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FAD oxidizes the ERO1-PDI electron transfer chain: the role of membrane integrity.

Abstract：

:The molecular steps of the electron transfer in the endoplasmic reticulum from the secreted proteins during their oxidation are relatively unknown. We present here that flavine adenine dinucleotide (FAD) is a powerful oxidizer of the oxidoreductase system, Ero1 and PDI, besides the proteins of rat liver microsomes and HepG2 hepatoma cells. Inhibition of FAD transport hindered the action of FAD. Microsomal membrane integrity was mandatory for all FAD-related oxidation steps downstream of Ero1. The PDI inhibitor bacitracin could inhibit FAD-mediated oxidation of microsomal proteins and PDI, but did not hinder the FAD-driven oxidation of Ero1. Our data demonstrated that Ero1 can utilize FAD as an electron acceptor and that FAD-driven protein oxidation goes through the Ero1-PDI pathway and requires the integrity of the endoplasmic reticulum membrane. Our findings prompt further studies to elucidate the membrane-dependent steps of PDI oxidation and the role of FAD in redox folding.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Papp E,Nardai G,Mandl J,Bánhegyi G,Csermely P

doi

10.1016/j.bbrc.2005.10.027

subject

Has Abstract

pub_date

2005-12-16 00:00:00

pages

938-45

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02269-2

journal_volume

338

pub_type

杂志文章

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