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Details on Person Type IV collagen (Yurchenco & Furthmayr 1984) and laminin (Y...
| Class:Id | Summation:2328184 |
| _displayName | Type IV collagen (Yurchenco & Furthmayr 1984) and laminin (Y... |
| _timestamp | 2013-07-29 14:52:09 |
| created | [InstanceEdit:2328179] Jupe, S, 2012-06-25 |
| literatureReference | [LiteratureReference:2210332] Self-assembly of basement membrane collagen [LiteratureReference:2328150] Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity [LiteratureReference:2426346] Laminin forms an independent network in basement membranes [LiteratureReference:2328146] Self-assembly of laminin isoforms [LiteratureReference:2328123] Supramolecular assembly of basement membranes [LiteratureReference:2396364] Role of laminin terminal globular domains in basement membrane assembly [LiteratureReference:2396417] Basement membrane assembly, stability and activities observed through a developmental lens [LiteratureReference:2396203] Self-assembly and calcium-binding sites in laminin. A three-arm interaction model [LiteratureReference:2426354] Basement membrane complexes with biological activity [LiteratureReference:2426347] Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV [LiteratureReference:2328174] Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV [LiteratureReference:2161281] Binding of laminin to type IV collagen: a morphological study [LiteratureReference:2426369] Binding domain for laminin on type IV collagen [LiteratureReference:2426353] Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen [LiteratureReference:4084519] Laminin 5 binds the NC-1 domain of type VII collagen [LiteratureReference:2426361] NC1 domain of type VII collagen binds to the beta3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats |
| modified | [InstanceEdit:2396250] Jupe, S, 2012-07-09 [InstanceEdit:2426341] Jupe, S, 2012-08-01 [InstanceEdit:2867920] Jupe, S, 2012-12-19 [InstanceEdit:4084534] Jupe, S, 2013-07-29 |
| text | Type IV collagen (Yurchenco & Furthmayr 1984) and laminin (Yurchenco et al. 1985,1992, Cheng et al. 1997) can self-assemble in vitro, forming lattice-like polymeric networks which resemble laminin-collagen matrices observed in vivo (Timpl & Brown 1996). Purified laminins are the only basement membrane component able to assemble on cell surfaces in the absence of other components (McKee et al. 2007). Laminin knockouts prevent basement membrane assembly, arresting development at a much earlier stage than knockouts of other ECM components such as collagen IV, nidogens (entactin), perlecan or agrin (Yurchenko et al. 2004). This suggests a regulatory function for the laminin network. Laminin molecules bind to each other in a three-way interaction involving the LN domains located at the end of the three short arms. Each interaction involves one each of alpha, beta and gamma laminin subunits (Yurchenko & Cheng 1993, McKee et al. 2007) forming a polygonal structure (Yurchenko et al. 1992).
In the basement membrane collagen type IV and laminin are found in an approximately 1:1 molar ratio (Kleinman et al. 1986). Binding between laminin and collagen type IV is primarily facilitated by nidogen (Aumailley et al. 1989, Fox et al. 1991), but direct binding has been observed (Charonis et al. 1985, Rao et al. 1985). Laminin-111 (laminin-1) binds to type IV collagen through its short arms (Laurie et al. 1986). |
| (summation) | [Reaction:2328145] Laminin-111 binds collagen type IV [Homo sapiens] |
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