| Autor: |
Tsilibary EC; Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis 55455., Charonis AS, Reger LA, Wohlhueter RM, Furcht LT |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 1988 Mar 25; Vol. 263 (9), pp. 4302-8. |
| Abstrakt: |
Type IV collagen has the ability to self-assemble by amino end, carboxyl end, and lateral associations to complex network-like structures which can be visualized by rotary shadowing. The main noncollagenous NC1 domain which is located at the carboxyl end of type IV collagen molecules binds to itself to form dimers and also binds along the length of type IV collagen. The latter binding initiates lateral assembly. Following in vitro nonenzymatic glucosylation of the isolated NC1 domain, binding to the helix-rich domain of type IV collagen was impaired. In turbidity experiments, the nonenzymatically glucosylated NC1 domain minimally suppressed the development of turbidity of collagen solutions when compared to control NC1 domain. In rotary shadowing experiments nonenzymatically glucosylated NC1 domain did not significantly inhibit lateral associations or networks formed by type IV collagen, whereas control NC1 domain caused a drastic decrease in laterally assembled structures. These data suggest that nonenzymatic glucosylation of the NC1 domain may interfere with normal assembly of type IV collagen in diabetes mellitus and may be related to abnormal functions of basement membranes in this pathological condition. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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