Calmodulin interacts with ACE2 and its inhibition stimulates the shedding of the ACE2 ectodomain, suggesting a regulatory role for calmodulin in ACE2 surface expression.
Preclinical calmodulin-ACE2 data require validation before any clinical translation; leaves open effects on human cardiovascular or infectious outcomes.
Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin-angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-alpha converting enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors.
No takes yet. Share an insight, caveat, or question.
Lambert et al. (2007) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: