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Insulin binds to type V collagen with retention of mitogenic activity.

Abstract：

:The abilities of eight extracellular matrix proteins, fibronectin, vitronectin, laminin, and collagen types I, II, III, IV, and V to bind insulin were examined by binding studies with insulin conjugated with peroxidase. At a physiological pH and ionic strength, type V collagen bound to insulin most strongly. The other types of collagen, laminin, and vitronectin also bound insulin with affinity lower than that of type V collagen. The insulin-binding site of type V collagen was in a 30-kDa CNBr fragment of the alpha 1 (V) chain. Analysis of the amino acid sequence showed that this 30-kDa fragment was identical to the heparin-binding fragment of type V collagen. The insulin-binding sites of laminin and vitronectin were located in the A chain and in the heparin-binding domain, respectively. Insulin bound to type V collagen stimulated the synthesis of DNA by mouse mammary tumor MTD cells, indicating that bound insulin retained mitogenic activity.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Yaoi Y,Hashimoto K,Takahara K,Kato I

doi

10.1016/0014-4827(91)90351-t

subject

Has Abstract

pub_date

1991-06-01 00:00:00

pages

180-5

issue

2

eissn

0014-4827

issn

1090-2422

pii

0014-4827(91)90351-T

journal_volume

194

pub_type

杂志文章

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