Estrogen modulates Ca(2+)-independent lipid-stimulated kinase in the rabbit corpus luteum of pseudopregnancy. Identification of luteal estrogen-modulated lipid-stimulated kinase as protein kinase C delta
| Autor: | Mary Hunzicker-Dunn, Keiko Mizuno, Josephine B. Miller, Victoria Jackiw, Richard E. Cutler, Shigeo Ohno, Ellen M. Carney, Evelyn T. Maizels |
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| Rok vydání: | 1992 |
| Předmět: |
endocrine system
medicine.medical_specialty medicine.drug_class Kinase Cell Biology Luteal phase Biology Protamine Kinase Biochemistry Endocrinology medicine.anatomical_structure Estrogen Phosphoprotein Internal medicine medicine Kinase activity Molecular Biology Corpus luteum hormones hormone substitutes and hormone antagonists Protein kinase C |
| Zdroj: | Journal of Biological Chemistry. 267:17061-17068 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(18)41892-3 |
| Popis: | Rabbit corpora lutea were tested for the presence of phosphorylative responses sensitive to estrogen. Luteal Ca(2+)-independent lipid-stimulated kinase activity was detected by phosphorylation of the endogenous substrate, p76. Estrogen treatment, by way of estradiol-17 beta implant, increased levels of the lipid-stimulated phosphoprotein 2-3-fold throughout pseudopregnancy. Midpseudopregnant rabbit luteal extracts were further evaluated to determine the identity of the lipid-stimulated kinase. Results of low pH-activated phosphorylation were consistent with the identification of p76 as an autophosphorylated member of the protein kinase C (PKC) family. Partial purification of the luteal lipid-stimulated kinase was performed using sequential DEAE-cellulose/hydroxylapatite chromatographies and using gel filtration. Western immunoblot with type-specific anti-PKC delta antiserum showed coelution of kinase p76 activity with immunoreactive PKC delta. Immunoblot analysis confirmed that luteal levels of PKC delta were increased by estrogen treatment. |
| Databáze: | OpenAIRE |
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