Schittny, Johannes Constantin; Schittny, Christiane Martha (1993). Role of the B1 short arm in laminin self-assembly. European journal of biochemistry, 216(2), pp. 437-441. Blackwell Science
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Laminin self-assembles into a basement membrane polymer through specific low-affinity interactions. Recently, it was shown that the terminal short-arm domain (domains VI and V) of the B1 chain (fragment E4) possesses one of the laminin self-interaction sites [Schittny, J.C. & Yurchenco, P.D. (1990) J. Cell Biol. 110, 825-832], but that the binding partner(s) of this domain is unknown. Using affinity retardation chromatography we now investigate the domain(s) fragment E4 binds to. The elution of E4 was clearly retarded on immobilized laminin and fragment E1' (three-chain short-arm complex excluding the distal part of the B1 chain), but not on immobilized E4 in calcium containing buffer and at 37 degrees C. Under the same conditions, E1' strongly interacts with immobilized E4. In addition, E1' is able to non-covalently cross-link soluble E4 to immobilized E4. No further interaction of laminin and E4 with additional fragments (P1', A, B2 and B1 chain short-arm complex without B1-domains VI-IV and without globules; E8, distal long arm and G1-3; E3, long-arm G subdomains 4 and 5) could be demonstrated. These data are interpreted as evidence that (a) the primary laminin-laminin bonds are formed between the short arms of laminin, that (b) the terminal B1 short-arm domain (E4) can interact with the short arm(s) of the A and/or B2 chain(s) (domain E1'), but does not self-interact, and that (c) due to at least three self-binding sites, laminin polymerization behaves co-operatively.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy > Functional Anatomy |
UniBE Contributor: |
Schittny, Johannes |
Subjects: |
500 Science > 570 Life sciences; biology |
ISSN: |
0014-2956 |
Publisher: |
Blackwell Science |
Language: |
English |
Submitter: |
Johannes Schittny |
Date Deposited: |
18 Aug 2014 16:22 |
Last Modified: |
05 Dec 2022 14:33 |
PubMed ID: |
8375382 |
BORIS DOI: |
10.7892/boris.50165 |
URI: |
https://boris.unibe.ch/id/eprint/50165 |
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