IndraLab

"Recently Wallingford and colleagues have identified an enzyme, prolylcarboxypeptidase (PRCP), that inactivates α-MSH by removing the C-terminal valine residue ( xref )."

"The serine protease prolylcarboxypeptidase (PRCP) inactivates α-MSH by catalyzing cleavage at the carboxyl terminal Pro-Val bond, producing inactive α-MSH 1–12 . suggests PRCP could have an appetite stimulating (orexigenic) effect [ xref , xref ]."

"PRCP inactivates α-MSH by the removal of the N-terminal valine residue."

"Obesity is known to cause inflammation and insulin resistance in the vasculature and non-vascular tissues involved in glucose metabolism. xref Evidence suggests that hyperglycemia may contribute to defective NO-dependent vasodilation in diabetes. xref The inducible NO synthase (iNOS) expression is elevated in adipose tissue of obese people compared to those of lean people xref and is a mediator of inflammation and a key enzyme in insulin resistance. xref The colocalization of α-MSH 1–13 receptors (MC4R) with iNOS has been reported, suggesting a role for α-MSH 1–13 in obese people. xref The inactivation of α-MSH 1–13 by PRCP provides a positive feedback loop for postprandial enhancement of food intake and inflammation by inhibiting α-MSH 1–13 function, as shown in xref . xref Since PRCP regulates the anorectic action of α-MSH 1–13 , this study highlights the presence of a newly recognized interaction between inflammation, obesity, and the expression and activity of PRCP ( xref ). xref In view of the above studies, we consider that PRCP may be a key player in the obesity-associated metabolic complications, inflammatory response, and the host defense mechanism."