Calcatin: Inhibitor Protein of the Ca-ATPase
{'Code': '08070600', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Maryanna P. Henkart', 'PO_EMAI': None, 'PO_PHON': None}
It has been proposed that cells contain a calcium-dependent                     protein, "calcatin", that specifically inhibits the calcium-                    ATPase.  Since the calcium ATPase is the enzymatic activity                     underlying the calcium pump, calcatin could affect the ability of               the cell to control intracellular calcium.  This laboratory has                 identified and purified a protein that may be calcatin.  The                    proposed research is directed toward verifying that this protein                is, indeed, responsible for the observed inhibition of the                      calcium-ATPase, characterizing the protein, and assessing its                   potential role in regulating the calcium-ATPase.  The specific                  aims of the project are to:  1) complete the purificaiton of the                protein identified as calcatin; 2) determine whether the purified               protein is calcatin, the proposed inhibitor; 3) raise antibodies                to calcatin (to inhibit its activity and to use in affinity                     purification for the large scale production of calcatin); 4)                    characterize the biochemical and physical properties of calcatin;               5) determine the mechanism by which calcatin inhibits the                       calcium-ATPase; 6) determine whether calcatin inhibits the                      calcium pump.                                                                                                                                                   This research may lead to the identification of a calcium-                      dependent protein, "calcatin", that regulates the calcium-ATPase                or "calcium pump".  This would be of major physiological                        significance, because the calcium-ATPase is one of the most                     important mechanisms controlling intracellular calcium.  The                    calcium-ATPase of the human red cell is an ideal model system in                which to study the effects of calcatin, because the enzyme has                  been purified and its interaction with other modifiers (calcium,                ATP, and calmodulin) has already been extensively characterized.                Ultimately it should be possible to study the interaction of the                regulatory protein, calcatin, with the purified calcium-ATPase at               the molecular level.
[{'FirstName': 'Daniel', 'LastName': 'Walz', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Daniel A Walz', 'EmailAddress': 'dwalz@med.wayne.edu', 'NSF_ID': '000123162', 'StartDate': '05/01/1990', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}, {'FirstName': 'Douglas', 'LastName': 'Yingst', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Douglas Yingst', 'EmailAddress': 'dyingst@med.wayne.edu', 'NSF_ID': '000295061', 'StartDate': '05/01/1990', 'EndDate': None, 'RoleCode': 'Principal Investigator'}]
{'Name': 'Wayne State University', 'CityName': 'DETROIT', 'ZipCode': '482023692', 'PhoneNumber': '3135772424', 'StreetAddress': '5700 CASS AVE STE 4900', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Michigan', 'StateCode': 'MI', 'CONGRESSDISTRICT': '13', 'CONGRESS_DISTRICT_ORG': 'MI13', 'ORG_UEI_NUM': 'M6K6NTJ2MNE5', 'ORG_LGL_BUS_NAME': 'WAYNE STATE UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1114', 'Text': 'Cellular Dynamics and Function'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8817269.xml'}