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Expression of mRNA for Cell Adhesion Molecules in the Bovine Corpus Luteum During the Estrous Cycle and PGF2α-Induced Luteolysis OAK
SHIRASUNA, Koumei; WATANABE, Sho; NAGAI, Kaya; SASAHARA, Kiemi; SHIMIZU, Takashi; RICKEN, Albert M.; SPANEL-BOROWSKI, Katharina; MIYAMOTO, Akio; 白砂, 孔明; 清水, 隆; 宮本, 明夫.
Cell-to-cell interaction via cell contact-dependent pathway is essentially important for maintenance and regulation of corpus luteum (CL) integrity and its physiological actions. The objective of the present study was to evaluate the mRNA expression of the cell adhesion molecules (CAMs) that are constituent factors of gap junctions [connexin (Cx) 43] and adherence junctions (VE-, E-, N-cadherin) in two types of endothelial cells from the mid CL and in CL tissue during the estrous cycle and PGF2α-induced luteolysis in the cow. Specific mRNA expression for Cx43 and N-cadherin was detected in cytokeratin-positive (CK+) and cytokeratin-negative (CK-) luteal endothelial cells (EC) and fully luteinized granulosa cells (LGC). E-cadherin mRNA was expressed in...
Palavras-chave: Cadherin; Connexin; Corpus luteum; Cow; Luteolysis.
Ano: 2007 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/2988
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Identification of a protein kinase activity that phosphorylates connexin43 in a pH-dependent manner BJMBR
Yahuaca,P.; Ek-Vitorin,J.F.; Rush,P.; Delmar,M.; Taffet,S.M..
The carboxyl-terminal (CT) domain of connexin43 (Cx43) has been implicated in both hormonal and pH-dependent gating of the gap junction channel. An in vitro assay was utilized to determine whether the acidification of cell extracts results in the activation of a protein kinase that can phosphorylate the CT domain. A glutathione S-transferase (GST)-fusion protein was bound to Sephadex beads and used as a target for protein kinase phosphorylation. A protein extract produced from sheep heart was allowed to bind to the fusion protein-coated beads. The bound proteins were washed and then incubated with 32P-ATP. Phosphorylation was assessed after the proteins were resolved by SDS-PAGE. Incubation at pH 7.5 resulted in a minimal amount of phosphorylation while...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Connexin; Phosphorylation; Phosphotransferases; Protein kinase.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000400005
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