Synthesis of Dopamine-Hydroxylase, Chromogranins and        Chromaffin Vesicles by Adrenal Medullary Cells
{'Code': '08090200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'IOS', 'LongName': 'Division Of Integrative Organismal Systems'}}
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The chromaffin vesicles of the adrenal medulla participate in the               synthesis, storage and secretion of catecholamines and are                      analogous to synaptic vesicles in catecholaminergic neurons in                  the central and peripheral nervous system.  Knowledge of the                    synthesis and factors regulating the synthesis of major                         functional or constituitive proteins of the vesicles, namely                    dopamine-beta-hydroxylase and chromogranin A, and their                         incorporation into chromaffin vesicles will enhance our                         understanding of the secretory cycle in the adrenal madulla and                 sympathetic nerves.  The objectives of the proposed research are                to characterize the synthesis of dopamine-beta-hydroxylase and                  chromogranin A and their subsequent incorporation into chromaffin               vesicles, to determine whether certain factors affect these                     processes and to determine whether chromaffin vesicle membranes                 are recycled using primary cultures of adrenal medullary cells.                 The synthesis of the proteins and their incorporation into                      chromaffin vesicles will be determined by labeling cell cultures                with ı35S!methionine followed by quantitative immunoprecipitation               of the labeled proteins with monospecific anti-sera.  The                       radiochemical purity of the immunoprecipitates will be verified                 by gel electrophresis and autoradiography.                                                                                                                      Preliminary studies show that adrenal medullary cells labeled                   with ı35S!methionine secrete a highly labeled protein into the                  culture medium.  This protein is the major labeled protein which                appears in the medium and represents about 5% of the                            ı35S!methionine incorporated into total protein.  Dr. Kirshner                  proposes to:  1) further characterize the synthesis and secretion               of the protein; 2) to purify the protein and determine its                      molecular weight and subunit structure; 3) to establish its                     identity either as a known protein or as a new protein.
{'FirstName': 'Norman', 'LastName': 'Kirshner', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Norman Kirshner', 'EmailAddress': None, 'NSF_ID': '000206092', 'StartDate': '08/15/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Duke University', 'CityName': 'DURHAM', 'ZipCode': '277054640', 'PhoneNumber': '9196843030', 'StreetAddress': '2200 W MAIN ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'NC04', 'ORG_UEI_NUM': 'TP7EK8DZV6N5', 'ORG_LGL_BUS_NAME': 'DUKE UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1192', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8701525.xml'}