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 Lettjournal_title
FEBS lettersauthors
Kita K,Okumura N,Takao T,Watanabe M,Matsubara T,Nishimura O,Nagai Kdoi
10.1016/j.febslet.2005.11.074keywords:
subject
Has Abstractpub_date
2006-01-09 00:00:00pages
199-205issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(05)01451-1journal_volume
580pub_type
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