| Autor: |
Timur ZK; Izmir Institute of Technology, Molecular Biology and Genetics Izmir, Turkey., Akyildiz Demir S; Izmir Institute of Technology, Molecular Biology and Genetics Izmir, Turkey., Seyrantepe V; Izmir Institute of Technology, Molecular Biology and Genetics Izmir, Turkey. |
| Jazyk: |
angličtina |
| Zdroj: |
Frontiers in molecular biosciences [Front Mol Biosci] 2016 Oct 25; Vol. 3, pp. 68. Date of Electronic Publication: 2016 Oct 25 (Print Publication: 2016). |
| DOI: |
10.3389/fmolb.2016.00068 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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