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 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 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.

Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases. (1/105)

The low abundance fibrillar collagen type V is incorporated into and regulates the diameters of type I collagen fibrils. Bone morphogenetic protein-1 (BMP-1) is a metalloprotease that plays key roles in regulating formation of vertebrate extracellular matrix; it cleaves the C-propeptides of the major fibrillar procollagens I-III and processes precursors to produce the mature forms of the cross-linking enzyme prolysyl oxidase, the proteoglycan biglycan, and the basement membrane protein laminin 5. Here we have successfully produced recombinant pro-alpha1(V)(2)pro-alpha2(V) heterotrimers, and we have used these to characterize biosynthetic processing of the most prevalent in vivo form of type V procollagen. In addition, we have compared the processing of endogenous pro-alpha1(V) chains by wild type mouse embryo fibroblasts and by fibroblasts derived from embryos doubly homozygous null for the Bmp-1 gene and for a gene encoding the closely related metalloprotease mammalian Tolloid-like 1. Together, results presented herein indicate that within pro-alpha1(V)(2)pro-alpha2(V) heterotrimers, pro-alpha1(V) N-propeptides and pro-alpha2(V) C-propeptides are processed by BMP-1-like enzymes, and pro-alpha1(V) C-propeptides are processed by furin-like proprotein convertases in vivo.  (+info)

Schwann cell adhesion to a novel heparan sulfate binding site in the N-terminal domain of alpha 4 type V collagen is mediated by syndecan-3. (2/105)

Previously we reported that type V collagen synthesized by Schwann cells inhibits the outgrowth of axons from rat embryo dorsal root ganglion neurons but promotes Schwann cell migration (Chernousov, M. A., Stahl, R. C., and Carey, D. J. (2001) J. Neurosci. 21, 6125-6135). Analysis of Schwann cell adhesion and spreading on dishes coated with various type V collagen domains revealed that Schwann cells adhered effectively only to the non-collagenous N-terminal domain (NTD) of the alpha4(V) collagen chain. Schwann cell adhesion to alpha4(V)-NTD induced actin cytoskeleton assembly, tyrosine phosphorylation, and activation of the Erk1/Erk2 protein kinases. Adhesion to alpha4(V)-NTD is cell type-specific because rat fibroblasts failed to adhere to dishes coated with this polypeptide. Schwann cell adhesion and spreading on alpha4(V)-NTD was strongly inhibited by soluble heparin (IC(50) approximately 30 ng/ml) but not by chondroitin sulfate. Analysis of the heparin binding activities of a series of recombinant alpha4(V)-NTD fragments and deletion mutants identified a highly basic region (not present in other type V collagen NTD) as the site responsible for high affinity heparin binding. Schwann cells adhered poorly to dishes coated with alpha4(V)-NTD that lacked the heparin binding site and failed to spread or assemble organized actin-cytoskeletal structures. Soluble alpha4(V)-NTD polypeptide that contained the heparin binding site inhibited spreading of Schwann cells on dishes coated with alpha4(V)-NTD. Affinity chromatography of Schwann cell detergent extracts on a column of immobilized alpha4(V)-NTD resulted in the isolation of syndecan-3, a transmembrane heparan sulfate proteoglycan. Together, these results suggest that Schwann cells bind to collagen type V via syndecan-3-dependent binding to a novel high affinity heparin binding site in the alpha4(V)-NTD.  (+info)

Type V collagen distribution in liver is reconstructed in coculture system of hepatocytes and stellate cells; the possible functions of type V collagen in liver under normal and pathological conditions. (3/105)

The contents of type I, type III and type V collagen and the collagen type specific distributions in liver under normal and cirrhotic conditions were examined. In CCl4 injected rat, the increasing amount of type V collagen was a specific event during the progression of cirrhosis. In normal liver, immunohistochemical observation showed that type V collagen was localized on the fine fibrils, while type I was localized on the thick fibril. Type V collagen was partially colocalized with type IV collagen. In the cirrhotic liver, type V collagen was localized on the margin of the thick fibrous septa along with type IV collagen. Type I collagen existed in the core region of fibrous septa where the stellate cells were prominent. To elucidate the mechanism of the type specific deposition of collagen in the liver, we constructed a coculture system using both stellate cells and hepatocytes. In this system, type V collagen was mainly deposited on hepatocyte colonies not on stellate cells, while type I collagen fibrils were localized on stellate cells. The spatial positioning of type I and type V collagens in vitro was similar to that in the liver. In the cell adhesion assay, the adhesion of stellate cells to type V collagen was poorer than that of the hepatocytes. The collagen type-specific affinity of the stellate cells and hepatocytes may explain the specific localization of type V collagen in the liver and coculture system. These results suggested that the functions of type V collagen are not only to connect type IV collagen with type I collagen fibril, but also to protect the parenchyma from excess type I collagen deposition produced by stellate cells under pathological conditions.  (+info)

Evidence for immune responses to a self-antigen in lung transplantation: role of type V collagen-specific T cells in the pathogenesis of lung allograft rejection. (4/105)

We have reported that lung allograft rejection involves an immune response to a native protein in the lung, type V collagen (col(V)), and that col(V)-induced oral tolerance prevented acute and chronic rejection. In support of these findings col(V) fragments were detected in allografts during rejection, but not in normal lungs. The purpose of the current study was to isolate and characterize col(V)-specific allograft-infiltrating T cells and to determine their contribution to the rejection response in vivo. Two col(V)-specific T cell lines, LT1 and LT3, were isolated from F344 (RT1(lv1)) rat lung allografts during rejection that occurred after transplantation into WKY (RT1(l)) recipients. Both cell lines, but not normal lung lymphocytes, proliferated in response to col(V). Neither LT1 nor LT3 proliferated in response to alloantigens. LT1 and LT3 were CD4(+)CD25(-) and produced IFN-gamma in response to col(V). Compared with normal CD4(+) T cells, both cell lines expressed a limited V-beta TCR repertoire. Each cell strongly expressed V-beta 9 and 16, but differed in expression of other V-betas. Adoptive transfer of each cell line did not induce pathology in lungs of normal WKY rats. In contrast, adoptive transfer of LT1, but not LT3, caused marked peribronchiolar and perivascular inflammation in isograft (WKY) lungs and abrogated col(V)-induced oral tolerance to allograft (F344) lungs. Collectively, these data show that lung allograft rejection involves both allo- and autoimmune responses, and graft destruction that occurs during the rejection response may expose allograft-infiltrating T cells to potentially antigenic epitopes in col(V).  (+info)

Order of intron removal influences multiple splice outcomes, including a two-exon skip, in a COL5A1 acceptor-site mutation that results in abnormal pro-alpha1(V) N-propeptides and Ehlers-Danlos syndrome type I. (5/105)

Ehlers-Danlos syndrome (EDS) type I (the classical variety) is a dominantly inherited, genetically heterogeneous connective-tissue disorder. Mutations in the COL5A1 and COL5A2 genes, which encode type V collagen, have been identified in several individuals. Most mutations affect either the triple-helical domain of the protein or the expression of one COL5A1 allele. We identified a novel splice-acceptor mutation (IVS4-2A-->G) in the N-propeptide-encoding region of COL5A1, in one patient with EDS type I. The outcome of this mutation was complex: In the major product, both exons 5 and 6 were skipped; other products included a small amount in which only exon 5 was skipped and an even smaller amount in which cryptic acceptor sites within exon 5 were used. All products were in frame. Pro-alpha1(V) chains with abnormal N-propeptides were secreted and were incorporated into extracellular matrix, and the mutation resulted in dramatic alterations in collagen fibril structure. The two-exon skip occurred in transcripts in which intron 5 was removed rapidly relative to introns 4 and 6, leaving a large (270 nt) composite exon that can be skipped in its entirety. The transcripts in which only exon 5 was skipped were derived from those in which intron 6 was removed prior to intron 5. The use of cryptic acceptor sites in exon 5 occurred in transcripts in which intron 4 was removed subsequent to introns 5 and 6. These findings suggest that the order of intron removal plays an important role in the outcome of splice-site mutations and provide a model that explains why multiple products derive from a mutation at a single splice site.  (+info)

Release of biologically active TGF-beta1 by alveolar epithelial cells results in pulmonary fibrosis. (6/105)

Idiopathic pulmonary fibrosis (IPF) is a progressive fatal fibrotic lung disease. Transforming growth factor (TGF)-beta1 is present in a biologically active conformation in the epithelial cells lining lesions with advanced IPF. To determine the role of aberrant expression of biologically active TGF-beta1 by alveolar epithelial cells (AECs), the AECs of explanted normal rat lungs were transfected with the TGF-beta1 gene using the retrovirus pMX-L-s223,225-TGF-beta1. In situ hybridization using a digoxigenin-labeled cDNA of the puromycin resistance gene contained in the pMX demonstrated that pMX-L-s233,225-TGF-beta1 was selectively transfected into AECs of the explants. Conditioned media overlying explants obtained 7 days after being treated with pMX-L-s223,225-TGF-beta1 contained 14.5 +/- 3.15 pg/ml of active TGF-beta1. With the use of Masson's trichrome staining of explant sections obtained 14 days after transfection, there were lesions similar to those in IPF, characterized by type II AEC hyperplasia, interstitial thickening, extensive increase in interstitial and subepithelial collagen, an increase in the number of fibroblasts, and areas resembling fibroblast buds. Collagens I, III, IV, and V and fibronectin were increased in explants treated with pMX-L-s223,225-TGF-beta1. The findings in the current study suggest that IPF may be a disorder of epithelial cells and not inflammatory cells.  (+info)

Differential expression of Smad7 transcripts identifies the CD4+CD45RChigh regulatory T cells that mediate type V collagen-induced tolerance to lung allografts. (7/105)

Regulatory T cells (Tregs) induced by oral tolerance may suppress immunity by production of TGF-beta that could also enhance Treg activity. However, all cells that are phenotypically Tregs in rats (CD4(+)CD45RC(high)-RC(high)) may not have regulatory function. Because Smad7 expression in T cells is associated with inflammation and autoimmunity, then lack of Smad7 may identify those cells that function as Tregs. We reported that feeding type V collagen (col(V)) to WKY rats (RT1(l)) induces oral tolerance to lung allografts (F344-RT1(lvl)) by T cells that produce TGF-beta. The purpose of the current study was to identify the Tregs that mediate col(V)-induced tolerance, and determine Smad7 expression in these cells. RC(high) cells from tolerant rats were unresponsive to allogeneic stimulation and abrogated rejection after adoptive transfer. In contrast, CD4(+)CD45RC(low) (RC(low)) cells from tolerant rats and RC(high) or RC(low) cells from normal rats or untreated allograft recipients proliferated vigorously in response to donor Ags, and did not suppress rejection after adoptive transfer. TGF-beta enhanced proliferation in response to col(V) presented to tolerant RC(high), but not other cells. In contrast to other cells, only RC(high) cells from tolerant rats did not express Smad7. Collectively, these data show that the Tregs that mediate col(V)-induced tolerance to lung allografts do not express SMAD7 and, therefore, are permissive to TGF-beta-mediated signaling.  (+info)

Role of 12-lipoxygenase in the stimulation of p38 mitogen-activated protein kinase and collagen alpha5(IV) in experimental diabetic nephropathy and in glucose-stimulated podocytes. (8/105)

The 12-lipoxygenase (12-LO) pathway of arachidonic acid metabolism is implicated in extracellular matrix (ECM) synthesis, but its role in podocytes has not been studied. This study tested whether 12-LO induction by diabetes or by high glucose (HG) in cultured podocytes alters glomerular basement membrane by activating signal transduction pathways culminating in ECM synthesis. Sprague-Dawley rats received an injection of diluent (control [C]) or streptozotocin 65 mg/kg (DM) and were killed at 1 or 4 mo. Glomerular 12-LO mRNA and protein levels were higher in DM than in C glomeruli at 1 and 4 mo, and 12-LO localized predominantly in podocytes. Glomerular p38 mRNA and protein were higher in DM at months 1 and 4, but phospho-p38 mitogen-activated protein (MAPK) was increased only at month 1. Glomerular collagen alpha5(IV)/glutaraldehyde-3-phosphate dehydrogenase (GAPDH) mRNA ratio was increased in DM at month 1 but not at month 4, whereas collagen alpha5(IV) protein was higher at both 1 and 4 mo. Mouse podocytes were cultured in media with 25 mM glucose (HG) with or without the 12-LO inhibitor cinnamyl-3,4-dihydroxy-cyanocinnamate (CDC) or with 5.5 mM glucose + 19.5 mM mannitol (low glucose [LG+M]) for 10 d at 37 degrees C. 12-LO mRNA and protein levels were higher in HG than in LG+M as was the p38 MAPK/GAPDH mRNA ratio. Phospho-p38 MAPK protein but not total p38 MAPK was higher in HG compared with LG+M. Collagen alpha5(IV)/GAPDH mRNA ratio and protein were higher in HG than in LG+M. 12-LO inhibition by CDC decreased HG-induced phospho-p38 MAPK and the phospho-p38/total p38 MAPK ratio, collagen alpha5(IV)/GAPDH mRNA ratio, and collagen alpha5(IV) protein expression. In summary, diabetes in vivo and exposure of podocytes to HG in vitro stimulated 12-LO, p38 MAPK, and collagen alpha5(IV) mRNA and (activated) protein. 12-LO inhibition by CDC diminished the expression of podocyte phospho-p38 MAPK and collagen alpha5(IV) mRNA and protein. These findings implicate 12-LO and the p38 MAPK signaling pathway in the mediation of ECM synthesis by podocytes in diabetes.  (+info)

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.

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.

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.

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- ... Collagen IV is the more common usage, as opposed to the older terminology of "type-IV collagen".[citation needed] Collagen IV ...
Type I collagen Collagen, type III, alpha 1 Park KS, Park MJ, Cho ML, Kwok SK, Ju JH, Ko HJ, Park SH, Kim HY (2009). "Type II ... Type II collagen is organised into fibrils. This fibrillar network of collagen allows the cartilage to entrap the proteoglycan ... Collagen+type+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with short ... Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by ...
It is related to the fibrillar collagens: type II, type XI, and type XXIV. Current research suggests that it is made by ... Type XXVII collagen is the protein predicted to be encoded by COL27A1. It was first described by Dr. James M. Pace and his ... v t e (Articles lacking sources from December 2009, All articles lacking sources, Collagens, All stub articles, Protein stubs) ...
... is a type of collagen which can be cleaved to form endostatin. The endostatin is from the c terminus end of ... 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 ... When type XVIII collagen is mutated at the COL18A1 gene, exon 2 in the sequence is skipped, which results in production of an ...
Collagen Type II collagen Collagen, type I, alpha 1 Collagen, type I, alpha 2 Collagen, type III, alpha 1 "Collagen: What it is ... Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen. It ... The cross-links result in the formation of very strong mature type I collagen fiber. See Collagen, type I, alpha 1#Clinical ... to make a molecule of type I pro-collagen. These triple-stranded, rope-like pro-collagen molecules must be processed by enzymes ...
... is a 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 ... Together, Collagen V and Collagen I acts as a dominant regulator of collagen fibrillogenesis. Type V Collagens interacts with ...
"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- ...
... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... This gene encodes one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in ... Type-I collagen Collagen GRCh38: Ensembl release 89: ENSG00000164692 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... "Entrez Gene: COL1A2 collagen, type I, alpha 2". Byers PH, Wallis GA, Willing MC (1991). "Osteogenesis imperfecta: translation ...
The COL11A1 gene encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen. Type XI collagen is a ... collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene ... "Entrez Gene: COL11A1 collagen, type XI, alpha 1". GeneReviews/NCBI/NIH/UW entry on Stickler Syndrome Yoshioka H, Ramirez F ( ... Keene DR, Oxford JT, Morris NP (1995). "Ultrastructural localization of collagen types II, IX, and XI in the growth plate of ...
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 ... Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a- ... 2015). "Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial recurrent erosion dystrophy (ERED)". Hum. Mutat. ...
Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. ... "Entrez Gene: COL9A3 collagen, type IX, alpha 3". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
"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 ...
"Entrez Gene: COL23A1 collagen, type XXIII, alpha 1". Banyard J, Bao L, Zetter BR (June 2003). "Type XXIII collagen, a new ... The molecule of collagen XXIII can be found either in membrane-bond form or in shed form. Type XXIII collagen is expressed in ... Collagen XXIII is a type II transmembrane protein and the fourth in the subfamily of non-fibrillar transmembranous collagens. ... Collagen XXIII shows structural homology with collagen XIII and collagen XXV . Apart from having the characteristic structure ...
"Entrez Gene: COL8A1 collagen, type VIII, alpha 1". Shuttleworth CA (1998). "Type VIII collagen". Int. J. Biochem. Cell Biol. 29 ... This gene encodes one of the two alpha chains of type VIII collagen. The gene product is a short chain collagen and a major ... Plenz GA, Deng MC, Robenek H, Völker W (2003). "Vascular collagens: spotlight on the role of type VIII collagen in ... The type VIII collagen fibril can be either a homo- or a heterotrimer. Alternatively spliced transcript variants encoding the ...
"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 ... The protein encoded by this gene is the alpha 1 subunit of type VI collagen (alpha1(VI) chain). Mutations in the genes that ... 1996). "Type VI collagen mutations in Bethlem myopathy, an autosomal dominant myopathy with contractures". Nat. Genet. 14 (1): ...
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 ... 1998). "Type XIII collagen is identified as a plasma membrane protein". J. Biol. Chem. 273 (25): 15590-7. doi:10.1074/jbc. ...
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 ...
Type IX collagen is usually found in tissues containing type II collagen, a fibrillar collagen. Studies in knockout mice have ... sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type ... This gene encodes one of the three alpha chains of type IX collagen, a collagen component of hyaline cartilage. ... "Entrez Gene: COL9A1 collagen, type IX, alpha 1". GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant ...
... type III collagen is also an important regulator of the diameter of type I and II collagen fibrils. Type III collagen is also ... types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of ... 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 ... 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. ... the structure of type I collagen is compromised. Tissues that are rich in type I collagen, such as the skin, bones, and tendons ... Ehlers-Danlos type IV is most attributed to abnormalities in the reticular fibers (collagen Type III). Ehlers-Danlos syndrome, ...
"Entrez Gene: COL25A1 collagen, type XXV, alpha 1". Kakuyama H, Söderberg L, Horigome K, et al. (2006). "CLAC binds to ... Collagen, type XXV, alpha 1 has been shown to interact with Amyloid precursor protein. GRCh38: Ensembl release 89: ... CLAC-P/collagen type XXV". EMBO J. 21 (7): 1524-34. doi:10.1093/emboj/21.7.1524. PMC 125364. PMID 11927537. " ... Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene. COL25A1 is a brain-specific membrane- ...
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. ...
... 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 ...
... 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 ... Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another ...
... or collagen IV NC1 domain) is a duplicated domain present at the C-terminus of type IV collagens. Each type IV collagen ... Structural basis for type IV collagen assembly in basement membranes". J. Biol. Chem. 277 (34): 31142-53. doi:10.1074/jbc. ... In molecular biology, the type IV collagen C4 domain ( ... The collagen IV C4 domain is composed of two similarly folded ... domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link". Proc. Natl. Acad. ...
This protein is an alpha chain of type VI collagen that aids in microfibril formation. As part of type VI collagen, this ... This gene encodes the alpha 3 chain, one of the three alpha chains of type VI collagen, a beaded filament collagen found in ... "The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen". Journal of Molecular Biology. 246 ... "Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution ( ...
... also known as COL28A1 is a protein that in humans is encoded by the COL28A1 gene. This protein ... "COL28A1 collagen, type XXVIII, alpha 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2015-09-25. v t e ... belongs to a class of collagens that contain von Willebrand factor type A domains. The protein is encoded by the COL28A1 gene ... Veit G, Kobbe B, Keene DR, Paulsson M, Koch M, Wagener R (Feb 2006). "Collagen XXVIII, a novel von Willebrand factor A domain- ...
... chain of type II collagen. This gene encodes the alpha-1 chain of type II collagen, a fibrillar collagen found in cartilage and ... "A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in ... type 2 by affecting tissues that are rich in type II collagen. Platyspondylic lethal skeletal dysplasia, Torrance type:Fewer ... chain that cannot be incorporated into type II collagen fibers. As a result, cells make a reduced amount of type II collagen. ...
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 ...
"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 ... Collagen alpha-1(XIV) chain is a protein that in humans is encoded by the COL14A1 gene. It likely plays a role in collagen ...

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