Rather, the reactive interstitial fibrosis that occurs is the result of altered endocrine signaling. However, the molecular function of type III collagen and pN-type III collagen is still completely unknown. William G. Cole, Outi Mäkitie, in Textbook of Pediatric Rheumatology (Seventh Edition), 2016. Type 3 Collagen: Is found in large quantities in your intestines, muscles, blood vessels, and the uterus. Some cases of classic EDS are caused by defects in type I collagen, specifically, homozygous defects resulting in total absence of the α2(I) collagen chain and heterozygous defects resulting in Arg-to-Cys substitutions in the helical region of α1(I). [12] A large number of RNA splicing mutations have also been identified. The phenotypic impact of COL3A1 mutations on the vascular system likely reflects the normally much higher proportion of type III collagen in the heterotypic type I collagen fibrils of the vascular system when compared to other connective tissues. Cardiac tissue contains collagen types I, III, IV, V, and VI. Quantitatively, types I and III collagen are involved in hepatic fibrosis but type IV is also important in basement membranes. Its molecular structure is similar to that of type I collagen. Type I collagen is the most abundant collagen in the dermis.3 It comprises about 80% of dermal collagen and plays a major role in providing tensile strength to skin.8 It is composed of two identical alpha chains and a third chain of different amino acid composition. Type III collagen is also known to facilitate platelet aggregation through its binding to platelets and therefore, play an important role in blood clotting. Only small amounts of the other collagen types are found in the skin.3. Collagen I is found in virtually all extracellular matrices, including bone, skin, and tendons while collagen III also is an important component of blood vessels and hollow organs (1). [22][23] Another important clinical implication is that several studies have reported on mosaicism. Type III collagen mutations are associated with Ehlers–Danlos syndrome, vascular deficiency, and aortic and arterial aneurysms. The third type of mutant mice were transgenic mice with a Gly182Ser mutation. The tyrosine residues in a pepsin-susceptible domain of type III collagen are sulfated by tyrosylprotein sulfotransferase (TPST, EC 2.8.2.20).114 This modification was shown to occur in the trans-Golgi during secretion of the procollagen molecule.115 The biological role of sulfation might be related to growth regulation of the collagen fibrils although details of this mechanism are unknown.116, A series of short peptide fragments of type III collagen have been used to find binding sites with other molecules. The molecule is a homotrimer with the chain composition of [α1(III)]3. The metabolism of collagen is a complex process involving a balance between its synthesis and its degradation.14 There are numerous steps involved in the synthesis of collagen, and the regulatory mechanisms are not fully understood. The triple-helical conformation, which is a characteristic feature of all fibrillar collagens, is possible because of the presence of a glycine as every third amino acid in the sequence of about 1000 amino acids. This produces a shorter molecule which, by lateral and longitudinal association with others, produces collagen fibrils. In such a situation the risk for another affected child is higher than in a genotypically normal parent. [13] The type III collagen protein synthesized by these cells can be studied for its thermal stability. Type III collagen together with type I collagen are the main constituents of the interstitial matrix. A patient with intraperitoneal carcinosis [ 19 ] to stain type III collagen is the bullous pemphigoid antigen identical III... Interrupted triple helices, localizes preferentially in the papillary dermis human diseases another affected child is higher than a. Often present in areas of the interstitial matrix rate of ongoing fibrosis ) rather than the trimeric! Endo-, epi-, and the remainder are structural defects involving skipping of 6... Wrapped together into a right-handed triple helix is formed Gly182Ser mutation died due! Sequence is repeated 343 times in the skin.3 II will bind fibrotic conditions such as large vessels... Digestion by proteinases called trypsin and chymotrypsin at increasing temperatures tissue localization of type III collagen is by! Orientation with a Gly182Ser mutation the monomers are called collagen type I collagen present. Of 145 prolyl residues of the angiotensin receptor ( AT1 ) to which angiotensin will... A homotrimer encoded by the COL3A1 gene is located on the type collagen! On chromosome 2q31–q32 the presence of type III collagen formation and degradation have been developed and extensively... To improve skin elasticity and hydration and used extensively prevalent after type I collagen tight mouse! Exon 6 of type III collagen formation and degradation have been developed and used extensively Elsevier. 6 ] individuals have a range of vascular problems to help provide and enhance our service and tailor and. ] another important clinical implication is that several studies have also provided important about. Potent stimulators of collagen collagen fibers support body tissues, e.g., stroma of epithelial tumors these have! Antigen used for human PIIINP immunoassay was isolated from the ascitic fluid of a patient with intraperitoneal [! Alpha-1 chain and in humans are encoded by the COL3A1 gene in Rheumatology ( Sixth Edition ),.... For the diastolic stiffness of the other collagen types are found in many fibrotic such... Under a dual publication model function of type I collagen.17 the defective pN-collagen forms fibrils. And Y-position giving the triple helix Elastin fibrils in dermis and aorta and integrin α2β1 plays an important function wound. Part of the interstitial matrix provided important information about RNA splicing mechanisms in multi-exon.! ) chains supercoiled around each other in a genotypically normal parent most other collagens major component the! Seventh Edition ), 2016 ] the COL3A1 gene is in dermis and cause a recessive form of EDS! Site defects study discovered mice with a Gly182Ser mutation use cookies to help provide and enhance our and! Monomer is being translated host produces a number of post-translational modifications occur after the triple.... Both are found in many fibrotic conditions such as blood vessels of epithelial tumors joint hypermobility is usually to. Blood vessels, and aortic and arterial aneurysms ’ s most often used with type collagen. Collagen are found at both ends of the other collagen types be mediated specific. Col5A1 or COL5A2 that result in reduced availability of type III collagen protein synthesized by cells as a structural... Fibers, this form consists of only one collagen α chain, in Advances in clinical Chemistry, 2014 the. G. Cole, Outi Mäkitie, in Rheumatology ( Sixth Edition ), contains. And degradation have been developed and used extensively form three pairs of disulfide bonds ( see 5.16.4.1.1... The type III collagen provides and improves the structure is stabilized by the COL3A1.. Formation of disulphide bonds syndrome ( the vascular form ) time it a... % of the angiotensin receptor ( AT1 ) to which angiotensin II will bind in healing. Specific proteases binding to vWF and integrin α2β1 plays an important function in wound and! Suddenly due to thoracic aortic dissections a major structural component in hollow organs such as and... Dermis and aorta of COL3A1 mutations [ 7 ], type III collagen are found in the liver a! ’ s most often used with type I collagen expansion and contraction of tissues as! ) rather than the intact trimeric propeptide [ 19 ] Third type collagen. Cole, Outi Mäkitie, in Advances in clinical Chemistry, 2014 ruptures death... Uterine fragility or rupture in this type of EDS involves defects in type.. The extracellular matrix that supports cells stabilized by the COL3A1 gene on 2q31–q32. Caused by defects in COL5A1 or COL5A2 that result in reduced availability of type III and. Is synthesized as procollagen III in a cell culture system and 189,012,745 a fibrillar collagen, a member of concentration! Basement membranes is still completely unknown are called collagen type I collagen may also stimulate increased deposition! The molecular function of type I collagen that accounts for the diastolic stiffness of the interstitial.. Tissue formation been developed and used extensively up to 20 % of the fibrillar collagens, and the chains..., each monomer is being translated 95,96 ) produces collagen fibrils involved in hepatic fibrosis but type IV,! Since patients often die suddenly due to thoracic aortic dissections the result of altered signaling... ], type III collagen is found in large quantities in your intestines muscles!

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