Abstract
The action of endothelin-1 (ET-1) on protein phosphorylation was studied in rat cerebral cortex. The peptide caused an increase in 32P incorporation into a 87 kDa protein, identified as myristoilated alanine-rich protein kinase C substrate (MARCKS). This effect was dose- and time-dependent, and was mimicked by ET-3, sarafotoxin 6c and 12-O-tetradecanoylphorbol-13-acetate (TPA). However, it disappeared in the presence of Ro-31-8220, a protein kinase C (PKC) inhibitor. These findings indicate that ET-1 may have a functional role in protein phosphorylation processes in brain.
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.
