Lysosomal Cathepsin A Plays Significant Role In The Processing Of Endogenous Bioactive Peptides

• Main Authors: Zehra Timur, Secil Akyildiz, Volkan Seyrantepe
• Format: Article
• Language: English
• Published: Frontiers Media S.A. 2016-10-01
• Series: Frontiers in Molecular Biosciences
• Subjects: Cathepsin A; Mouse; regulation; Lysosome; bioactive peptid
• Online Access: http://journal.frontiersin.org/Journal/10.3389/fmolb.2016.00068/full

Lysosomal serine carboxypeptidase Cathepsin A (CTSA) is a multifunctional enzyme with distinct protective and catalytic function. CTSA that is present in the lysosomal multienzyme complex facilitates correct lysosomal routing, stability and activation of betagalactosidase and alpha-neuraminidase. In addition, CTSA plays a role in the inactivation of bioactive peptides including bradykinin, substances P, oxytocin, angiotensin I and endothelin-I by cleavage of one or two amino acid(s) from the C-terminal ends. In this study, we aimed to elucidate the regulatory role of CTSA on bioactive peptides in a knock-in mouse model of CTSAS190A. We evaluated the levels of bradykinin, substances P, oxytocin, angiotensin I and endothelin-I in the kidney, liver, lung, brain and serum of the CTSAS190A mouse model at three- and six-months of age. Our results suggest that CTSA selectively contributes to the processing of bioactive peptides in different tissues of CTSAS190A mice compared to those of age-matched wild-type mice.