Dual Effect of Prolactin on Protein Kinase C Activity in CHO Cells Expressing Functional Prolactin Receptors
Autor: | M. C. Audy, Anne-Marie Vacher, Bernard Dufy, Pierre Vacher |
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Rok vydání: | 1996 |
Předmět: |
endocrine system
medicine.medical_specialty endocrine system diseases Endocrinology Diabetes and Metabolism Clinical Biochemistry Genistein Biology chemistry.chemical_compound Internal medicine medicine Staurosporine Pharmacology (medical) Receptor Molecular Biology Protein kinase C Chinese hamster ovary cell Biochemistry (medical) Cell Biology General Medicine Molecular biology Prolactin Cytosol Endocrinology chemistry Tyrosine kinase hormones hormone substitutes and hormone antagonists medicine.drug |
Zdroj: | Journal of Biomedical Science. 3:126-132 |
ISSN: | 1423-0127 1021-7770 |
Popis: | We investigated the effects of prolactin (PRL) on the protein kinase C (PKC) activity in Chinese hamster ovary (CHO-E32) cells stably transfected with rabbit mammary gland PRL receptor cDNA. These cells express a functional long form of PRL-R. A 10-min to 2-hour treatment with 5 nM PRL resulted in the translocation of PKC activity from the cytosol to the membrane. Longer treatment (10-24 h) with the same concentration of PRL decreased the PKC activity in both particulate and cytoplasmic fractions. The PRL effect was dose dependent: maximal action was obtained with 1-10 nM. The PRL-induced activation of PKC was blocked by 20 nM staurosporine, a PKC inhibitor. Two inhibitors of tyrosine kinase, herbimycin A (1.75mgr;M) and genistein (100mgr;M), had no effect on PRL-induced activation of PKC. Copyright 1996 S. Karger AG, Basel |
Databáze: | OpenAIRE |
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