Abstract
Isovalerylcarnitine (IVC) a product of the catabolism of L-leucine, is a potent activator of the Ca2+-dependent proteinase (calpain) of human neutrophils. At concentrations of Ca2+ in the low micromolar range, activation was 12 to 15-fold, and the activity exceeded that observed with millimolar concentrations of Ca2+ in the absence of the activator. Of the acylcarnitine derivatives tested, IVC was most active; D-isovalerylcarnitine was much less effective and palmitylcarnitine was ineffective. IVC did not increase the activity of calpain that was fully activated by an endogenous cytoskeleton-associated activator protein, but at low concentrations of the latter synergistic effects of the two activators were observed. Activation of neutrophil calpain by IVC is fully reversible. Inhibition by calpastatin was also reversed by IVC.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More 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.