Modulation of Estrogen Receptor Levels in Mouse Uterus by Protein Kinase C Isoenzymes1

Autor:	Silvia Migliaccio, Silvia Fillo, William C. Wetsel, Hector Rivera, Anna Teti, Kenneth S. Korach, Todd F. Washburn
Rok vydání:	1998
Předmět:	medicine.medical_specialty Messenger RNA medicine.diagnostic_test medicine.drug_class Estrogen receptor Transfection Biology Molecular biology Cytosol Endocrinology Western blot Estrogen Internal medicine medicine Northern blot Protein kinase C
Zdroj:	Endocrinology. 139:4598-4606
ISSN:	1945-7170 0013-7227
DOI:	10.1210/endo.139.11.6300
Popis:	We have recently shown that protein kinase C (PKC) modifies estrogen receptor (ER) binding and modulates the responsiveness to estrogens in a clonal osteoblast-like cell line stably transfected with the ER. The purpose of the present study was to determine whether the interaction observed between the ER and PKC signaling in these cells occurs in additional estrogen target organs, such as the uterus. When uteri were incubated for 2 h with increasing concentrations of a kinase inhibitor (H7), ER binding was enhanced in a dose-dependent manner. Stimulation of PKC with phorbol ester reduced PKC activity levels, but increased ER binding. Interestingly, the changes in binding appeared to be due primarily to alterations in cytosolic ER levels, as binding in the nuclear fraction was minimally enhanced. When levels of ER messenger RNA were evaluated by Northern blot analysis, no differences were observed among the H7- or 12-O-tetradecanoylphorbol-13-acetate (TPA)-treated and untreated groups. Western blot analysis...
Databáze:	OpenAIRE
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