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PMID: 3997977 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Binding of laminin to type IV collagen: a morphological study.

The Journal of cell biology ·Vol. 100 ·No. 6 ·1985-06-00 ·Pages 1848-53

Charonis AS, Tsilibary EC, Yurchenco PD, Furthmayr H

Abstract

A mixture of laminin and type IV collagen was analyzed by rotary shadowing using carbon/platinum and electron microscopy. Laminin was found to form distinct complexes with type IV collagen: one site of interaction is located 140 nm from the COOH-terminal, noncollagenous (NC1) domain and the other is located within the NH2-terminal region. The isolated NC1 fragment of type IV collagen does not appear to interact with laminin, while pepsin-treated type IV collagen, which lacks the NC1 domain, retains its ability to form complexes with laminin. Analysis of the laminin-type IV complexes indicates that laminin binds to type IV collagen via the globular regions of either of its four arms. This finding is supported by experiments using fragment P1 of laminin which lacks the globular regions and which does not bind to type IV collagen in a specific way. In addition, after heat-denaturation of laminin no specific binding is observed.

MeSH Terms
Animals Binding Sites Carbon Collagen/metabolism Hot Temperature Laminin/metabolism Macromolecular Substances Mice Microscopy, Electron Peptide Fragments/metabolism Platinum Protein Binding Protein Denaturation
Chemicals
Laminin Macromolecular Substances Peptide Fragments Platinum Carbon Collagen
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Charonis A S
Tsilibary E C
Yurchenco P D
Furthmayr H
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21 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1985-06-00
Pages
1848-53
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2113590
Subset
IM
Grants
NIADDK NIH HHS · AM-30556 · United States
NIGMS NIH HHS · GM-07562 · United States
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