1992
DOI: 10.1016/s0021-9258(19)50337-4
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Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction.

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Cited by 427 publications
(41 citation statements)
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“…Thus, the most reasonable explanation for our observations is that caffeine treatment leads to reduced intracellular [Ca 2T ], which in turn potentiates the effect of injected antibodies. Interaction of the Rho family of GTPases with Ca 2+ signaling has also been reported in animal and fungal cells (Miyamoto et al, 1987;Bender and Pringle, 1989;Hirata et al, 1992;Gronroos et al, 1996;Peppelenbosch et al, 1996).…”
Section: Min Aftermentioning
confidence: 83%
“…Thus, the most reasonable explanation for our observations is that caffeine treatment leads to reduced intracellular [Ca 2T ], which in turn potentiates the effect of injected antibodies. Interaction of the Rho family of GTPases with Ca 2+ signaling has also been reported in animal and fungal cells (Miyamoto et al, 1987;Bender and Pringle, 1989;Hirata et al, 1992;Gronroos et al, 1996;Peppelenbosch et al, 1996).…”
Section: Min Aftermentioning
confidence: 83%
“…The RhoA protein is a well-known member of the p21 Ras superfamily of small GTPases, which shuttles between an inactive GDP-bound state and an active GTP-bound state and exhibits intrinsic GTPase activities. RhoA regulates signal transduction from cell surface receptors to intracellular target molecules and is involved in a variety of biological processes, including cell morphology (Paterson et al 1990), motility (Takaishi et al 1993), smooth muscle contraction (Hirata et al 1992), and tumor progression (Prendergast et al 1995), and RhoA also acts as a molecular switch. Previous reports have shown that overexpression of RhoA facilitated the accumulation of RhoA protein in the cell membrane and led to further RhoA activation (Horiuchi et al 2008).…”
Section: Discussionmentioning
confidence: 99%
“…For example, eight years ago it was found that injection into fibroblasts of antibodies raised against MLC kinase induced a decrease in MLC phosphorylation accompanied by the loss of stress fibres [27]. Lysophosphatidic acid (LPA) rapidly stimulates MLC phosphorylation, and various inhibitors of MLC kinase have been reported to prevent LPA-and Rhoinduced contractility and stress-fibre formation [26,28]. Furthermore, it has been shown that Rho is involved in regulating smooth-muscle cell contraction, a process dependent on MLC phosphorylation [29].…”
Section: Rho and The Actin Cytoskeletonmentioning
confidence: 99%