Samudra S. Gangopadhyay, Ph.D.
Research Scientist
Smooth muscle biology
Email: samudra at bbri.org

Research Summary
In the United States the leading cause of death is cardiovascular disease. Understanding the molecular mechanisms of this disease is the first step towards its prevention. Defects in blood vessel cells lead to the development of stroke and various heart diseases.

The normal functioning of blood vessels involves cascades of signals from protein to protein within the muscle cells that make up the wall of the blood vessels. Ca2+/CaM dependent protein kinase II (CaM Kinase II) is one of those signaling molecules that activate major contractile regulatory proteins. The present area of investigation includes identification and cloning of the alternative splice- and alternative polyadenylation- variants of smooth muscle CaM Kinase II, their expression and biochemical characterization. The study emphasizes the functional differences in those variants in smooth muscle contractility.

Another approach of study is to understand the smooth muscle regulation by molecular scaffolds, particularly, those involved in cytoskeleton rearrangement and contractility. Calponin, a smooth muscle marker has been targeted to identify its function as an adaptor protein. The assay methods to find out its binding partners include Yeast Two-Hybrid assay, Pull-down assay, Overlay assay etc. We have recently identified Smooth muscle archvillin (SmAV) as a novel Calponin binding protein that regulates contractility and acts through a Calponin mediated signaling pathway requiring PKC and ERK1/2.

Selected Publications
Marganski, W., Gangopadhyay, S.S., Je, H.D., Gallant, C. and Morgan, K.G. Targeting of a novel Ca2+/calmodulin-dependent protein kinase II is essential For ERK-mediated signaling in differentiated smooth muscle cells. Circ Res. 2005; 97:541-549.

Gangopadhyay, S.S., Takizawa, N, Gallant, C,Barber, A.L., Je, H.D., Smith, T.C., Luna, E.J. and Morgan, K.G. Smooth Muscle Archvillin: A Novel Regulator of Signaling and Contractility in Vascular Smooth Muscle. J Cell Sci. 2004; 117:5043-5057.

Gangopadhyay, S.S., Barber, A.L., Gallant, C., Grabarek, Z., Smith J.L., and Morgan, K.G.Differential functional properties of calmodulin-dependent protein kinase II gamma variants isolated from smooth muscle. Biochem J. 2003; 372:347-357.

Je, H.D., Gangopadhyay, S.S., Ashworth, T. and Morgan, K.G. Calponin is required for agonist-induced signal transduction – evidence from an antisense approach in ferret smooth muscle. J Physiol. 2001; 537:567-577.

Morgan, K.G. and Gangopadhyay, S.S.  Cross-bridge regulation by thin filament associated proteins. J. Appl. Physiol. 2001; 91:953-962.

Leinweber, B., Parissenti, A.M., Gallant, C., Gangopadhyay, S.S., Kirwan-Rhude, A., Leavis, P.C. and Morgan, K.G. Regulation of protein kinase C by the cytoskeletal protein calponin. J Biol Chem. 2000; 275:40329-40336.

PubMed:
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