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Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase

¹Department of Physiology, University of Oklahoma Health Science Center, Oklahoma City, Oklahoma 73104; and ²Division of Gastroenterology, University of Texas Medical Branch, Galveston, Texas 77555

Submitted 26 February 2004 ; accepted in final form 5 April 2004

ABSTRACT

The capsaicin receptor TRPV1 is a nonselective cation channel that is expressed in sensory neurons. In this study, we examined the role of the nonreceptor cellular tyrosine kinase c-Src kinase in the modulation of the rat TRPV1. Capsaicin-induced currents in identified colonic dorsal root ganglion neurons were blocked by the c-Src kinase inhibitor PP2 and enhanced by the tyrosine phosphatase inhibitor sodium orthovandate. PP2 also abolished currents in human embryonic kidney-293 cells transfected with rat TRPV1, whereas cotransfection of TRPV1 with v-Src resulted in fivefold increase in capsaicin-induced currents. In cells transfected with dominant-negative c-Src and TRPV1, capsaicin-induced currents were decreased by approximately fourfold. TRPV1 co-immunoprecipitated with Src kinase and was tyrosine phosphorylated. These studies demonstrate that TRPV1 is a potential target for cellular tyrosine kinase-dependent phosphorylation.

capsaicin; pp⁶⁰; cation channel; immunoprecipitation; inflammatory bowel disease; pain

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