Neurochemistry of Schwann 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}
Two experimental animal models of neuropathy permit the in                 vivo assessment of alterations in Schwann cell metabolism that                  occur during the presence and absence of myelin assembly.  The                  crush-injured, adult rat sciatic nerve permits the analysis of                  Schwann cell metabolism during active myelin assembly whereas the               permanently transected nerve permits analysis of Schwann cells in               the absence of myelin assembly.  The purpose of this grant                      application is to determine the biosynthetic control mechanisms                 in the post-translational processing of the major myelin protein                (PO) expressed by Schwann cells in these two models of                          neuropathy.  This will be compared to the processing events in                  the normal adult nerve, as well as the nerve during development.                Processing events that will be investigated will include                        glycosylation, phosphorylation, sulfation, and acylation.  In                   addition, by directly comparing these events, using the                         appropriate radioactive precursor, it should be possible to                     assess the sequence of these post translational modifications.                  Scientific methods to be employed include 1) radioactive                        precursor incorporation into PO after in vitro incubation                       gradient electrophoresis as identified by fluorography and                      autoradiography; c) serial lectin affinity chromatography coupled               with endoglycosidase and exoglycosidase digestion to determine                  the precise oligosaccharide structure calibrated gel filtration                 and high performance liquid chromatography.  The post-                          translational modification of proteins is an important processing               event which governs the appropriate targeting of proteins to                    their often uniquely determined by the protein modifications.                   Little information is available concerning the mechanism which                  regulate these post-translational control mechanisms will foster                future research concerning potential abnormal protein processing                resulting in defective intra- or extracellular targeting and                    subsequent disruption of cellular communication.
{'FirstName': 'Joseph', 'LastName': 'Poduslo', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Joseph F Poduslo', 'EmailAddress': None, 'NSF_ID': '000196084', 'StartDate': '01/15/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Mayo Clinic Rochester', 'CityName': 'ROCHESTER', 'ZipCode': '559050001', 'PhoneNumber': '5072844715', 'StreetAddress': '200 1ST ST SW', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Minnesota', 'StateCode': 'MN', 'CONGRESSDISTRICT': '01', 'CONGRESS_DISTRICT_ORG': 'MN01', 'ORG_UEI_NUM': 'Y2K4F9RPRRG7', 'ORG_LGL_BUS_NAME': 'MAYO CLINIC', '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': '1192', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8706703.xml'}