AUTHOR=Timur Zehra Kevser , Akyildiz Demir Secil , Seyrantepe Volkan 

TITLE=Lysosomal Cathepsin A Plays a Significant Role in the Processing of Endogenous Bioactive Peptides

JOURNAL=Frontiers in Molecular Biosciences

VOLUME=3

YEAR=2016

URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2016.00068

DOI=10.3389/fmolb.2016.00068

ISSN=2296-889X

ABSTRACT=<p>Lysosomal serine carboxypeptidase Cathepsin A (CTSA) is a multifunctional enzyme with distinct protective and catalytic function. CTSA present in the lysosomal multienzyme complex to facilitate the correct lysosomal routing, stability and activation of with beta–galactosidase and alpha-neuraminidase. Beside CTSA has role in inactivation of bioactive peptides including bradykinin, substances P, oxytocin, angiotensin I and endothelin-I by cleavage of 1 or 2 amino acid(s) from C-terminal ends. In this study, we aimed to elucidate the regulatory role of CTSA on bioactive peptides in knock-in mice model of <italic>CTSA</italic><sup><italic>S190A</italic></sup>. We investigated the level of bradykinin, substances P, oxytocin, angiotensin I and endothelin-I in the kidney, liver, lung, brain and serum from <italic>CTSA</italic><sup><italic>S190A</italic></sup> mouse model at 3- and 6-months of age. Our results suggest CTSA selectively contributes to processing of bioactive peptides in different tissues from <italic>CTSA</italic><sup><italic>S190A</italic></sup> mice compared to age matched WT mice.</p>