Abstract
A novel synthetic peptide AIP (autocamtide-2-related inhibitory peptide), a nonphosphorylatable analog of autocamtide-2, was found to be a highly specific and potent inhibitor of calmodulin-dependent protein kinase II (CaM-kinase II). It was 50 and 500 times more potent than CaMK-(281-302A1a286) and KN-93, respectively, under the assay conditions used. The inhibition was unaffected by the presence or absence of Ca2+/calmodulin, and it was competitive with autocamtide-2 and noncompetitive with syntide-2. AIP (1 μM) completely inhibited CaM-kinase II activity, but did not affect cyclic AMP-dependent protein kinase, protein kinase C, calmodulin-dependent protein kinase IV, and unidentified protein kinases occurring in a rat brain extract. These results indicate that AIP is a useful tool for studying the physiological roles of CaM-kinase II.
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 callMore From: Biochemical and Biophysical Research Communications
Disclaimer: 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.
