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Increased Phosphorylation of Myosin Light Chain Prevents in Vitro Decidualization

Departments of Obstetrics and Gynecology (I.I., A.T.F., Z.S.) and Physiology and Biophysics (W.H., P.d.L.), University of Illinois at Chicago, Chicago, Illinois 60612; and Loyola University Medical Center (J.L.M.), Maywood, Illinois 60153

Address all correspondence and requests for reprints to: Zuzana Strakova, Ph.D., Department of Obstetrics and Gynecology, The University of Illinois at Chicago, 820 South Wood Street (M/C 808), Chicago, Illinois 60612-7313. E-mail: zstrakov{at}uic.edu.

Differentiation of stromal cells into decidual cells, which is critical to successful pregnancy, represents a complex transformation requiring changes in cytoskeletal architecture. We demonstrate that in vitro differentiation of human uterine fibroblasts into decidual cells includes down-regulation of -smooth muscle actin and ß-tubulin, phosphorylation of focal adhesion kinase, and redistribution of vinculin. This is accompanied by varied adhesion to fibronectin and a modified ability to migrate. Cytoskeletal organization is determined primarily by actin-myosin II interactions governed by the phosphorylation of myosin light chain (MLC₂₀). Decidualization induced by cAMP [with estradiol-17ß (E) and medroxyprogesterone acetate (P)] results in a 40% decrease in MLC₂₀ phosphorylation and a 55% decline in the long (214 kDa) form of myosin light-chain kinase (MLCK). Destabilization of the cytoskeleton by inhibitors of MLCK (ML-7) or myosin II ATPase (blebbistatin) accelerates decidualization induced by cAMP (with E and P) but inhibits decidualization induced by IL-1ß (with E and P). Adenoviral infection of human uterine fibroblast cells with a constitutively active form of MLCK followed by decidualization stimuli leads to a 30% increase in MLC₂₀ phosphorylation and prevents decidualization. These data provide evidence that the regulation of cytoskeletal dynamics by MLC₂₀ phosphorylation is critical for decidualization.

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