Journal article
Protein kinase C stimulatory activity in the pseudopregnant rat ovary
Molecular and cellular endocrinology, Vol.86(1-2), pp.125-132
07/1992
DOI: 10.1016/0303-7207(92)90183-7
PMID: 1324855
Abstract
Ovarian cytosol from pseudopregnant rats was heated to 80-90 degrees C for 2 min and precipitated proteins removed by centrifugation. The supernatant of the heated ovarian cytosol contained no protein kinase C activity but when added to a control preparation containing protein kinase C, enzyme activity was increased to 200% of control. The stimulatory activity was stable to heating for 10 min, was retained on a centrifugal filtration device with a 100,000 M(r) cut-off, did not affect cAMP-dependent protein kinase, was not extractable in petroleum ether or chloroform/methanol (2:1), and enhanced the phosphorylation of protein kinase C-specific peptide substrates. The stimulatory factor was calcium-dependent and could substitute for phosphatidylserine and diacylglycerol in the protein kinase C assay. This stimulatory factor may provide a mechanism whereby the response of protein kinase C to hormonal activation could be regulated by the cell.
Details
- Title: Subtitle
- Protein kinase C stimulatory activity in the pseudopregnant rat ovary
- Creators
- K M Eyster - Department of Physiology and Pharmacology, University of South Dakota, VermillionM S WallerM J Johnson
- Resource Type
- Journal article
- Publication Details
- Molecular and cellular endocrinology, Vol.86(1-2), pp.125-132
- DOI
- 10.1016/0303-7207(92)90183-7
- PMID
- 1324855
- ISSN
- 0303-7207
- eISSN
- 1872-8057
- Grant note
- HD26640 / NICHD NIH HHS
- Language
- English
- Date published
- 07/1992
- Academic Unit
- Internal Medicine
- Record Identifier
- 9984094766602771
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