Calcium-Dependent Proteolysis in Mammalian Cells
{'Code': '08060200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'DCB', 'LongName': 'Division of Cellular Biosciences'}}
{'SignBlockName': 'Maryanna P. Henkart', 'PO_EMAI': None, 'PO_PHON': None}
The goals of this research are, first to develop a widely                       applicable assay for measuring the activation of calcium-                       dependent proteases ("calpains", EC 3.4.22.17), and second, to                  determine whether alterations in calcium homeostasis, either                    influx through the plasma membrane or release of intracellular                  calcium stores regulate autoproteolytic activation of these                     proteases.  The results of these studies will provide the basis                 for subsequent investigations to identify physiological                         substrates, which may include talin, filamin, fodrin and protein                kinase C, and the consequences of proteolytic modification on the               functions of these proteins.                                                                                                                                    An increase in intracellular calcium is one important type of                   cellular response to certain external signals.  Mechanisms by                   which a generalized increase in intracellular calcium is                        translated into specific, local effects on different cellular                   functions are currently being sought and studied by many                        laboratories.  One such mechanism which has only begun to be                    appreciated is the activation by calcium of specific protease                   enzymes. This mechanism is potentially of great importance, but                 the absence of an assay for calcium-dependent proteases in cells                has prevented elucidation of the details of their regulation and                identification of their physiological substrates.  Thus, the                    contributions of these enzymes to localized, calcium-dependent                  processes such as secretion, membrane fusion, and other cellular                functions have remained obscure.  The results of this research                  promise to provide a new dimension of insight into the mechanisms               of cellular signalling involving calcium.
{'FirstName': 'Dorothy', 'LastName': 'Croall', 'PI_MID_INIT': 'E', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Dorothy E Croall', 'EmailAddress': 'croall@maine.edu', 'NSF_ID': '000198392', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Texas Southwestern Medical Center', 'CityName': 'DALLAS', 'ZipCode': '753907208', 'PhoneNumber': '2146484494', 'StreetAddress': '5323 HARRY HINES BLVD', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Texas', 'StateCode': 'TX', 'CONGRESSDISTRICT': '30', 'CONGRESS_DISTRICT_ORG': 'TX30', 'ORG_UEI_NUM': 'YZJ6DKPM4W63', 'ORG_LGL_BUS_NAME': 'THE UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER', 'ORG_PRNT_UEI_NUM': 'X5NKD2NFF2V3'}
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[{'Code': '111400', 'Text': 'Cellular Dynamics and Function'}, {'Code': '111700', 'Text': 'CELLULAR PHYSIOLOGY'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8812433.xml'}