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Journal of Histochemistry and Cytochemistry
Volume 52 (4): 517-527, 2004
Copyright ©The Histochemical Society, Inc.

Involvement of Myosin II in Dopamine-induced Reorganization of the Lactotroph Cell's Actin Cytoskeleton

María L. Vitale and M. Eloísa Carbajal

Département de Pathologie et Biologie Cellulaire, Faculté de Médecine, Université de Montréal, Montréal, QC, Canada

Correspondence to: María L. Vitale, Dept. Pathologie et Biologie Cellulaire, Faculté de Médecine, Université de Montréal, 2900 Édouard-Montpetit, Montréal, Québec H3T 1J4, Canada. E-mail: maria.leiza.vitale{at}umontreal.ca

We have shown that dopamine (DA), an inhibitor of prolactin secretion from anterior pituitary lactotrophs, stabilizes the cortical actin cytoskeleton. DA-induced cortical actin stabilization is accompanied by cytoplasmic actin cable disassembly and cell rounding up. Our aim was to identify the mechanisms involved in DA-induced stabilization of the lactotroph's actin cytoskeleton. Here we show that DA increased the association of myosin II with the cell cortex, suggesting that DA facilitates actin–myosin interaction to stabilize cortical actin filaments. This notion was supported by the finding that inhibitors of actin–myosin interaction blocked DA-evoked morphological responses. In addition, our results showed that DA-induced myosin association with the cell periphery may be mediated by inhibition of Rac1/Cdc42-dependent pathways, whereas, DA-induced cytoplasmic actin filament disassembly may be mediated by the inhibition of MLCK- and RhoA-dependent pathways. In conclusion, the present results provide evidence that myosin II is involved in the DA-induced remodeling of actin filaments in lactotrophs, and that DA-induced cortical actin filament assembly and stabilization involve the translocation of myosin II to the cell cortex. This effect requires, among other things, inhibition of the Rac1/Cdc42-dependent signaling pathway. (J Histochem Cytochem 52:517–527, 2004)

Key Words: dopamine • lactotrophs • actin • myosin II


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