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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Clevenger, Charles V. Rycyzyn, Michael A. |
| Description | Author Affiliation: Rycyzyn MA ( Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.); |
| Abstract | The nuclear translocation of peptide hormones, such as the somatolactogenic hormone prolactin, after receptor internalization has been widely reported. Prolactin has been demonstrated to interact with cyclophilin B, a member of the immunophilin family of proteins. Cyclophilin B interaction with prolactin potentiated prolactin-induced proliferation, cell growth, and the nuclear retrotransport of prolactin. These effects could be abrogated by the removal of the peptidyl-prolyl isomerase activity of cyclophilin B. Our findings indicate that the intranuclear prolactin/cyclophilin B complex acts as a transcriptional inducer by interacting directly with Stat5, resulting in the removal of the Stat-repressor protein inhibitor of activated Stat 3 (PIAS3), thereby enhancing Stat5 DNA-binding activity and prolactin-induced, Stat5-mediated gene expression. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 10 |
| Volume Number | 99 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2002-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cyclophilins Metabolism DNA-Binding Proteins Milk Proteins Prolactin Trans-Activators Transcription, Genetic Animals Carrier Proteins Caseins Genetics Cell Division Cell Nucleus Peptidylprolyl Isomerase STAT5 Transcription Factor Tumor Cells, Cultured Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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