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C-propeptide region of human pro alpha 1 type 1 collagen interacts with thioredoxin.

Abstract：

:Thioredoxin (TRX) is one of major components of thiol reducing systems. To investigate the molecular mechanism of TRX function in the lung tissue, we screened a human lung epithelial cell cDNA library for TRX-binding protein by yeast two-hybrid systems. We isolated a plasmid containing C-propeptide region of human pro alpha 1 type 1 collagen (CP-pro alpha 1(1)). CP-pro alpha 1(1) stably binds to wild type TRX but not to mutant TRX, in which redox-active cysteine residues are substituted. Failure of the interaction of mutant TRX with CP-pro alpha 1(1) was confirmed in yeast two-hybrid systems. The CP-pro alpha 1(1)/TRX interaction was increased by dithiothreitol treatment, but was markedly inhibited by hydrogen peroxide or diamide treatment. These data showed that the reducing status of TRX active site cysteine residues is important for the TRX-CP-pro alpha 1(1) interaction, indicating that collagen biosynthesis is under the regulation of TRX-dependent redox control.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Matsumoto K,Masutani H,Nishiyama A,Hashimoto S,Gon Y,Horie T,Yodoi J

doi

10.1016/s0006-291x(02)00727-1

subject

Has Abstract

pub_date

2002-07-19 00:00:00

pages

663-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(02)00727-1

journal_volume

295

pub_type

杂志文章

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