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Type: Journal article
Title: Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the α3(VI) chain of type VI collagen
Other Titles: Microfibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagen
Author: Finnis, M.
Gibson, M.
Citation: Journal of Biological Chemistry, 1997; 272(36):22817-22823
Publisher: American Society for Biochemistry and Molecular Biology
Issue Date: 1997
ISSN: 1083-351X
Statement of
Merran L Finnis and Mark A Gibson
Abstract: The interactions of type VI collagen have been investigated, using solid phase binding assays, with two components of the fibrillin-containing microfibrils, the elastin-binding protein, MAGP-1 and its structural relative MAGP-2. Both native and pepsin-treated forms of type VI collagen specifically bound to MAGP-1 but not to MAGP-2. Pepsin type VI collagen was shown to block the binding of MAGP-1 to native type VI collagen indicating that the major MAGP-1-binding site was in the triple-helical region of the molecule. MAGP-1 was found not to bind to collagens I, III, and V. Affinity blotting of pepsin-treated type VI collagen showed that MAGP-1 binding was specific for the collagenous domain of the α3(VI) chain. Decorin and biglycan were found not to inhibit the interaction of pepsin-treated type VI collagen with MAGP-1, indicating that its binding site on the collagen is not close to that for the proteoglycans. Reduction and alkylation of disulfide bonds in MAGP-1 did not destroy its type VI collagen-binding properties, indicating that the binding site was likely to be in the cysteine-free, N-terminal domain of MAGP-1. Interestingly, the interaction of MAGP-1 with type VI collagen was inhibited by tropoelastin, suggesting that the binding sites for tropoelastin and type VI collagen may be in the same domain of MAGP-1. A peptide, corresponding to amino acids 29–38 of MAGP-1, was found to inhibit the interactions of MAGP-1 with type VI collagen and tropoelastin. The results suggest that the peptide may contain the binding sequences for both type VI collagen and tropoelastin, and thus that these two proteins may share the same binding site on MAGP-1. The interactions of MAGP-1 with type VI collagen and tropoelastin were both determined to be of moderately high affinity, withK d values of 5.6 × 10−7 m and 2.6 × 10−7 m, respectively. The findings indicate that MAGP-1 may mediate a molecular interaction between type VI collagen microfibrils and fibrillin-containing microfibrils, structures which are often found in close proximity to each other in a wide range of extracellular matrices.
Keywords: Collagen
Pepsin A
Contractile Proteins
Extracellular Matrix Proteins
Amino Acid Sequence
Protein Binding
Molecular Sequence Data
RNA Splicing Factors
Rights: © 1997 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI: 10.1074/jbc.272.36.22817
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