Phosphorylation of Human Progesterone Receptors
{'Code': '08070000', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Bruce L. Umminger', 'PO_EMAI': None, 'PO_PHON': None}
Progesterone is a steroid hormone of fundamental importance in             reproduction.  To generate probes for studying the mechanisms of                progesterone action the progesterone receptor has been purified from            T47D, a human cell line which provides a particularly rich source of            the receptor.  Three IgG monoclonal antibodies have been raised                 against the progesterone receptor proteins.  Though only purified B-            receptors (120,000 daltons) were the antigens, 1 of the 3 antibodies            cross-reacts with A-receptors (94,000 daltons).  In the continuation            of this research immunochemistry, photoaffinity labeling and                    autoradiography will be applied to study how phosphorylation of the             progesterone receptor proteins affects their action.  The first goal            is, using whole cells, to assess the effect of progestins, and                  intracellular A- and B-receptor localization on the phosphorylation             state of the receptors, to analyze phospho-amino acids and peptides,            and to study phosphorylation of receptor-associated proteins that do            not bind hormone.  The second goal is to use reconstituted, cell-free           systems to characterize receptor kinases, particularly a putative               nuclear kinase, and to assess receptor autophosphorylation capacity.            The third goal is to determine whether the phosphorylation state of             the receptor proteins varies with relevant physiological stimuli,               including known modualtors of progesterone receptors such as                    estradiol.  In sum, the overall goal is to understand how this                  covalent modification of the progesterone receptor proteins affects             their ability to bind hormone, to acquire tight nuclear binding                 capacity, and to be down-regulated in nuclei.                                        The results of this research should further our understanding of           the mechanism of action of this important steroid hormone.
{'FirstName': 'Kathryn', 'LastName': 'Horwitz', 'PI_MID_INIT': 'B', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Kathryn B Horwitz', 'EmailAddress': None, 'NSF_ID': '000152818', 'StartDate': '12/15/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Colorado at Denver', 'CityName': 'AURORA', 'ZipCode': '800452571', 'PhoneNumber': '3037240090', 'StreetAddress': '13001 E 17TH PL STE F428', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Colorado', 'StateCode': 'CO', 'CONGRESSDISTRICT': '06', 'CONGRESS_DISTRICT_ORG': 'CO06', 'ORG_UEI_NUM': 'MW8JHK6ZYEX8', 'ORG_LGL_BUS_NAME': 'THE REGENTS OF THE UNIVERSITY OF COLORADO', 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
[{'Code': '111700', 'Text': 'CELLULAR PHYSIOLOGY'}, {'Code': '114100', 'Text': 'PHYSIOLOG & STRUCTURAL SYS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8709790.xml'}