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High levels of the molecular chaperone Mdg1/ERdj4 reflect the activation state of endothelial cells.

Abstract：

:Mdg1/ERdj4, a mammalian chaperone that belongs to the HSP40 protein family, has been reported to be located in the endoplasmic reticulum (ER), is induced by ER stress, and protects ER stressed cells from apoptosis. Here we show that under normal physiological conditions, Mdg1/ERdj4 is expressed at various levels in the vasculature due to different activation states of the endothelium. To elucidate the stimuli that induce ER stress and thus upregulate Mdg1/ERdj4, we investigated the effect of several endothelium specific stressors on its expression. Mdg1/ERdj4 mRNA is induced by activated macrophages, by nitric oxide (NO) and heat shock, and during terminal cell differentiation, whereas shear stress does not affect Mdg1/ERdj4 expression levels. While the mRNA stability of BiP/GRP78 is unaffected in ER stressed cells, the stability of Mdg1/ERdj4 mRNA is prolonged during ER stress resulting in rapid increases and high levels of Mdg1/ERdj4 mRNA. Mdg1/ERdj4 protein is localized in the ER under control conditions. While heat shock induces a rapid translocation of Mdg1/ERdj4 to the nucleoli, no translocation could be observed during ER stress. This indicates that Mdg1/ERdj4 protein has diverse mechanisms to protect stressed cells from apoptosis.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Berger BJ,Müller TS,Buschmann IR,Peters K,Kirsch M,Christ B,Pröls F

doi

10.1016/s0014-4827(03)00316-1

keywords:

subject

Has Abstract

pub_date

2003-10-15 00:00:00

pages

82-92

issue

1

eissn

0014-4827

issn

1090-2422

pii

S0014482703003161

journal_volume

290

pub_type

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