PMID: 9178102Jun 15, 1997Paper

Identification of Rad's effector-binding domain, intracellular localization, and analysis of expression in Pima Indians

Journal of Cellular Biochemistry
M A PaulikJ M Lenhard

Abstract

In order to characterize the endogenous gene product for rad (ras-related protein associated with diabetes), we prepared antibodies to synthetic peptides that correspond to amino acids (109-121, 178-195, 254-271) within the protein. These antibodies were used to analyze the expression, structure, and function of rad. Western analysis with these antibodies revealed that rad was a 46 kDa protein which was expressed during myotube formation. Further, immunolocalization studies showed that rad localized to thin filamentous regions in skeletal muscle. Interestingly, when muscle biopsies from diabetic and control Pima Indians were compared, no differences in rad protein or mRNA expression were observed. Similarly, no differences were observed in protein expression in diabetic and control Zucker diabetic fatty (ZDF) rats. Functional analysis of muscle rad revealed that its GTP-binding activity was inhibited by the addition of N-ethylmaliemide, GTP, GTP gamma S, and GDP beta S but not ATP or dithiothreitol. Moreover, cytosol-dependent rad-GTPase activity was stimulated by the peptide corresponding to amino acids 109-121. Antibodies corresponding to this epitope inhibited cytosol-dependent rad-GTPase activity. Taken together, the result...Continue Reading

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Citations

Mar 16, 2006·Proceedings of the National Academy of Sciences of the United States of America·Jacob IlanyC Ronald Kahn
Dec 7, 2007·Circulation·Lin ChangY Eugene Chen
Feb 25, 2005·The Journal of Biological Chemistry·Brian S FinlinDouglas A Andres

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