Abstract
Protein kinase C (PKC) activity in the muscular layer of stem villi vessels from the human term placenta was studied. Resting state PKC activity was distributed evenly between the cytosol and the particulate fractions. Upon stimulation by three different activators, phorbol 12-myristate 13-acetate, fluoride and endothelin-1, a translocation of PKC activity from the cytosolic to the particulate fraction was observed. The expression and distribution of PKC isoforms were then examined by Western blot analysis using specific antibodies to PKC isoforms. At least four PKC isoforms, PKCα, PKCβ 1, PKCβ 2, PKCζ, and trace amounts of PKCϵ were detected in both fractions. Their relative responses to the different agonists were examined by quantifying their subcellular redistribution. No significant differential activation of the four mainly expressed PKC isoforms were observed in response to stimulation with any of the stimuli. Moreover, our results show that endothelin-1 induced translocation/activation of PKC in this vascular smooth muscle.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
