Phosphoproteomics of mouse cardiomyocytes reveals signalling pathways triggered by a vasodilator cryptide

Animal venoms are natural sources of bioactive molecules such as cryptides that consist in biological active peptides released after proteolytic cleavage of a peptide or protein precursor. The KPP is a cryptided derived from the c-terminal of an hypotensin (TsHpI) a peptide isolated from the venom of Tityus serrulatus scorpion. Previous studies of our group in rodent model demonstrated that KPP maintained the cardioprotective properties of its precursor. Nonetheless, the molecular machinery involved in the cellular response is poorly described to date. Thus, in order to characterize the signalling pathways triggered by KPP we incubate mouse cardiomyocytes with KPP during 5 or 30 min and explore the cell proteome and phosphoproteome by dimethyl labelling quantitation.