collagen Peptides contains types 1,2, ... Multi-Collagen Blend (Beef Collagen, Marine Collagen, Eggshell Membrane Collagen, Chicken Collagen). 20 g. †. ... Longevity Collagen + TYPE I, II, III, V, & X Hydrolyzed Collagen Peptides Unflavored Powder - 690 grams. SKU: PH618. ...
Improve your day-to-day wellness with NeoCell Super Collagen Peptides Type 1 & 3 - Unflavored 6.6 g 7 oz Pwdr from Swanson ... Get the building materials for growth and maintenance with Super Collagen Peptides Type 1 & 3 from NeoCell. Collagen is a ... When Super Collagen is taken internally, the body receives the raw materials it needs to supplement the collagen found in all ... Super Collagen is collagen protein that provides building materials for growth and maintenance of a healthy body. ...
Type III Collagen:. Also known as "fishtail collagen," this type of your health proteins helps make up about 5 percent of the ... Variety I Collagen:. Variety I collagen is regarded as the plentiful type of collagen inside our bodies-making up 90 percent of ... Kind II Collagen:. Also referred to as "cartilage collagen," sort II collagen helps make up about 50 percent of all of the ... Variety III collagen is usually located alongside sort I-providing framework to things like bloodstream and muscle groups. This ...
Type I, II, III, V, X - 90 ct , Shop Vitamins & Supplements products online at SalonCentric professional salon beauty supply. ... Features a blend of 5 types of collagen (I, II, III, V & X), 18 amino acids, and hydrolyzed collagen peptides for easy ... Multi Collagen Protein Capsules, Type I, II, III, V, X - 90 ct ... Multi Collagen Protein Capsules, Type I, II, III, V, X - 90 ct ... Codeage Multi Collagen capsules supplement features a blend of five types of collagen peptides sourced from high-quality ...
It is also found in many other tissues together with type I collagen. Peptides: Type I and Type III Collagen. Type III is ... Type IV EDS results from defects in the structure or synthesis of type III collagen. Increased amounts of type III collagen are ... The proportion of this pN-collagen is higher than for type I collagen, as practically all type III collagen fibers possess an ... Quantitatively, types I and III collagen are involved in hepatic fibrosis but type IV is also important in basement membranes. ...
Hydrolyzed Type I and III Collagen 10oz (283g) Note: Moisture could cause clumping of the product. Please make sure you open ... Collagen is a naturally occurring protein that supports healthy skin, bones, muscles, tendons, a ... Derived from grass-fed cows, Patriot Street Fighter Collagen Peptides contains Type I and Type III collagen that has been ... Patriot Street Fighter Collagen Peptides - Hydrolyzed Type I and III Collagen 10oz (283g) (3-Pack) ...
Hydrolyzed Type I and III Collagen 10oz (283g) Note: Moisture could cause clumping of the product. Please make sure you open ... Hydrolyzed Type I and III Collagen.. Our premium bovine collagen powder uses lab-verified Type I and Type III collagen. The ... The most important and abundant types of collagen inside your body are Type I and Type III collagen.. Although your skin ... Groovy Bee® Collagen Peptides - Hydrolyzed Type I and III Collagen 10oz (283g) ...
Collagen Type 1 & 3 June 6, 2015. /in collagen type 1 & 3 /by PureCollagen. *Do you want to look younger? ... We at Pure Collagen.US will be offering products that help set back the biological clock with your skin appearance.. You will ... www.purecollagen.us/wp-content/uploads/2015/11/pure-collagen-logo.png PureCollagen2015-06-06 08:11:212022-06-09 20:28:32 ... https://www.purecollagen.us/wp-content/uploads/2015/11/pure-collagen-logo.png 0 0 PureCollagen https:// ...
Fish collagen differs from bovine or porcine sourced-collagen because it contains higher amounts of the amino acids, Glycine ... Marine Collagen, provides 9.4 grams of protein per serving, and 8 out of 9 essential amino acids. ... and Proline, and is absorbed into the body faster.* Fish collagen peptides are comprised of two t ... Fish collagen peptides are comprised of two types of collagen, types I & III. Type I and Type III collagen benefits include ...
... type 1 and type 3 hydrolyzed collagen peptides. Collagen is a complex structural protein that maintains strength and f... ... type 1 and type 3 hydrolyzed collagen peptides. Collagen is a complex structural protein that maintains strength and ... Super Collagen Type 1 & 3 NeoCell 198 grams NeoCell Super Collagen Powder, ... Super Collagen Type 1 & 3 NeoCell 198 grams NeoCell Super Collagen Powder, ...
... skin and nails as part of a daily beauty regimen with collagen peptides types I & III that are sourced form grass-fed cows. ... Bluebonnet Nutrition Collagen Refreshers Hydrolzyed Collagen Powder Unflavored -- 10.58 oz * Shop all Bluebonnet Nutrition ... Collagen peptides help to replenish nutrients lost over time by boosting collagen production, which helps to strengthen hair ... Bluebonnets Hydrolyzed Collagen Powder is carefully crafted to revive hair, ...
III With high-purity, bioactive collagen peptides derived from grass-fed bovine to help support healthy skin Unflavored ... 6.6 grams of collagen peptides type I + III. With high-purity, bioactive collagen peptides derived from grass-fed bovine to ... 6.6 grams of collagen peptides type I + ... BEAUTIFUL ALLY® COLLAGEN TYPES I & III Caplets. Size 30 ...
Among the 28 different types of collagen identified, types I, II, and III are the most abundant and significant. Each type of ... Collagen is a vital protein that constitutes a significant portion of the human bodys structural components, providing ... Type III Collagen: Type III collagen is commonly found alongside type I collagen in various tissues, including skin, blood ... Among the 28 different types of collagen identified, types I, II, and III are the most abundant and significant. Each type of ...
Type III - Crucial for the structure of muscles, organs and arteries, this type of collagen is generally found in the skin, ... While there are at least sixteen types of collagen in the body, there are 4 primary types that impact your health:. *Type I - ... there are 4 main types that impact your health:. *Type I - This type of collagen is made of densely-packed fibers that supply ... Type III - Important for the structure of muscles, organs and arteries, this kind of collagen is usually discovered in the skin ...
Supplementary collagen can help support the bodys own natural collagen stores that may diminish due to age or other factors.* ... Collagen is also a contributing factor in maintaining healthy hair and skin. NatureWise Enhanced C ... Collagen is an important component of healthy connective tissues like cartilage and ligaments. ... Hydrolyzed Bovine Collagen Peptides - Sourced from grass-fed cows, our collagen type I and type III peptides provide support ...
... and tendons of cows that provide type I and III collagen. Collagen is well known as a natural treatment for skin and promote ... Moreover, Collagen Type I, III and II support your joint healthier and also your hair, skin and nail as well. ... Collagen Type I, II &III Glucosamine, MSM, Chondroitin and the new Boron and Hyaluronic Acid helps maintain healthy structure, ... Collagen Type II is the most abundant protein. It gives our skin strength and elasticity, along with replacing dead skin cells ...
Native dog collagen type I and III from tail tendon. No cross-reactivity towards dog collagen type IV, V and other god plasma ... Native dog collagen type I and III from tail tendon. No cross-reactivity towards dog collagen type IV, V and other god plasma ... 775 Rabbit anti-canine collagen type I and III polyclonal antibody 1 ml ...
III native porcine collagen from pigs tissue, 10 mg. Highest quality collagen for research use. It is widely used as a thin ... Collagen Type I and III, Canine, 10 mg Purified type I & III canine collagen. Type I collagen is the most abundant collagen and ... Collagen Type III, Bovine, 10 mg Purified type III bovine collagen. 10 mg. Lyophilized. Type III collagen is the second most ... Porcine collagen type I - 45%. Porcine collagen type III - 45%. Porcine collagen type IV - 10%. Porcine collagen type V - below ...
OptiCol™ Human Collagen Type III is initially produced as procollagen, a protein consisting of three pro-α1(III) chains that ... OptiCol™ Human Collagen Type III (1 mg/ml), 10 mg. Code. Description. Price. Qty. ... 2. Dilute Type III collagen solution with a 0.01 M HCl solution water to ~50 to 100 μg/ml (~1:10). ... 4. Add appropriate amount of diluted Type III Collagen to the culture surface ensuring that the entire surface is coated. ...
But with our Super Collagen + C, you can reveal your inner beauty. This clinically studied formula combines Hydrolyzed Collagen ... our bodys collagen gets depleted, which can lead to many common signs of aging. ... Joint Support 6 g Collagen Dietary Supplement Grass-Fed Paleo-Friendly + Gluten-Free Igen - Non-GMO Tested Certified Paleo ... Hydrolyzed Bovine Collagen 6 g † † Daily Value (DV) not established. ...
Primal Multi Collagen is the most convenient way to give your body all the benefits of the essential collagen types I, II, III ... 5 KEY COLLAGEN TYPES* To ensure you get the most from your daily collagen, weve included 5 collagen types (I, II, III, X, and ... FISH COLLAGEN. Type I & III hydrolyzed collagen proteins, the two most commonly-found types in the human body, work together in ... MULTI COLLAGEN CAPSULES EASY-TO-TAKE COLLAGEN CAPSULES Formulated with a blend of 5 hydrolyzed collagen types, our Multi ...
... on immobilized human collagen type III with cross-absorption using immobilised human plasma proteins and human collagen type I ... Detection of human collagen type III by ELISA, Histochemistry (frozen sections). Immunostaining of ECM in cell culture. Not ... Overall process is designed to obtain a high purity type-specific antibody to native 3D collagen. ... Binds native 3D epitopes of human collagen type III. Affinity purification ...
Types I & III collagen can be taken together. Types I & III collagen comprises over 90% of the collagen in the body. Types I & ... III collagen contains 19 amino acids (proteins). Type II collagen should be taken SEPERATELY from Types 1 & 3 to ensure ... Collagen Peptides Type I & III: Muscles, Bones, Tendons, Ligaments, Anti-Aging, Hair, Skin, Nails. Types 1 & 3 collagen ... Type II collagen consists of the fluids within the cartilage, joints and supports their functions. Type II collagen is produced ...
Read Applied Nutrition Liquid Collagen Skin Revitalization reviews from M&S Customers. ... Applied Nutrition Liquid Collagen Skin Revitalization on sale now at Muscle & Strength! ... Hydrolyzed Collagen (Type I & III). 4000 mg. †. Antioxidant Blend. 3030 mg. †. Blueberry (Vaccinium angustifolium) Juice ... Liquid Collagen Skin Revitalization. Liquid Collagen Skin Revitalization Collagen may be the most important element of human ...
BioCell Collagen is a clinically researched, multi-patented nutraceutical ingredient that promotes active joints and younger ... Support skin & joint collagens (type I, II & III). *Reduce wrinkles and fine lines ... BioCell Collagen®, a holistic approach to more active joints * BioCell Collagen®, a holistic approach to skin beauty from ... naturally occurring matrix of hydrolyzed type II collagen (60%), chondroitin sulfate (20%), and hyaluronic acid (HA) (10%). The ...
... super collagen type 1and 3 powder Collagen (collagen hydrolysate) is a complex structural protein that maintains strength and ... Super collagen Type I and III is 100% pure collagen protein that provides building materials for growth and maintenance of a ... Neocell super collagen powder, type 1 and 3 - 7 oz. Neocell super collagen powder, type 1 and 3 - 7 oz ... Decrease quantity for Neocell super collagen powder, type 1 and 3 - 7 oz Increase quantity for Neocell super collagen powder, ...
  • Multi Collagen Protein Complex: Hydrolyzed Bovine Collagen Peptides, Egg Shell Membrane Collagen, Organic Ashwagandha Root Extract (Withania somnifera), Hydrolyzed Fish Collagen Peptides (Cod, Snapper), Chicken Bone Broth, Organic Amla Berry Powder (Phyllanthus emblica). (saloncentric.com)
  • Our premium bovine collagen powder easily dissolves in both cold and hot beverages (up to 120 degrees) and can be added to shakes, smoothies, fruit juices, teas, and coffees. (brighteonstore.com)
  • Our premium bovine collagen powder uses lab-verified Type I and Type III collagen. (healthrangerstore.com)
  • The collagen powder is then carefully hydrolyzed for optimal digestion and absorption. (healthrangerstore.com)
  • Our hydrolyzed collagen powder, contains no odor or taste, is easy to digest, and readily dissolves in liquids or soft foods. (vitalnutrientspro.co)
  • Illuminate your inner beauty with NeoCell Super Collagen Powder, type 1 and type 3 hydrolyzed collagen peptides. (nutrientsdiscovery.com)
  • Super Collagen Powder is unflavored and makes a great addition to your morning smoothie, in a warm or cold beverage, or added to your favorite recipe. (nutrientsdiscovery.com)
  • COLLAGEN POWDER: A combination of Types 1 & 3 hydrolyzed collagen peptides, Super Collagen Powder provides some of the necessary building blocks to produce collagen in an easy to mix, unflavored powder. (nutrientsdiscovery.com)
  • JOINT SUPPORT: Super Collagen powder supports joint flexibility. (nutrientsdiscovery.com)
  • COLLAGEN DRINK: Simply dissolve 1 scoop of Super Collagen Powder in your favorite beverage, smoothie or add to a recipe and consume daily. (nutrientsdiscovery.com)
  • Bluebonnet's Hydrolyzed Collagen Powder is carefully crafted to revive hair, skin and nails as part of a daily beauty regimen with collagen peptides types I & III that are sourced form grass-fed cows. (vitacost.com)
  • Plus, it promotes comfortable digestion of beans, dairy, soy, grains, and meat - covering the spectrum of foods you may wish to mix your collagen powder into. (naturewise.com)
  • Multi-sourced collagen powder. (bodyenergyclub.com)
  • Organika®'s Full Spectrum Collagen Type 1, 2, 3 powder is an all-encompassing superfood that provides all the main types of collagen: type 1, 2, and 3. (bodyenergyclub.com)
  • But our Super Collagen Powder has been specifically formulated to support your beauty from the inside and promote your body's own collagen production. (mybigcommerce.com)
  • Horbaach has used years of industry experience to craft a super Multi Collagen Protein Powder. (horbaach.com)
  • Our Multi-Collagen powder is unflavored making it perfect for any coffee, drink, shake or baking recipe. (horbaach.com)
  • Our ultra powder has officially raised the bar for Collagen Innovation. (horbaach.com)
  • NeoCell Super Collagen Powder, which contains hydrolyzed collagen peptides of types 1 and 3, can help you reveal your inner beauty. (beautyfly.pk)
  • Collagen peptide powder made from grass-fed, hydrolyzed collagen peptides is available in a variety of packages. (beautyfly.pk)
  • Collagen powder that is safe for use around animals: There are no soy or artificial flavorings or preservatives in our NeoCell Super Collagen Peptides powder. (beautyfly.pk)
  • NeoCell Super Collagen Powder, Skin, muscle, tendon, ligament, and bone aging can be caused by collagen cross-linking and depletion as we grow older. (beautyfly.pk)
  • There is no taste to Super Collagen Powder, which makes it a fantastic addition to your morning smoothie, a warm or cold beverage, or a dish. (beautyfly.pk)
  • Boost your beauty and wellness with Built By Nature Grass-Fed Collagen Powder. (builtbynature.com)
  • Experience the myriad benefits of collagen with Built By Nature Collagen Powder, the natural choice for comprehensive wellness. (builtbynature.com)
  • Our collagen peptides powder comes from the purest sources and goes through a robust hydrolization process to produce the best-tasting collagen powder. (livezeal.com)
  • Our powder contains 100% hydrolyzed collagen which allows larger protein amino acids/molecules to be converted into smaller units that are easily absorbed by the human body. (wholesome-wellness.com)
  • Our Multi-Collagen Protein Powder will help Rejuvenate your body one scoop at a time. (wholesome-wellness.com)
  • Nourish your inner beauty with our Super Collagen Powder. (vitaminsmenu.com)
  • This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. (wikipedia.org)
  • Also referred to as "cartilage collagen," sort II collagen helps make up about 50 percent of all of the proteins located in cartilage. (htccommunity.org)
  • This specialised method of collagen offers cartilage its flexibility so it helps safeguard your joint parts from wear. (htccommunity.org)
  • Collagen is a vital healthy proteins that offers framework and power to many people different cells within our bodies-including our your bones, skin area, muscles, ligaments, and cartilage. (htccommunity.org)
  • Collagen is an important component of healthy connective tissues like cartilage and ligaments. (naturewise.com)
  • By supplementing with additional collagen, such as the bovine variety found in this NatureWise product, your body has more of the building blocks it needs to keep its cartilage and connective tissues in good shape. (naturewise.com)
  • Type II collagen is the principal collagen present in cartilage, which is the connective tissue that cushions and supports joints. (bemewellness.com)
  • Type II collagen is frequently used in supplements to promote joint health, alleviate inflammation, and facilitate cartilage repair. (bemewellness.com)
  • It comprises roughly 90% of your body's collagen and supports skin, bone, teeth, tendon and cartilage health. (bestliquidcollagen.com)
  • Type II - More loosely jam-packed than Type I, these collagen fibers are mostly present in flexible cartilage and serve as a cushion for the joints. (bestliquidcollagen.com)
  • Undenatured Type Ⅱ is a kind of undenatured type II collagen extracted from animal cartilage tissues with the complete retention of the triple helix structure of collagen. (chondroitinpowder.com)
  • The evidence for an autoimmune etiology includes pathological findings of infiltrating T cells, the presence of antigen-antibody complexes in affected cartilage, cellular and humoral responses against collagen type II and other collagen antigens, and the observation that immunosuppressive regimens most often suppress the disease. (medscape.com)
  • Various studies find circulating antibodies to cartilage-specific collagen types II, IX, and XI to be present in 30%-70% of patients with relapsing polychondritis. (medscape.com)
  • Autoantibodies to minor cartilage-specific collagens (ie, types IX and XI) have been described. (medscape.com)
  • There are three types of cartilage in the body: hyaline, elastic, and fibrocartilage. (lu.se)
  • However, the main collagen is type II that occurs in the articular cartilage. (lu.se)
  • It is the collagen that gives the cartilage its elasticity. (lu.se)
  • When Super Collagen is taken internally, the body receives the raw materials it needs to supplement the collagen found in all of these areas. (swansonvitamins.com)
  • You may also get Collagen Supplement. (htccommunity.org)
  • Codeage Multi Collagen capsules supplement features a blend of five types of collagen peptides sourced from high-quality sources and 18 amino acids. (saloncentric.com)
  • This multi collagen supplement formula also offers organic ashwagandha and amla berry extracts for added antioxidant support. (saloncentric.com)
  • This multi collagen capsules supplement is manufactured in a cGMP-certified facility in the USA. (saloncentric.com)
  • Getting supplemental collagen in your diet is easy with NatureWise's unflavored supplement. (naturewise.com)
  • By understanding the distinct roles of types I, II, and III collagen, you can make an informed decision about the most suitable liquid collagen supplement to meet your individual needs and promote optimal health. (bemewellness.com)
  • Enter Liquid Biocell ® , an innovative liquid collagen supplement for general much better health. (bestliquidcollagen.com)
  • Liquid Biocell ® is a medically crafted supplement containing high levels of natural collagen to help replenish what your body is struggling to produce. (bestliquidcollagen.com)
  • Meet complete: this all-encompassing collagen supplement makes beauty, gut health, and joint support easy as 1, 2, 3. (bodyenergyclub.com)
  • There are a variety of supplement brands that carry Collagen products in different forms. (horbaach.com)
  • Though, the more professional supplement brands use high quality innovation to create Hydrolyzed Collagen products. (horbaach.com)
  • Another study found reduced dryness and wrinkles in women who consumed a chicken-derived collagen supplement. (skinnybean.co)
  • Introducing Liquid Biocell ® , a revolutionary liquid collagen supplement for total much better health. (bestliquidcollagen.com)
  • Liquid Biocell ® is a scientifically engineered supplement consisting of high levels of natural collagen to help renew what your body is struggling to produce. (bestliquidcollagen.com)
  • Hydrolyzed Collagen Peptides: This high-quality collagen supplement features Type 1 & 3 peptides, hydrolyzed for optimal absorption and utilization by your body, offering a powerful boost to your overall wellness. (builtbynature.com)
  • This all-natural supplement aids your body's collagen production to maintain youthful vibrancy and physical wellbeing. (builtbynature.com)
  • Made with powerful hair skin and nails vitamins such as Biotin, Vitamin C, and Hyaluronic complex, this collagen supplement is perfectly formulated to strengthen your hair follicles, increase keratin proteins, and increase skin elasticity from the inside out. (livezeal.com)
  • The Dietary Supplement and Prescription Medication (DSQ) Section of the Sample Person (SP) Questionnaire, collects information on: 1) prescription and non-prescription dietary supplements (DS), 2) non-prescription antacids, 3) prescription medications, and 4) low-dose aspirin. (cdc.gov)
  • The NHANES 2017-2018 dietary supplement questions are similar to the NHANES 1999-2016 and NHANES III 1988-1994 questions, although, there have been additional questions added over the cycles. (cdc.gov)
  • Among the 28 different types of collagen identified, types I, II, and III are the most abundant and significant. (bemewellness.com)
  • These supplements contain different types of collagen sourced from natural sources like bovine, poultry, avian, and marine. (skinnybean.co)
  • There are several different types of collagen, but type-I collagen is the most common. (lu.se)
  • Mutations can exist in the genes that encode different types of collagen (eg, type I, III, or V) or collagen-modifying enzymes (eg, lysyl hydroxylase, a collagen-cleaving protease). (msdmanuals.com)
  • Supports strong and healthy hair and nails - High collagen intake can add volume to your hair. (brighteonstore.com)
  • NeoCell collagen supplements support healthy collagen formation for youthful skin, healthy hair and nails. (nutrientsdiscovery.com)
  • Collagen peptides help to replenish nutrients lost over time by boosting collagen production, which helps to strengthen hair and nails while supporting the skin's hydration balance and elasticity to counteract visible signs of aging. (vitacost.com)
  • Similar to how collagen can help with maintaining bone strength, it may also encourage stronger hair and nails. (naturewise.com)
  • Because of this additional support against breakage, collagen supplements can aid in achieving naturally long hair and nails. (naturewise.com)
  • We've included hydrolyzed collagen to deliver essential multi collagen peptides to help your hair and nails stay healthy. (primalharvest.com)
  • great for skin elasticity and increased strength of hair and nails, can be found in bovine and marine collagen. (bodyenergyclub.com)
  • Bovine Collagen provides a clean type 1 and 3 collagen, giving you thick hair, strong nails, supple skin, healthy joints, as well as supporting a healthy digestive tract. (bodyenergyclub.com)
  • The type 1 collagen in Marine collagen also supports fuller hair, stronger nails, and youthful skin. (bodyenergyclub.com)
  • Formulated to boost your beauty from the inside out, our hydrolyzed Super Collagen helps you feed your healthy beauty and enjoy radiant, youthful skin and healthy hair and nails. (mybigcommerce.com)
  • With a strong presence in hair, skin, nails and joints of men and women, Collagen has become the most popular ingredient in Beauty Products. (horbaach.com)
  • Hydrated NeoCell Collagen promotes the health of your hair, scalp, and nails so that you radiate beauty from the inside out. (beautyfly.pk)
  • collagen supplements from NeoCell help to keep skin, hair, and nails looking youthful and healthy. (beautyfly.pk)
  • Pure Collagen Hydrolysate + Biotin + Vitamin C + Hyaluronic Acid - Zeal Naturals Multi Collagen Protein is the ultimate collagen supplements for women and men to for joint support, stronger nails, and vibrant skin with the added vitamin C, biotin, and hyaluronic acid. (livezeal.com)
  • Healthy Skin, Hair & Nails: Collagen is the main protein that gives our skin elasticity. (nowketo.com)
  • With advanced collagen supplements from ForestLeaf , you can help minimize the effects of aging in your skin, hair and nails as you strengthen your bones and joints. (nowketo.com)
  • Collagen is the protein that gives our skin elasticity, makes hair and nails strong and maintains bone and joint strength. (nowketo.com)
  • Collagen is the main protein in the body that makes up our skin, hair and nails. (nowketo.com)
  • Lack of Collagen causes brittle and discolored nails that break easily. (wholesome-wellness.com)
  • COLLAGEN DEPLETION: The primary structural component for all tissues in the body, collagen supports healthy skin, hair, nails and joint. (vitaminsmenu.com)
  • Supports the growth of firm and youthful-looking skin - Since collagen makes up 75% of your skin's dry weight, supplementing with collagen can help maintain your skin's natural elasticity and moisturization. (brighteonstore.com)
  • Type I and Type III collagen benefits include promoting healthy hair and nail growth, improving skin elasticity and hydration, as well as supporting joint health and function, and bone strength. (vitalnutrientspro.co)
  • Collagen is one of the key components that helps skin retain its elasticity. (naturewise.com)
  • Liquid collagen supplements that include type III collagen can help support the health of blood vessels, skin, and internal organs, improving their overall resilience and elasticity. (bemewellness.com)
  • Collagen is the most abundant form of protein in our body, providing it with strength, elasticity, and tone. (bodyenergyclub.com)
  • For example, research has demonstrated improved skin elasticity in women who took collagen for eight weeks. (skinnybean.co)
  • As we age, collagen cross-linking and depletion can lead to common signs of aging in the skin, muscles, tendons, ligaments, and bones. (nutrientsdiscovery.com)
  • Collagen is the most abundant, naturally occurring protein found in the human body and is the building foundation for your cells and connective tissues, making it necessary for healthy hair, skin, nail, muscles, bones, joints, tendons and ligaments. (wholesome-wellness.com)
  • Marine collagen is typically high in glycine, which positively supports insulin and blood sugar management. (prohealth.com)
  • Effects of marine collagen peptides on glucose metabolism and insulin resistance in type 2 diabetic rats. (prohealth.com)
  • You will discover sort I Liquid Marine Collagen in food products like bone fragments broth, body organ lean meats, salmon, crazy activity, leafy green veggies like kale and kale, in addition to citrus fruit many fruits. (htccommunity.org)
  • Marine Collagen, provides 9.4 grams of protein per serving, and 8 out of 9 essential amino acids. (vitalnutrientspro.co)
  • Organika Marine Collagen is sustainably sourced from Codfish, providing clean type 1 collagen free from hormones and antibiotics. (bodyenergyclub.com)
  • Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. (wikipedia.org)
  • It is also found in many other tissues together with type I collagen. (gotoh.com.br)
  • This process breaks down collagen into smaller pieces so that your body can more easily use them as building blocks to rejuvenate your aging tissues. (healthrangerstore.com)
  • Collagen is a vital protein that constitutes a significant portion of the human body's structural components, providing essential support and strength to various tissues. (bemewellness.com)
  • Type I collagen offers strength, structure, and flexibility to these tissues, making it a critical component in maintaining their integrity. (bemewellness.com)
  • Type III collagen is commonly found alongside type I collagen in various tissues, including skin, blood vessels, and organs such as the lungs, liver, and spleen. (bemewellness.com)
  • Liquid collagen is highly bioavailable, meaning it is easily absorbed and utilized by the body, providing targeted support for the specific tissues that require it. (bemewellness.com)
  • Type I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. (mdbioproducts.com)
  • Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. (mdbioproducts.com)
  • The unique synergy of the molecules found in BioCell Collagen offers multi-dimensional nutritional support for the health of connective tissues such as skin, joint, tendon and ligament. (nutraingredients.com)
  • Type 2 collagen helps build strong joints and connective tissues. (bodyenergyclub.com)
  • Cells grown on porous collage-coated beads under fluid shear conditions in rotating wall vessel bioreactors differentiate into 3-D architectures resembling both the morphologic and physiologic function of in vivo tissues. (cdc.gov)
  • The design of the RWV bioreactor is based on the principle that organs and tissues function in a 3-D environment and that this spatial context is necessary for development of cultures that more realistically act like in vivo tissues and organs ( 25 ). (cdc.gov)
  • 1% sodium bicarbonate (NaHCO ) dis- ions in tissues such as collagen or muscle. (who.int)
  • Up to 30% of all the protein in your body consists of collagen, which can be found in your skin, bones, muscles, tendons, blood vessels and digestive system. (brighteonstore.com)
  • Type III collagen is especially crucial for maintaining the strength and flexibility of blood vessels, which is why it is often associated with cardiovascular health. (bemewellness.com)
  • Incorporating liquid collagen supplements into your daily routine can offer numerous health benefits, including improved skin appearance, enhanced joint function, and strengthened blood vessels. (bemewellness.com)
  • Type III - Crucial for the structure of muscles, organs and arteries, this type of collagen is generally found in the skin, intestinal tracts, blood vessels and lungs. (bestliquidcollagen.com)
  • Furthermore, collagen peptides contain proline, an amino acid that is crucial for maintaining healthy blood vessels and overall cardiovascular health. (groovybee.com)
  • Collagen is the most abundant protein your body makes. (prohealth.com)
  • Type III is abundant in the intestines. (gotoh.com.br)
  • The most important and abundant types of collagen inside your body are Type I and Type III collagen. (healthrangerstore.com)
  • Of all the proteins in your body, collagen is the most abundant, accounting for about a third of your natural peptides. (bestliquidcollagen.com)
  • Type I collagen is the most abundant collagen and is found. (mdbioproducts.com)
  • This effective nutraceutical is abundant in all-natural collagen and renewing phytonutrients developed to rejuvenate your body's collagen stores. (bestliquidcollagen.com)
  • Collagen offers protection from bone loss and supports healthy bones and joints to allow you to move more freely and painlessly. (prohealth.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)
  • Supports healthy bones and joints - Having adequate levels of collagen in your body can help support healthy bones and joints. (brighteonstore.com)
  • Just like with your joints, as the body's natural collagen levels deplete over time, your bones may become more susceptible to damage. (naturewise.com)
  • This product is readily available in numerous types depending on your body's specific requirements, but each includes the exact same nourishing compound of collagen peptides together with chondroitin sulfate and hyaluronic acid (both known to support healthy skin and joints). (bestliquidcollagen.com)
  • Designed to support optimal daily performance, this Multi Collagen is formulated to help support healthy bones and joints. (primalharvest.com)
  • BioCell Collagen is a clinically researched, multi-patented nutraceutical ingredient that promotes active joints and younger looking skin. (nutraingredients.com)
  • Collagen supplements have become popular as a way to replenish collagen levels and support healthy skin, joints, and bones. (skinnybean.co)
  • This product is offered in a number of types depending on your body's particular needs, but each contains the very same nourishing substance of collagen peptides in addition to chondroitin sulfate and hyaluronic acid (both understood to support healthy skin and joints). (bestliquidcollagen.com)
  • Thus, 3 joints per finger exist, all of which have significant motion and require stabilization to prevent subluxation and dislocation. (medscape.com)
  • Codeage collagen supplements also exist as collagen powders dietary supplements. (saloncentric.com)
  • Liquid collagen supplements containing type I collagen can be beneficial for promoting healthy skin, improving its appearance, and reducing signs of aging such as wrinkles and fine lines. (bemewellness.com)
  • Liquid collagen supplements containing type II collagen can be particularly helpful for individuals suffering from joint pain or arthritis, as they are more easily absorbed by the body and can provide targeted support to the affected areas. (bemewellness.com)
  • These Collagen types are found naturally in many food sources and added to nutritional supplements. (horbaach.com)
  • Collagen supplements should be considered as part of a comprehensive approach to health and wellness. (skinnybean.co)
  • Maintain and improve the moisture and fullness of your skin with our advanced collagen dietary supplements. (nowketo.com)
  • NeoCell Super Collagen supplements are formulated to support skin health, and your radiant beauty inside and out. (vitaminsmenu.com)
  • Bones are made, in part, of collagen. (naturewise.com)
  • Supporting your bones with added dietary collagen can help to encourage healthy and strong bones throughout your life. (naturewise.com)
  • Among the significant foundation of all the body's systems, collagen plays an essential role in supporting your skin, bones, arteries and the majority of your organs by keeping them structurally sound. (bestliquidcollagen.com)
  • Collagen (which originates from the Greek word kólla, or glue) functions as a sort of binding agent that helps keep your bones and numerous organ systems together. (bestliquidcollagen.com)
  • One of the significant building blocks of all the body's systems, collagen plays an essential function in supporting your skin, bones, arteries and most of your organs by keeping them structurally sound. (bestliquidcollagen.com)
  • Most of it is type I collagen, found in bones and tendons. (kidshealth.org)
  • Collagen is a large component of connective tissue in the body which is found in tendons that connect our muscles to our bones. (nowketo.com)
  • Start taking collagen to ensure strong and healthy bones today! (wholesome-wellness.com)
  • The fingers (index through small fingers) are composed of 3 bones each and are all associated with a single metacarpal. (medscape.com)
  • Collagen is the most numerous proteins in our body, accounting for about 1-thirdly of the healthy proteins seen in mammals. (htccommunity.org)
  • Also known as "fishtail collagen," this type of your health proteins helps make up about 5 percent of the collagen located in mammals. (htccommunity.org)
  • According to a study that appeared in the journal Skin Pharmacology and Physiology, collagen peptides can help nourish your skin and support your body's natural production of proteins that support optimal skin function and integrity, such as elastin and fibrillin. (healthrangerstore.com)
  • Affinity purification on immobilized human collagen type III with cross-absorption using immobilised human plasma proteins and human collagen type I, II, IV and IV. (yoproteins.com)
  • Collagen types contain different proteins that serve separate purposes within the body. (3naturalbionutrition.com)
  • No cross-reactivity towards dog collagen type IV, V and other god plasma proteins. (yoproteins.com)
  • Collagen is also one of the major proteins found in our nail beds. (wholesome-wellness.com)
  • Aggrecanase activity has been shown to be associated with joint deterioration and symptomatic disease through the degradation of extracellular matrix proteins, such as type III collagen. (nordicbioscience.com)
  • Our hydrolyzed collagen can give your body the building blocks it needs to make collagen or other proteins. (vitaminsmenu.com)
  • Antibodies are immune system proteins that normally attack foreign substances such as bacteria or viruses, but in people with Goodpasture syndrome, they target alpha3(IV) collagen chains. (medlineplus.gov)
  • Maintains healthy muscles and tendons - As an excellent source of the amino acids glycine and arginine, collagen peptides can support healthy muscle tissue. (brighteonstore.com)
  • Purified Bovine Collagen Type I (Atelocollagen) from bovine tendons. (mdbioproducts.com)
  • Purified native collagen type I and III from tail tendons of the mouse, 5 mg. (mdbioproducts.com)
  • One of the amino acids found in collagen, glycine, can help improve digestion by increasing stomach acid. (prohealth.com)
  • Super Collagen is enzymatically processed into its amino acid form with a very low molecular weight, which can be utilized 100% by the body. (swansonvitamins.com)
  • Features a blend of 5 types of collagen (I, II, III, V & X), 18 amino acids, and hydrolyzed collagen peptides for easy absorption. (saloncentric.com)
  • Its metabolism can be monitored by assaying the amino-terminal propeptide of type III procollagen (PIIINP). (gotoh.com.br)
  • Supports a healthy gastrointestinal tract - Collagen peptides contain amino acids that support a healthy gastrointestinal tract, such as glycine, glutamic acid, and proline. (brighteonstore.com)
  • Supports healthy cardiovascular function - Collagen peptides contain an amino acid called proline, which plays an important role in maintaining optimal cardiovascular health. (brighteonstore.com)
  • Collagen also contains the amino acid glycine, which can support healthy metabolism. (brighteonstore.com)
  • At least 18 different essential and non-essential amino acids are present in collagen peptides, all of which can significantly benefit your general health and well-being. (healthrangerstore.com)
  • Fish collagen differs from bovine or porcine sourced-collagen because it contains higher amounts of the amino acids, Glycine and Proline, and is absorbed into the body faster. (vitalnutrientspro.co)
  • AstraGin ® works well alongside collagen thanks to its support for amino acid absorption. (naturewise.com)
  • These digestive enzymes help your body break down the essential amino acids in collagen to help you get the most out of your collagen routine. (primalharvest.com)
  • Most of these variants change single protein building blocks (amino acids) in a region where the alpha3(IV) collagen chain combines with other collagen IV chains. (medlineplus.gov)
  • M.J. Nielsen, M.A. Also, the major triple helical domain, 1029 residues in humans, is a little longer than the same domain in type I and II collagen molecules containing 1014 residues. (gotoh.com.br)
  • Super Collagen uses an advanced enzymatic hydrolyzation process to convert large collagen molecules into small peptides that are bioactive in the body. (fredmeyer.com)
  • This chain combines with two other types of alpha (IV) chains (the alpha4 and alpha5 chains) to make alpha345(IV) collagen molecules. (medlineplus.gov)
  • According to studies, protein in the form of collagen peptides is more satiating than many other types of protein. (brighteonstore.com)
  • Collagen peptides are a bioavailable form of collagen produced through a process called hydrolysis. (healthrangerstore.com)
  • Type I collagen is the most prevalent form of collagen in the body, accounting for approximately 90% of the total collagen content. (bemewellness.com)
  • Two kinds of collagen and AstraGin ® combine to create support for complete wellness from the inside out. (naturewise.com)
  • What Are the Different Kinds of Collagen? (kidshealth.org)
  • Our bodies have many different kinds of collagen. (kidshealth.org)
  • Chicken Bone Broth is naturally high in type 2 collagen, as well as hyaluronic acid (HA) and glycosaminoglycans (GAGs). (bodyenergyclub.com)
  • Fish-sourced collagen types 1 & 3 peptides, hyaluronic acid, and a number of vitamins and minerals nourish your inner beauty for strong, radiant, younger-looking skin. (vitaminsmenu.com)
  • Loss of collagen is believed to be the primary cause of fine lines and wrinkles that occur in naturally aged skin. (muscleandstrength.com)
  • Derived from grass-fed cows, Patriot Street Fighter Collagen Peptides contains Type I and Type III collagen that has been hydrolyzed for easier digestion and absorption. (brighteonstore.com)
  • Hydrolyzed Bovine Collagen Peptides - Sourced from grass-fed cows, our collagen type I and type III peptides provide support for the body's natural collagen stores that may diminish with age or due to other life factors. (naturewise.com)
  • Organika Bovine Collagen is sourced from North American grass-fed cows, raised free from hormones and antibiotics. (bodyenergyclub.com)
  • Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: A randomised controlled trial. (prohealth.com)
  • 3.0.CO;2-9, "Diagnosis, natural history, and management in vascular Ehlers-Danlos syndrome", "Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries", "Characterization of human type III collagen expressed in a baculovirus system. (gotoh.com.br)
  • Compared with collagen products on the market, the biggest difference is that the existing collagen product is essentially macromolecular collagen after enzymatic hydrolysis, A collagen peptide whose tertiary and quaternary structure has been completely destroyed, The average molecular weight is below 10000 Da. (chondroitinpowder.com)
  • Formulated to support radiant beauty from the inside out, NeoCell Collagen is, non-GMO, paleo friendly and gluten free. (nutrientsdiscovery.com)
  • 2. König D, Oesser S, Scharla S, Zdzieblik D, Gollhofer A. Specific Collagen Peptides Improve Bone Mineral Density and Bone Markers in Postmenopausal Women-A Randomized Controlled Study. (prohealth.com)
  • Sourced from high-quality, grass-fed hydrolyzed collagen bovine, free-range chicken bone broth, hydrolyzed fish collagen peptides, and eggshell collagen for quality and purity. (saloncentric.com)
  • Introduction and Objective: Because L-PRP constitutes an important source of growth factor that is associated with osteogenesis and fibrogenesis, the aim of this study was to evaluate the effect of L-PRP on the presence of collagen III and MMP-2 and MMP-9, while comparing these results by means of a histomorphometric analysis of bone matrix and fibrous deposition on bone repair. (bvsalud.org)
  • Thus, the aim of this study was to verify the immunolocalization of MMP-2 and -9 and collagen III in rabbit calvarium bone defects treated with and without L-PRP insertion. (bvsalud.org)
  • Conclusions: These data suggest that 3 weeks of circadian disruption with concurrent sleep restriction can lead to an uncoupling of bone turnover wherein bone formation is decreased but bone resorption is unchanged. (cdc.gov)
  • Hans Peter BächingerKazunori MizunoJanice A. VrankaSergei P. Boudko, in Comprehensive Natural Products II, 2010, Type III collagen belongs to the fibrillar collagen group. (gotoh.com.br)
  • It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. (mdbioproducts.com)
  • It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form. (mdbioproducts.com)
  • A non-vascular form of connective tissue composed of CHONDROCYTES embedded in a matrix that includes CHONDROITIN SULFATE and various types of FIBRILLAR COLLAGEN. (bvsalud.org)
  • Fish collagen peptides are comprised of two types of collagen, types I & III. (vitalnutrientspro.co)
  • Collagen supplementation has been shown to support skin health to improve signs of aging, such as wrinkles and decreased puffiness. (prohealth.com)
  • Maintaining proper collagen levels within the body may help to slow visible signs of aging like sagging skin or wrinkles. (naturewise.com)
  • Collagen gives skin a smoother fuller appearance, reducing the look of lines and wrinkles. (nowketo.com)
  • This includes Fish, Chicken, Bovine and Eggshell Membrane Collagen. (horbaach.com)
  • Liquid Biocell ® is offered for a multitude of health and dietary needs- for those seeking to get the benefits of liquid collagen without any included calories or sugar, the Pure formula is a great-tasting method to go. (bestliquidcollagen.com)
  • For a detailed breakdown of this product's collagen profile, click " Ingredients " below! (bodyenergyclub.com)
  • Type IV EDS results from defects in the structure or synthesis of type III collagen. (gotoh.com.br)
  • Super collagen Type I and III is 100% pure collagen protein that provides building materials for growth and maintenance of a healthy body. (otcdeal.com)
  • Fortunately, you can boost your body's collagen levels by regularly consuming high-quality collagen peptides, thereby supporting the growth of healthy, glowing skin. (healthrangerstore.com)
  • 5], Type III collagen is synthesized by cells as a pre-procollagen. (gotoh.com.br)
  • OptiCol™ Human Collagen Type III is initially produced as procollagen, a protein consisting of three pro-α1(III) chains that form the triple-stranded, rope-like molecule. (cellgs.com)
  • the concentrations of the mRNAs for alpha1(III) procollagen and for beta-actin, however, were not significantly changed. (cdc.gov)
  • In addition, an apparent diffuse increase in alpha1(III) procollagen mRNA expression was observed. (cdc.gov)
  • No matter what sort of liquid collagen products you're looking for, Liquid Biocell ® Life is a terrific all-purpose product and an outstanding one to start with. (bestliquidcollagen.com)
  • Supported by doctor all over the world, Liquid Biocell® has actually gotten numerous awards for its quality, security and effectiveness and is revered as one of the very best liquid collagen products available. (bestliquidcollagen.com)
  • Type III collagen mutations are associated with Ehlers-Danlos syndrome, vascular deficiency, and aortic and arterial aneurysms. (gotoh.com.br)
  • Different gene mutations affect the amount, structure, or assembly of different collagens. (msdmanuals.com)
  • 1. Proksch E, Segger D, Degwert J, Schunck M, Zague V, Oesser S. Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. (prohealth.com)
  • Collagen is a naturally occurring protein that plays a crucial role in keeping your skin firm and plump. (healthrangerstore.com)
  • Although your skin naturally produces its own supply of collagen, this production noticeably slows down as you age. (healthrangerstore.com)
  • To help you maintain optimal collagen levels and support healthy skin, the Health Ranger Store is bringing you a new, clean lot of Groovy Bee® Collagen Peptides - Hydrolyzed Type I and III Collagen. (healthrangerstore.com)
  • Meanwhile, a study that was published in the Journal of Cosmetic Dermatology indicated that collagen peptides can support healthy skin barrier function, as well as support your skin's natural healing process. (healthrangerstore.com)
  • We at Pure Collagen.US will be offering products that help set back the biological clock with your skin appearance. (purecollagen.us)
  • Collagen is also a contributing factor in maintaining healthy hair and skin. (naturewise.com)
  • Keeping your skin younger, your body fit and your mind healthy are just a few of the many responsibilities your collagen cells tend to every day. (bestliquidcollagen.com)
  • Type IV - This filtrating collagen is mainly found in the different layers of the skin, eventually assisting bind them together. (bestliquidcollagen.com)
  • Since it is among the body's main building blocks, collagen is produced en masse at a young age- this is why you tend to have more flexible skin and a much healthier brain and body as a kid. (bestliquidcollagen.com)
  • Purified type I & III bovine collagen from calf skin. (mdbioproducts.com)
  • This clinically studied formula combines Hydrolyzed Collagen and an essential antioxidant, Vitamin C. Together, they can boost healthy collagen formation for youthful, healthy and radiant skin. (xtraherbal.com)
  • Liquid Collagen Skin Revitalization Collagen may be the most important element of human skin. (muscleandstrength.com)
  • Sooner or later, the reduction of collagen causes skin to become thinner, drier and more fragile. (muscleandstrength.com)
  • I love using multi collagen protein products especially with type 1 through 5 it does make your skin beautiful and you will look absolutely ageless I'm 60 years old and people of Florida when I tell them my age they all think I'm around 42. (horbaach.com)
  • Type III - Crucial for the structure of muscles, organs and arteries, this type of collagen is normally found in the skin, intestinal tracts, capillary and lungs. (bestliquidcollagen.com)
  • A collagen boost can help improve hair strength, nail growth and give healthy looking skin. (nowketo.com)
  • Our unflavored collagen peptides include DigeSEB ® Super enzymes for comfortable digestion, plus AstraGin ® to encourage excellent nutrient absorption. (naturewise.com)
  • Collagen is also an important component of the gut's connective tissue and may help support the protective lining of the digestive tract. (vitalnutrientspro.co)
  • Type I - This kind of collagen is made of densely-packed fibers that provide structure for connective tissue all over the body. (bestliquidcollagen.com)
  • Collagen is quickly produced during youth to support growing organ systems and develop brand-new connective tissue as the body increases in size. (bestliquidcollagen.com)
  • The body's structural protein collagen helps to keep muscles and connective tissue strong and flexible. (beautyfly.pk)