Work

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

Year: 2016

Type: article

Abstract: 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.

Source: Frontiers in Molecular Biosciences

DOI: 10.3389/fmolb.2016.00068

Authors: Zehra Kevser Timur, Secil Akyildiz Demir, Volkan Seyrantepe

Institution: Izmir Institute of Technology

Language: English

Topic: Coagulation, Bradykinin, Polyphosphates, and Angioedema

Subfield: Hematology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: gold

Estimated APC paid: $3,801