Ganglioside Binding Sites of Cell Adhesion Molecules
{'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}
The overall goal of the proposal is to determine the role of               the newly described ganglioside binding sites of both fibroblasts               and its 140 kD cell surface receptor protein in the mechanism of                cell adhesion. The PI recently demonstrated a ganglioside binding               site in the amino terminal domain of fibronectin and proposes to                further define the role of the ganglioside binding site in cell                 adhesion.  Using a quantitative binding assay, termed fluoresence               polarization, he will study the structure and and function of the               ganglioside binding sites of both fibronectin and its receptor.                 The fluorescence polarization assay will be used for studying the               binding of gangliosides to the 140 kD fibronectin receptor and                  platelet membrane glycoprotein IIb/IIIa. He will also determine                 the specificity of the receptors for both various ganglioside                   species and divalent cations.  Another objective is to determine                the precise site on fibronectin which binds gangliosides by (a)                 limited proteolytic digestion of fibronectin and (b) expression                 of the region of the fibronectin gene that codes for the                        ganglioside binding site.  Fluorescence polarization will also be               used to quantitatively measure cooperative interactions between                 the ganglioside binding site and other fibronectin binding sites.               Cell adhesion mutants will be used to examine the role of                       gangliosides in cell adhesion, and the molecular basis of the                   phenotype will be analyzed.                                                           The molecular basis of specific and non-specific                          interactions between cells, and between cells and the substrate,                is a important area of research in cell biology.  The proposed                  work promises to provide important new information concerning one               type of interaction, adhesion, and combines both biochemical and                molecular genetic approaches in a clever and productive way.
{'FirstName': 'Robert', 'LastName': 'Klebe', 'PI_MID_INIT': 'J', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Robert J Klebe', 'EmailAddress': 'rklebe@email.msn.com', 'NSF_ID': '000218462', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Texas Health Science Center San Antonio', 'CityName': 'SAN ANTONIO', 'ZipCode': '782293901', 'PhoneNumber': '2105672340', 'StreetAddress': '7703 FLOYD CURL DR', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Texas', 'StateCode': 'TX', 'CONGRESSDISTRICT': '20', 'CONGRESS_DISTRICT_ORG': 'TX20', 'ORG_UEI_NUM': 'C3KXNLTAAY98', 'ORG_LGL_BUS_NAME': 'THE UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO', 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '111400', 'Text': 'Cellular Dynamics and Function'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1986&All=true', 'xml': '8617256.xml'}