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Details on Person The biosynthesis of collagen is a multistep process. Collage...
| Class:Id | Summation:1650785 |
|---|---|
| _displayName | The biosynthesis of collagen is a multistep process. Collage... |
| _timestamp | 2014-05-28 04:52:33 |
| created | [InstanceEdit:1650793] Jupe, S, 2011-10-12 |
| literatureReference | [LiteratureReference:1650797] Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase. Effect of chain length, helical conformation and amino acid sequence in the substrate [Book:2008088] Post-translational modification of proteins Harding, J Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. [LiteratureReference:1474260] Building collagen molecules, fibrils, and suprafibrillar structures [LiteratureReference:2267325] Mechanisms of collagen trimer formation. Construction and expression of a recombinant minigene in HeLa cells reveals a direct effect of prolyl hydroxylation on chain assembly of type XII collagen [LiteratureReference:2267324] Involvement of prolyl 4-hydroxylase in the assembly of trimeric minicollagen XII. Study in a baculovirus expression system [LiteratureReference:1650798] Proline hydroxylation of collagens synthesized at different temperatures in vivo by two poikilothermic species [LiteratureReference:1650810] Comparative study on the thermostability of collagen I of skin and bone: influence of posttranslational hydroxylation of prolyl and lysyl residues [LiteratureReference:2008084] Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation [LiteratureReference:2008107] Folding of carboxyl domain and assembly of procollagen I [LiteratureReference:2008097] Interchain disulfide bonds in procollagen are located in a large nontriple-helical COOH-terminal domain [LiteratureReference:2008075] The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen [LiteratureReference:2152269] Trimerization and triple helix stabilization of the collagen XIX NC2 domain [LiteratureReference:2008077] Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells [LiteratureReference:2008076] Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage [LiteratureReference:2008096] Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization [LiteratureReference:2008100] Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition [LiteratureReference:2267229] Procollagen trafficking, processing and fibrillogenesis [LiteratureReference:1606413] Another look at collagen V and XI molecules [LiteratureReference:1643669] Helical model of nucleation and propagation to account for the growth of type I collagen fibrils from symmetrical pointed tips: a special example of self-assembly of rod-like monomers [LiteratureReference:1643663] The collagen fibril: the almost crystalline structure [LiteratureReference:1643679] Collagen cross-linking. Purification and substrate specificity of lysyl oxidase |
| modified | [InstanceEdit:2008095] Jupe, S, 2011-11-21 [InstanceEdit:2022095] Jupe, S, 2011-11-25 [InstanceEdit:2172318] Jupe, S, 2012-03-29 [InstanceEdit:2193145] Jupe, S, 2012-04-12 [InstanceEdit:2267323] Jupe, S, 2012-05-24 [InstanceEdit:2288091] Jupe, S, 2012-05-28 [InstanceEdit:5397972] D'Eustachio, Peter, 2014-04-30 [InstanceEdit:5490369] Matthews, Lisa, 2014-05-20 [InstanceEdit:5577005] Matthews, Lisa, 2014-05-28 |
| text | The biosynthesis of collagen is a multistep process. Collagen propeptides are cotranslationally translocated into the ER lumen. Propeptides undergo a number of post-translational modifications. Proline and lysine residues may be hydroxylated by prolyl 3-, prolyl 4- and lysyl hydroxylases. 4-hydroxyproline is essential for intramolecular hydrogen bonding and stability of the triple helical collagenous domain. In fibril forming collagens approximately 50% of prolines are 4-hydroxylated; the extent of this and of 3-hydroxyproline and lysine hydroxylation varies between tissues and collagen types (Kivirikko et al. 1972, 1992). Hydroxylysine molecules can form cross-links between collagen molecules in fibrils, and are sites for glycosyl- and galactosylation. Collagen peptides all have non-collagenous domains; collagens within the subclasses have common chain structures. These non-collagenous domains have regulatory functions; some are biologically active when cleaved from the main peptide chain. Fibrillar collagens all have a large triple helical domain (COL1) bordered by N and C terminal extensions, called the N and C propeptides, which are cleaved prior to formation of the collagen fibril. The C propeptide, also called the NC1 domain, is highly conserved. It directs chain association during intracellular assembly of the procollagen molecule from three collagen propeptide alpha chains (Hulmes 2002). The N-propeptide has a short linker (NC2) connecting the main triple helix to a short minor one (COL2) and a globular N-terminal region NC3. NC3 domains are variable both in size and the domains they contain. Collagen propeptides typically undergo a number of post-translational modifications. Proline and lysine residues are hydroxylated by prolyl 3-, prolyl 4- and lysyl hydroxylases. 4-hydroxyproline is essential for intramolecular hydrogen bonding and stability of the triple helical collagenous domain. Prolyl 4-hydroxylase may also have a role in alpha chain association as no association of the C-propeptides of type XII collagen was seen in the presence of prolyl 4-hydroxylase inhibitors (Mazzorana et al. 1993, 1996). In fibril forming collagens approximately 50% of prolines are 4-hydroxylated; the extent of this is species dependent, lower hydroxylation correlating with lower ambient temperature and thermal stability (Cohen-Solal et al. 1986, Notbohm et al. 1992). Similarly the extent of 3-hydroxyproline and lysine hydroxylation varies between tissues and collagen types (Kivirikko et al. 1992). Hydroxylysine molecules can form cross-links between collagen molecules in fibrils, and are sites for glycosyl- and galactosylation. Collagen molecules fold and assemble through a series of distinct intermediates (Bulleid 1996). Individual collagen polypeptide chains are translocated co-translationally across the membrane of the endoplasmic reticulum (ER). Intra-chain disulfide bonds are formed within the N-propeptide, and hydroxylation of proline and lysine residues occurs within the triple helical domain (Kivirikko et al. 1992). When the peptide chain is fully translocated into the ER lumen the C-propeptide folds, the conformation being stabilized by intra-chain disulfide bonds (Doege and Fessler 1986). Pro alpha-chains associate via the C-propeptides (Byers et al. 1975, Bachinger et al. 1978), or NC2 domains for FACIT family collagens (Boudko et al. 2008) to form an initial trimer which can be stabilized by the formation of inter-chain disulfide bonds (Schofield et al. 1974, Olsen et al. 1976), though these are not a prerequisite for further folding (Bulleid et al. 1996). The triple helix then nucleates and folds in a C- to N- direction. The association of the individual chains and subsequent triple helix formation are distinct steps (Bachinger et al. 1980). The N-propeptides associate and in some cases form inter-chain disulfide bonds (Bruckner et al., 1978). Procollagen is released via carriers into the exracellular space (Canty & Kadler 2005). Fibrillar procollagens undergo removal of the C- and N-propeptides by procollagen C and N proteinases respectively, both Zn2+ dependent metalloproteinases. Propeptide processing is a required step for normal collagen I and III fibril formation, but collagens can retain some or all of their non-collagenous propeptides. Retained collagen type V and XI N-propeptides contribute to the control of fibril growth by sterically limiting lateral molecule addition (Fichard et al. 1995). Processed fibrillar procollagen is termed tropocollagen, which is considered to be the unit of higher order fibrils and fibres. Tropocollagens of the fibril forming collagens I, II, III, V and XI sponteneously aggregate in vitro in a manner that has been compared with crystallization, commencing with a nucleation event followed by subsequent organized aggregation (Silver et al. 1992, Prockop & Fertala 1998). Fibril formation is stabilized by lysyl oxidase catalyzed crosslinks between adjacent molecules (Siegel & Fu 1976). |
| (summation) | [Pathway:1650814] Collagen biosynthesis and modifying enzymes [Homo sapiens] |
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