Abstract:
:In this study we have investigated the protein phosphorylation pattern in the membrane fraction prepared from bovine luteal cells. The phosphorylation reaction was carried out in vitro, under defined conditions, using either [gamma-32P]ATP or [gamma-35S]ATP as the phosphate donor. The results obtained show that [gamma-35S]ATP was a suitable phosphate donor for performing in vitro phosphorylation studies, and that thiophosphorylation of at least eight protein bands (120 kDa to 18 kDa) was observed. The extent of phosphorylation was dependent upon the duration of incubation and the amount of membrane protein used. The presence of Ca2+ was obligatory for phosphorylation and an enhanced phosphorylation was observed in the presence of Ca2+, phosphatidyl serine and phorbol 12-myristate 13-acetate (PMA), agents known to activate protein kinase C. Interestingly, when phosphorylation was carried out in the presence of luteinizing hormone (LH), a phosphorylation pattern was obtained which was similar to that obtained in the presence of calcium and phospholipid. Furthermore, in the case of two protein bands corresponding to 80-82 and 44-46 kDa, an additive phosphorylation was observed when the phosphorylation reaction was carried out for 5 min in the presence of both LH and Ca2+, phosphatidyl serine and PMA. To conclude, we have demonstrated a calcium- and phospholipid-dependent endogenous protein phosphorylation in the membrane fraction prepared from bovine luteal cells and the data obtained suggest that LH is able to stimulate this endogenous protein phosphorylation via a protein kinase C-mediated mechanism.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Budnik LT,Mukhopadhyay AKdoi
10.1016/0303-7207(90)90018-4subject
Has Abstractpub_date
1990-03-05 00:00:00pages
245-53issue
2-3eissn
0303-7207issn
1872-8057pii
0303-7207(90)90018-4journal_volume
69pub_type
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