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2004 MAY 14 - (NewsRx.com & NewsRx.net) -- Phosphorylated HSP27 is essential for acetylcholine-induced association of RhoA with PKC alpha.
According to a study from the United States, "Reorganization of the cytoskeleton and association of contractile proteins are important steps in modulating smooth muscle contraction. Heat shock protein (HSP) 27 has significant effects on actin cytoskeletal reorganization during smooth muscle contraction. We investigated the role of phosphorylated HSP27 in modulating acetylcholine-induced sustained contraction of smooth muscle cells from the rabbit colon by transfecting smooth muscle cells with phosphomimic (3D) or nonphosphomimic (3G) HSP27.
"In 3G cells, the initial peak contractile response at 30 seconds was inhibited by 25% (24.0[+ or -]4.5% decrease in cell length, n=4)," reported Suresh B. Patil and colleagues at the University of Michigan. "The sustained contraction was greatly inhibited by 75% [9.3[+ or -]0.9% decreases in cell length (n=4)]. Furthermore, in 3D cells, translocation of both PKCalpha and of RhoA was greatly enhanced and resulted in a greater association of PKCalpha-RhoA in the membrane fraction. In 3G transfected cells, PKCalpha and RhoA failed to translocate in response to stimulation with acetylcholine, resulting in an inhibition of association of PKCalpha-RhoA in the membrane fraction.
Source: HighBeam Research, Phosphorylated HSP27 essential for association of RhoA with PKC alpha.