Spatiotemporal Interactions of Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) Protein with the Actin Cytoskeleton and Exocytosis of Oxytocin upon Prostaglandin F2α Stimulation of Bovine Luteal Cells1

Autor:	N. Saito, Fred Stormshak, Ugur Salli
Rok vydání:	2003
Předmět:	Prostaglandin Cell Biology General Medicine Transfection Biology Actin cytoskeleton Exocytosis Cell biology Green fluorescent protein chemistry.chemical_compound Reproductive Medicine Biochemistry chemistry MARCKS Protein kinase A Cytoskeleton
Zdroj:	Biology of Reproduction. 69:2053-2058
ISSN:	1529-7268 0006-3363
Popis:	In the bovine corpus luteum (CL) phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein in response to prostaglandin F2α (PGF2α) is correlated with the secretion of oxytocin. The present study was conducted to 1) examine the intracellular translocation characteristics of wild-type and mutant forms of a green fluorescent protein (GFP)-conjugated MARCKS (MARCKS-GFP) after PGF2α treatment and 2) evaluate PGF2α-induced temporal changes in MARCKS-GFP and actin cortex associated with exocytosis of oxytocin. In experiment 1, cells of the bovine CL were cultured on coverslips overnight. Then, wild-type and mutant MARCKS-GFP constructs were transfected separately into cells and expression was detected through fluorescence microscopy. Forty-eight hours after transfection, cells were treated with vehicle, PGF2α (56 nM), or a phorbol ester (12-O-tetradecanoylphorbol-13-acetate [TPA], 1 μM). Treatment of cells expressing wild-type MARCKS-GFP with PGF2α and TPA resulted in translocat...
Databáze:	OpenAIRE
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