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dc.contributor.authorTimur, Zehra Keyser
dc.contributor.authorDemir, Secil Akyildiz
dc.contributor.authorSeyrantepe, Volkan
dc.descriptionWOS: 000455328600068en_US
dc.descriptionPubMed: 27826550en_US
dc.description.abstractLysosomal 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.en_US
dc.publisherFrontiers Media Saen_US
dc.subjectCathepsin Aen_US
dc.subjectbioactive peptiden_US
dc.titleLysosomal Cathepsin A Plays a Significant Role in the Processing of Endogenous Bioactive Peptidesen_US
dc.relation.journalFrontiers In Molecular Biosciencesen_US
dc.contributor.departmentIzmir Institute of Technologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.cont.department-temp[Timur, Zehra Keyser; Demir, Secil Akyildiz; Seyrantepe, Volkan] Izmir Inst Technol, Mol Biol & Genet, Izmir, Turkeyen_US

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