Abstract
The presence of a kinase with the activation characteristics of protein kinase C (PKC) was demonstrated in supernatants of homogenates of the cestode Hymenolepis diminuta. Maximal phosphorylation activity was observed in diluted supernatants in the presence of Ca 2+, phosphatidylserine and β-phorbol-12-myristate-13-acetate (PMA), whereas α-PMA was inactive. PKC-like activation in tissue slice extracts was abrogated by prior treatment of tissue slices with staurosporine. Specific activity of H. diminuta PKC was low compared with that of mammalian brain extracts but similar to that of other invertebrates. The present study demonstrates the presence of a kinase activity in H. diminuta that possesses activation and inhibition characteristics similar to the α-, β-, and γ-isomers of mammalian PKC.
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.
