Biochemical Mechanisms Regulating Cellular Response to      Growth Factors
{'Code': '08090200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'IOS', 'LongName': 'Division Of Integrative Organismal Systems'}}
{'SignBlockName': 'Stacy Springer', 'PO_EMAI': None, 'PO_PHON': None}
Dr. Vulliet's research will investigate the biochemical                         mechanisms controlling cellular responses to growth factors.                    Previous work has demonstrated that PC12 cells respond to                       treatment with nerve growth factor (NGF) and epidermal growth                   factor (EGF) by altering the phosphorylation of specific                        proteins.  Dr. Vulliet has identified a unique site distinct from               other known phosphorylation sites on tyrosine hydroxylase that is               phosphorylated following NGF and EGF treatment.  The amino acid                 sequence around this site suggests that it may be phosphorylated                by a novel protein kinase.  Screening of other known kinases for                their ability to phosphorylate tyrosine hydroxylase has failed to               demonstrate any phosphorylation of this specific site.  Using a                 synthetic peptide identical with the first 19 amino acids of                    tyrosine hydroxylase, Dr. Vulliet has developed an assay for this               kinase activity and succeeded in obtaining a partial purification               and characterization of this protein kinase.  Dr. Vulliet now                   proposes to further isolate, purify and characterize this novel                 kinase activity by employing a combination of traditional                       biochemical techniques and FPLC methods to develop a rapid                      purification of this kinase from pheochromocytoma tissue.  Other                embryonic and neoplastic tissues will be examined for the                       presence of this particular kinase activity.  The biochemical and               kinetic properties of this enzyme will be investigated.  In                     addition, the physiological function of this kinase will be                     investigated in PC12 cells treated with a variety of growth                     factors.  Dr. Vulliet anticipates that this novel protein kinase                may play an important role in mediating the biochemical responses               of the PC12 cells to NGF and EGF.
{'FirstName': 'Philip', 'LastName': 'Vulliet', 'PI_MID_INIT': 'R', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Philip R Vulliet', 'EmailAddress': None, 'NSF_ID': '000439488', 'StartDate': '05/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Davis', 'CityName': 'DAVIS', 'ZipCode': '956186153', 'PhoneNumber': '5307547700', 'StreetAddress': '1850 RESEARCH PARK DR STE 300', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'CA04', 'ORG_UEI_NUM': 'TX2DAGQPENZ5', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF CALIFORNIA, DAVIS', 'ORG_PRNT_UEI_NUM': 'NUDGYLBB4S99'}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1192', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8716846.xml'}