Myosin Phosphorylation and Neurotransmitter Secretion
{'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}
Transmitter release and other secretory processes have been                     compared to muscle contraction in that both processes are                       regulated by Ca2+ and depend upon metabolic energy.  Although                   secretion was thought initially to resemble the contraction of                  skeletal muscle, recent experiments suggest that it may more                    closely resemble smooth muscle contraction.  Ca2+ is known to                   regulate smooth muscle contraction through the activation of the                Ca2+/calmodulin-dependent enzyme myosin light chain kinase.  The                active enzyme phosphorylates smooth muscle myosin, which results                in a stimulation of the rate of ATP hydrolysis by actin and                     myosin.  In this study, knowledge of smooth muscle contraction                  will be used as a basis to investigate the role of myosin                       phosphorylation in catecholamine secretion.  The studies will be                performed on PC12 rat pheochromocytoma cells and on bovine                      chromaffin cells.  Myosin and myosin light chain kinase will be                 purified from chromaffin cells, and the sites on myosin that are                phosphorylated by myosin light chain kinase and by protein kinase               C will be identified.  Polyclonal antibodies against purified                   chromaffin cell myosin and myosin light chain kinase will be                    raised and used in the following experiments:  (1) Antibodies                   will be used to correlate quantitatively myosin phosphorylation                 in intact chromaffin cells with intracellular Ca2+ and with                     catecholamine secretion in response to a variety of                             secretagogues;  (2) They will be used to study the sites on                     myosin that are phosphorylated in order to identify the kinases                 that phosphorylate myosin in intact chromaffin cells;  (3) Anti-                myosin and anti-myosin light chain kinase antibodies will be                    electroinjected into chromaffin cells to study the effects of                   these antibodies on catecholamine secretion.  These experiments                 are designed to elucidate the role of site-specific myosin                      phosphorylation in the regulation of neurotransmitter secretion.                Moreover, by simultaneously studying myosin phosphorylation, cell               calcium and secretion, these studies will provide important                     information on the physiology, pharmacology and biochemistry of                 transmitter release.
{'FirstName': 'Primal', 'LastName': 'de Lanerolle', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Primal de Lanerolle', 'EmailAddress': 'Primal@uic.edu', 'NSF_ID': '000461122', 'StartDate': '05/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Illinois at Chicago', 'CityName': 'CHICAGO', 'ZipCode': '606124305', 'PhoneNumber': '3129962862', 'StreetAddress': '809 S MARSHFIELD AVE M/C 551', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Illinois', 'StateCode': 'IL', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'IL07', 'ORG_UEI_NUM': 'W8XEAJDKMXH3', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF ILLINOIS', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '118800', 'Text': 'SYNAPTIC MECHANISMS'}, {'Code': '119200', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8720429.xml'}