Abstract:
:Crude membrane fractions prepared from the superficial cortical fiber cells of bovine lenses were incubated with [gamma-32P]-ATP. Membrane-associated 4.1-like proteins were then immunoprecipitated and analyzed for 32P-incorporation. Band 4.1-like proteins of 150 kd, 80 kd, and 78 kd were found to be labeled in a time-dependent fashion, with the 150 kd protein incorporating label at an 8-fold greater rate than the 80 kd and 78 kd proteins. Addition of cAMP or Ca2+ to the membrane preparations stimulated the phosphorylation of all three of these proteins. Our results indicate that the 4.1-like proteins of the lens fiber cell share with band 4.1 of the RBC the characteristic of being substrates for cAMP-independent and cAMP-dependent protein kinases.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Aster JC,Brinn K,Maisel H,Brewer GJdoi
10.1016/0006-291x(85)90308-0subject
Has Abstractpub_date
1985-02-15 00:00:00pages
1166-73issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(85)90308-0journal_volume
126pub_type
杂志文章abstract::The hepatocyte growth factor is closely related to liver regeneration. And the c-met protooncogene is reported to encode a hepatocyte growth factor receptor. Little is known, however, about how the c-met gene is activated during liver regeneration. In this study, we demonstrated that expression of the c-met gene/hepat...
journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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