title: Tyrosine phosphorylation and subcellular localization of focal adhesion proteins during in vitro decidualization of human endometrial stromal cells.
abstract: Human endometrial stromal cells undergo in vitro decidualization when treated with progesterone and estrogen. Using this model, we previously reported specific changes in the c-Src kinase activity and tyrosine phosphorylation of several proteins during in vitro decidualization. Focal adhesion kinase (FAK) and paxillin are known to form a complex with c-Src at the focal contacts and to participate in the integrin-mediated signal transduction as c-Src substrates. We here examined the tyrosine phosphorylation and subcellular localization of the focal adhesion proteins in stromal cells isolated from human endometrium. We found, however, that the total levels of FAK and paxillin tyrosine phosphorylation were not markedly changed during decidualization or after steroid withdrawal. In our culture system numerous multicellular nodules were developed in cultures of decidualized stromal cells, within whose nodules the focal contacts were found to disappear. Moreover, disruption of the focal contacts was accompanied by disorganization of the actin-based cytoskeleton. These findings suggest that tyrosine phosphorylation of the endometrial paxillin and FAK is not tightly regulated by the kinase activity of c-Src during in vitro decidualization. The escape from regulation by c-Src may be in part due to the dissociation of the focal adhesion proteins/c-Src complex caused by the breakdown of the focal adhesion plaques as well as the loss of the actin-based cytoskeletal architecture.
authors.affiliation: Department of Obstetrics and Gynecology, Keio University School of Medicine, Tokyo, Japan. maruyamt@exchange.nih.gov
authors.forename: T
authors.initials: T
authors.lastname: Maruyama
authors.forename: Y
authors.initials: Y
authors.lastname: Yoshimura
authors.forename: H
authors.initials: H
authors.lastname: Sabe
mesh_terms: D000081247:CSK Tyrosine-Protein Kinase; D015815:Cell Adhesion Molecules / Q000032:analysis / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000032:analysis / Q000378:metabolism; D003599:Cytoskeleton / Q000648:ultrastructure; D003656:Decidua / Q000502:physiology*; D004717:Endometrium / Q000166:cytology*; D005260:Female; D051417:Focal Adhesion Kinase 1; D051416:Focal Adhesion Protein-Tyrosine Kinases; D006801:Humans; D051419:Paxillin; D010750:Phosphoproteins / Q000032:analysis / Q000378:metabolism; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000032:analysis / Q000378:metabolism; D017154:Stromal Cells / Q000378:metabolism* / Q000648:ultrastructure; D013347:Subcellular Fractions / Q000737:chemistry*; D019061:src-Family Kinases
chemical_list: D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; C496061:PXN protein, human; D051419:Paxillin; D010750:Phosphoproteins; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases; D000081247:CSK Tyrosine-Protein Kinase; D051417:Focal Adhesion Kinase 1; D051416:Focal Adhesion Protein-Tyrosine Kinases; C496050:PTK2 protein, human; D019061:src-Family Kinases; C000631346:CSK protein, human