Kailash N. Pandey, PhD
Professor of Physiology
Structure-function relationship of different domains of NPRA cDNA by deletion and site-directed mutagenesis of the structural components
Dr. Pandey received his Ph.D. in Cell Biology from the University of Kentucky in 1979. He carried out postdoctoral studies in the Department of Biochemistry at Vanderbilt University and in 1986 was appointed as a faculty member. In 1990 he joined the faculty of the Medical College of Georgia as an Associate Professor in the Department of Biochemistry and Molecular Biology. Dr. Pandey joined Tulane in 1997. He has served on the Editorial Board of Endocrinology and reviewed manuscripts for a number of other journals. He has served on AHA, NIH and NSF grant review committees. The long-term objectives of his research projects are to delineate the molecular and cellular action of atrial natriuretic peptide (ANP) hormone, which controls natriuresis, diuresis, cell proliferation, and steroidogenesis. The regulatory action of ANP is mediated by interacting with the guanylyl cyclase/natriuretic peptide receptor-A (NPRA) that synthesizes the intracellular second messenger cyclic-GMP. Interaction of ANP with the NPRA plays a central role in the pathophysiology of hypertension and cardiovascular disorders.
The current studies in his laboratory are aimed at examining the structure-function relationship of different domains of NPRA cDNA by deletion and site-directed mutagenesis of the structural components that may be involved in ligand-binding, activation of protein kinase-like domain, cGMP production, and receptor down-regulation and desensitization. These studies involve the analysis of the molecular determinants in receptor sequence mediating the overall functional ability of NPRA, critical for the hormone-dependent signaling process. Dr. Pandey has expanded his recent studies to examine the transcriptional regulation and function of the murine NPRA gene promotor using model cell lines and the NPRA gene-targeted mutant mice generated by homologous recombination that either disrupted (knockout) or duplicated the NPRA gene. The impact of NPRA gene dosage and null mutation should help to determine the function of the receptor in vivo and in cultured cells in vitro. These ongoing studies should provide the means to directly test the efficacy of NPRA regulatory elements and the impact of NPRA gene dosage and null mutation in ANP/cGMP-mediated biological responses.
Kailash N. Pandey, PhD
Department of Physiology
1430 Tulane Avenue, SL-39
New Orleans, LA 70112
1430 Tulane Ave, New Orleans, LA 70112 504-988-5187 email@example.com