Substrate-directed modulation of elastin oxidation by lysyl oxidase.

Abstract:

:The oxidation of an elastin substrate by highly purified bovine aortic lysyl oxidase (LO) is markedly influenced by amphiphilic molecules known to bind to elastin. Negatively charged elastin ligands, including fatty acids, bile salts or sodium dodecyl sulfate can completely inhibit the oxidation of lysine in elastin, the cationic amphiphilic ligands stimulate the enzymatic reaction five-fold, while small hydrophilic molecules of either charge or neutral detergents have no effect. In addition, evidence has been obtained that changes in the conformation of a synthetic polypeptide substrate markedly alter its susceptibility to LO. The coacervated state of the substrate is most readily oxidized and crosslinked by the enzyme. These results point to the importance of small ligands, electrostatic charge, and conformation as substrate-directed influences which can control the expression of LO activity.

journal_name

Connect Tissue Res

authors

Kagan HM,Simpson DE,Tseng L

doi

10.3109/03008208109152378

subject

Has Abstract

pub_date

1981-01-01 00:00:00

pages

213-7

issue

3-4

eissn

0300-8207

issn

1607-8438

journal_volume

8

pub_type

杂志文章
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  • Molecular events surrounding collagen fibril assembly in the early healing rabbit medial collateral ligament--failure to recapitulate normal ligament development.

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