Lysosomal Cathepsin A Plays a Significant Role in the Processing of Endogenous Bioactive Peptides.
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 ofCTSAS190A. We investigated the level of bradykinin, substances P, oxytocin, angiotensin I and endothelin-I in the kidney, liver, lung, brain and serum fromCTSAS190Amouse model at 3- and 6-months of age. Our results suggest CTSA selectively contributes to processing of bioactive peptides in different tissues fromCTSAS190Amice compared to age matched WT mice.
Izmir Institute of Technology, Molecular Biology and Genetics Izmir, Turkey.
Zehra Kevser
ZK
Timur
Izmir Institute of Technology, Molecular Biology and Genetics Izmir, Turkey.
Secil
S
Akyildiz Demir
Izmir Institute of Technology, Molecular Biology and Genetics Izmir, Turkey.
Volkan
V
Seyrantepe
Cathepsin A; bioactive peptid; lysosome; mouse; regulation