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• W2083503468 abstract "Domain V of the major basement-membrane proteoglycan perlecan, a domain which consists of three laminin type G (LG) and four epidermal-growth-factor-like (EG) modules, was obtained in recombinant form by transfecting embryonic kidney cells with an episomal expression vector. A major 90-kDa fragment V was obtained together with fragments Va (74 kDa) and Vb (26 kDa) which were generated by endogenous proteolysis in front of the most C-terminal LG module. All three fragments bound to a heparin affinity column and could be displaced at a moderate (0.2 M) NaCl concentration. Rotary-shadowing electron microscopy demonstrated a three-globule structure for fragment V. Fragment V also showed a strong immunological cross-reaction with tissue-derived perlecan, indicating that it was folded into a native structure. A further, larger fragment, Vc, was apparently substituted with heparan sulphate and/or chondroitin sulphate chains and failed to bind to heparin. Fragment V but not fragment Vc promoted a distinct adhesion of several cell lines and this could be blocked by antibodies against the integrin β1 chain. This domain may, however, represent only one of several cell-adhesive sites of perlecan. The recombinant perlecan fragment V bound in surface plasmon resonance assays to fibulin-2, laminin-nidogen complex, nidogen and two nidogen fragments. This indicated two different nidogen-binding epitopes on perlecan domain V with about a 10-fold difference in their affinities (Kd= 0.05–0.2 μM and about 2 μM). Perlecan domain V therefore seems to participate in the supramolecular assembly and cell connections of basement membranes." @default.
• W2083503468 created "2016-06-24" @default.
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• W2083503468 date "1997-11-15" @default.
• W2083503468 modified "2023-10-09" @default.
• W2083503468 title "The C-Terminal Domain V of Perlecan Promotes beta1 Integrin-Mediated Cell Adhesion, Binds Heparin, Nidogen and Fibulin-2 and Can be Modified by Glycosaminoglycans" @default.
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• W2083503468 doi "https://doi.org/10.1111/j.1432-1033.1997.t01-1-00039.x" @default.
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