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Details on Person Collagen fibrils are the principal tensile element of the ex...
| Class:Id | Summation:9014262 |
|---|---|
| _displayName | Collagen fibrils are the principal tensile element of the ex... |
| _timestamp | 2017-09-06 10:05:07 |
| created | [InstanceEdit:9014268] Varusai, Thawfeek, 2017-07-27 |
| literatureReference | [LiteratureReference:9014031] 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 [LiteratureReference:2127624] Echinoderm collagen fibrils grow by surface-nucleation-and-propagation from both centers and ends [LiteratureReference:2127632] Growth of collagen fibril seeds from embryonic tendon: fractured fibril ends nucleate new tip growth [LiteratureReference:2559652] Collagen fibrillogenesis in tendon development: current models and regulation of fibril assembly |
| modified | [InstanceEdit:9014278] Varusai, Thawfeek, 2017-07-27 [InstanceEdit:9020462] Varusai, Thawfeek, 2017-09-06 |
| text | Collagen fibrils are the principal tensile element of the extracellular matrix in a wide range of animal connective tissues. Several models have been proposed including the simple surface nucleation and propagation (SNAP) model (Trotter et al. 2000) but the mechanism of fibril assembly and regulation of fibril diameter and length are not completely understood (Holmes et al. 2001, Banos et al. 2008). Fibrils frequently contain more than one type of collagen, and the outer surface of fibrils frequently interacts with proteoglycans, fine-tuning its structural and signaling properties (Ricard-Blum et al. 2011). Laterally, molecules are believed to be packed into a quasi-hexagonal structure (Trus & Piez 1980) resulting in locally ordered crystalline regions interspersed with disordered regions across the lateral plane of the fibril (Hulmes 2002). Interactions between molecules stabilize the fibril, including the formation of divalent and subsequently trivalent crosslinks, unique to collagen, that involve lysine or hydroxylysine residues. Mutations in procollagen peptide type V (COL5A1) can cause diseases such as Ehlers-Danlos Sydrome. Majority of the cases result from haploinsufficiency of COL5A1 protein that may lead to a disorganised extracellular matrix. Moreover, other mutations result in structural defects which may in turn result in defective collagen fibrils. The accumulation and interaction of this defective collagen fibrils may lead to ER stress and other complications in the cell (Takahara K et al. 2002, Symoens S et al. 2012). |
| (summation) | [Polymerisation:9014269] Formation of defective COL5A1 collagen fibrils [Homo sapiens] |
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