title: Possible interrelationship between changes in F-actin and myosin II, protein phosphorylation, and cell volume regulation in Ehrlich ascites tumor cells.
abstract: Osmotic shrinkage of Ehrlich ascites tumor cells (EATC) elicited translocation of myosin II from the cytosol to the cortical region, and swelling elicits concentration of myosin II in the Golgi region. Rho kinase and p38 both appeared to be involved in shrinkage-induced myosin II reorganization. In contrast, the previously reported shrinkage-induced actin polymerization [Pedersen et al. (1999) Exp. Cell Res. 252, 63-74] was independent of Rho kinase, p38, myosin light chain kinase (MLCK), and protein kinase C (PKC), which thus do not exert their effects on the shrinkage-activated transporters via effects on F-actin. The subsequent F-actin depolymerization, however, appeared MLCK- and PKC-dependent, and the initial swelling-induced F-actin depolymerization was MLCK-dependent; both effects were apparently secondary to kinase-mediated effects on cell volume changes. NHE1 in EATC is activated both by osmotic shrinkage and by the serine/threonine phosphatase inhibitor Calyculin A (CL-A). Both stimuli caused Rho kinase-dependent myosin II relocation to the cortical cytoplasm, but in contrast to the shrinkage-induced F-actin polymerization, CL-A treatment elicited a slight F-actin depolymerization. Moreover, Rho kinase inhibition did not significantly affect NHE1 activation, neither by shrinkage nor by CL-A. Implications for the possible interrelationship between changes in F-actin and myosin II, protein phosphorylation, and cell volume regulation are discussed.
authors.affiliation: Department of Biochemistry, August Krogh Institute, University of Copenhagen, Denmark. sfpedersen@aki.ku.dk
authors.forename: S F
authors.initials: SF
authors.lastname: Pedersen
authors.forename: E K
authors.initials: EK
authors.lastname: Hoffmann
mesh_terms: D000199:Actins / Q000378:metabolism*; D000577:Amides / Q000494:pharmacology; D000818:Animals; D000906:Antibodies / Q000276:immunology; D001381:Azepines / Q000494:pharmacology; D002286:Carcinoma, Ehrlich Tumor; D048429:Cell Size; D004789:Enzyme Activation; D007552:Isotonic Solutions; D008387:Marine Toxins; D051379:Mice; D024462:Myosin Type II / Q000276:immunology / Q000378:metabolism*; D009281:Naphthalenes / Q000494:pharmacology; D009995:Osmosis; D010080:Oxazoles / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors; D010766:Phosphorylation; D020033:Protein Isoforms / Q000276:immunology; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism; D011725:Pyridines / Q000494:pharmacology; D015398:Signal Transduction; D017923:Sodium-Hydrogen Exchangers / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: D000199:Actins; D000577:Amides; D000906:Antibodies; D001381:Azepines; D007552:Isotonic Solutions; D008387:Marine Toxins; D009281:Naphthalenes; D010080:Oxazoles; D020033:Protein Isoforms; D011725:Pyridines; D017923:Sodium-Hydrogen Exchangers; C069139:growth factor-activatable Na-H exchanger NHE-1; C070571:ML 7; C108830:Y 27632; C059041:calyculin A; D017346:Protein Serine-Threonine Kinases; D010749:Phosphoprotein Phosphatases; D024462:Myosin Type II