Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/9355
Title: Lysosomal Cathepsin A plays a significant role in the processing of endogenous bioactive peptides
Authors: Timur, Zehra Kevser
Akyıldız Demir, Seçil
Seyrantepe, Volkan
Keywords: Cathepsin A
Bioactive peptid
Mouse
Lysosomes
Regulation
Publisher: Frontiers Media S.A.
Abstract: 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 CTSA(S190A). We investigated the level of bradykinin, substances P, oxytocin, angiotensin I and endothelin-I in the kidney, liver, lung, brain and serum from CTSA(S190A) mouse model at 3- and 6-months of age. Our results suggest CTSA selectively contributes to processing of bioactive peptides in different tissues from CTSA(S190A) mice compared to age matched WT mice.
URI: https://doi.org/10.3389/fmolb.2016.00068
https://hdl.handle.net/11147/9355
ISSN: 2296-889X
Appears in Collections:Molecular Biology and Genetics / Moleküler Biyoloji ve Genetik
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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