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Details on Person Collagen type VII formation begins with the assembly of proc...
| Class:Id | Summation:1637775 |
|---|---|
| _displayName | Collagen type VII formation begins with the assembly of proc... |
| _timestamp | 2011-10-11 14:59:20 |
| created | [InstanceEdit:1637810] Jupe, S, 2011-10-05 |
| literatureReference | [LiteratureReference:1643664] Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain [LiteratureReference:1643667] The relationship of the biophysical and biochemical characteristics of type VII collagen to the function of anchoring fibrils [LiteratureReference:1637805] Type VII collagen: the anchoring fibril protein at fault in dystrophic epidermolysis bullosa [LiteratureReference:1643671] The tissue form of type VII collagen is an antiparallel dimer [LiteratureReference:1637812] Type VII collagen is a major structural component of anchoring fibrils [LiteratureReference:1637820] Procollagen VII self-assembly depends on site-specific interactions and is promoted by cleavage of the NC2 domain with procollagen C-proteinase [LiteratureReference:1643684] Large complex globular domains of type VII procollagen contribute to the structure of anchoring fibrils [LiteratureReference:1637806] Type VII collagen forms an extended network of anchoring fibrils [LiteratureReference:1637807] Most anchoring fibrils in human skin originate and terminate in the lamina densa |
| modified | [InstanceEdit:1643675] Jupe, S, 2011-10-11 |
| text | Collagen type VII formation begins with the assembly of procollagen type VII, believed to consist of three identical alpha-1(VII) chains (Bentz et al. 1983, Bachinger et al. 1990). These pro-alpha-1(VII) polypeptides associate through their carboxy-terminal ends to form a trimer and the collagen-like portion folds into a triple-helix (Chung & Uitto 2010). The trimers are then secreted to the extracellular region where they form an anti-parallel dimer, via the amino terminus (Morris et al. 1986, Sakai et al. 1986). Dimer assembly is accompanied by proteolytic removal of a portion of the carboxy-terminus and stabilization by inter-molecular disulfide bond formation (Colombo et al. 2003). Dimers aggregate laterally to form fibrils that have a characteristic centro-symmetric banding pattern (Lunstrum et al. 1986). Collagen type VII is the major constituent of anchoring fibrils, the structures which mediate the attachment of the epidermis to the dermis (Keene et al. 1987). The interaction of type VII collagen with the lamina densa is believed to be mediated by a non-triple helical portion of type VII collagen that is lost during proteolytic solubilization. Most, if not all, anchoring fibrils attach at both ends to the lamina densa, allowing entrapment of interstitial collagen fibers in a U-shaped structure (Shimizu et al. 1997). |
| (summation) | [Polymerisation:1637815] Formation of collagen type VII fibrils [Homo sapiens] |
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