Signal Transduction in Cultured Neural Cells
{'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}
Signal transduction within the central nervous system involves                  the recognition of a neurotransmitter or neuromodulator by a                    specific receptor and the subsequent activation (or inhibition)                 of a cellular event.  These cellular events (ion translocation,                 neurotransmitter release, etc.) are often mediated by second                    messengers evoked as a result of receptor occupancy.  Dr.                       Rasenick will determine how a number of components within the                   neuron are integrated with respect to the adenylate cyclase                     second messenger system.  Cultured glial, neuronal or hybrid                    cells will be permeabilized with saponin, and the components of                 the adenylate cyclase system will be probed, in situ.  Dr.                      Rasenick's laboratory has developed an assay for adenylate                      cyclase (as opposed to cAMP accumulation) in permeabilized                      cells; C6 NG.108.15 and NCB.20 cells will be used for the                       proposed experiments.  Initially, Dr. Rasenick will study the                   kinetics for the receptor mediated activation of the adenylate                  cyclase system through the stimulatory GTP binding protein                      (GNs). The agonist catalyzed activation of GNs will be studied                  with a GTP.photoaffinity probe.  This study also will examine                   the recently discovered interaction between GNs and the                         inhibitory GTP binding  protein (GNi) both through kinetic                      experiments and by photoaffinity experiments.  Dr. Rasenick has                 demonstrated that GTP analogues may be exchanged between GNs                    and GNi (as well as tubulin and GNi) in synaptic membranes; he                  further intends to examine the possible role of receptors in                    the nucleotide exchange process.  The permeabilized cells                       provide the ideal milieu for such experiments; many of the                      elements which may act in concert to modify receptor                            responsiveness are retained in this system.  As the saponin                     treated cells have holes sufficiently large to allow the                        passage of proteins and Fab fragments, a variety of experiments                 to probe the role of the cytoskeleton, as well as that of a                     newly discovered 32KDa GTP binding protein, are planned.                        Lastly, effects of morphological differentiation will be                        examined.  This research provides the exciting possibility to                   investigate the cellular response to neurotransmitters in a                     environment resembling that of the intact neuron.
{'FirstName': 'Mark', 'LastName': 'Rasenick', 'PI_MID_INIT': 'M', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Mark M Rasenick', 'EmailAddress': 'raz@uic.edu', 'NSF_ID': '000297240', 'StartDate': '03/15/1988', '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': '119200', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8719758.xml'}