Protein kinase A and C activities and endogenous substrates in ovine small and large luteal cells.
作者： Patricia B. Hoyer , Wuyi Kong
DOI: 10.1016/0303-7207(89)90007-5
关键词: Cell type 、 cGMP-dependent protein kinase 、 Biology 、 Kinase 、 Protein kinase A 、 Molecular biology 、 Akt/PKB signaling pathway 、 Biochemistry 、 Phosphoprotein 、 Protein kinase C 、 Phosphorylation
摘要: Protein kinase A (cAMP-dependent) and C (calcium, phospholipid-dependent) activities were measured in vitro phosphorylation of endogenous proteins by these kinases observed SDS-PAGE 100000 × g supernatant (soluble) fractions ovine small (12–22 μm) large (> 22 luteal cells. No differences stimulation (P 0.05) By direct comparison, greater < over basal versus (6.1- 2.9-fold) was These stimulations than those cells (A kinase, 4.8-fold; 1.8-fold). Maximal specific both (per mg protein) cells. Endogenous that could serve as substrates for differed between Phosphorylation six consistently One protein (37 kDa) appeared to a preferred substrate (81 predominantly phosphorylated rather calcium-dependent, kinase-indepen- dent mechanism. These results support the accepted role cAMP via possible regulating Steroidogenesis The inability respond with enhanced secretion progesterone may be due an unavailability phosphoprotein kinase. Furthermore, activity available display quantitative qualitative Differences regulation cell types differences.
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