Molecular Mechanisms of Regulation of Tyrosine Hydroxylase
{'Code': '08090200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'IOS', 'LongName': 'Division Of Integrative Organismal Systems'}}
{'SignBlockName': 'Stacy Springer'}
Tyrosine hydroxylase (TH) is the enzyme which catalyzes the rate                limiting step in the biosynthesis of catecholamines.  TH is                     subject to both short-term and long-term regulation.  Regulation                of TH is influenced by steroids, growth factors, increased                      neuronal activity, cold and immolization stress, treatment with                 protein kinases and drug treatment.                                                                                                                             The short-term activation of TH (within minutes) involves                       phosphorylation of the enzyme.  Four phosphorylation sites have                 been localized on the N-terminal regulatory alteration of mRNA                  levels.                                                                                                                                                         This research project will study the mechanism for long-term                    regulation of TH activity, protein and mRNA levels by treatment                 with elevated potassium, which depolarizes the neurons and is a                 model for sustained neuronal activity.                                                                                                                          A full-length cDNA for this enzyme will be cloned and expressed                 in a tissue culture cell which does not normally make tyrosine                  hydroxylase.  This will be a first step to begin to change                      specific phosphorylation sites in the cDNA and determine the                    activation of the enzyme.                                                                                                                                       The study should lead to valuable information in understanding                  the molecular basis for the complex regulation of catecholamine                 biosynthesis.
{'FirstName': 'Esther', 'LastName': 'Sabban', 'EmailAddress': 'sabban@nymc.edu', 'StartDate': '04/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'New York Medical College', 'CityName': 'Valhalla', 'ZipCode': '105951524', 'PhoneNumber': '9145942600', 'StreetAddress': '40 Sunshine Cottage Road', 'CountryName': 'United States', 'StateName': 'New York', 'StateCode': 'NY'}
{'Code': '1192', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8819918.xml'}