Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin.

Abstract:

:Glucose-regulated protein 58 (GRP58)-like immunoreactivity in rat liver obtained in the evening or after fasting underwent an electrophoretic band-shift, which disappeared after phosphatase-treatment. Since mass spectrometric analysis raised a possibility that Ser150 of GRP58 is phosphorylated, an antibody against the phosphoserine150 GRP58 was generated. Immunoreactivity to this antibody was increased in the evening and after fasting. Since GRP58 was shown to interact with signal transducer and activator of transduction 3 (STAT3), a leptin-related protein, the effect of leptin was examined. Immunoreactivity to the anti-phosphoGRP58 antibody was markedly elevated after the leptin injection, indicating that Ser150 of GRP58 is phosphorylated after fasting and leptin-treatment.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kita K,Okumura N,Takao T,Watanabe M,Matsubara T,Nishimura O,Nagai K

doi

10.1016/j.febslet.2005.11.074

keywords:

subject

Has Abstract

pub_date

2006-01-09 00:00:00

pages

199-205

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)01451-1

journal_volume

580

pub_type

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