Abstract

Here we present the extended cleavage specificity of catfish granzyme-like I, previously identified in fish NK-like cells. This protease has been characterised using substrate phage display and further validated by using a panel of recombinant substrates. A strict preference for Met in the P1 (cleavage) position, indicating metase specificity was observed. A screening of potential in vivo substrates was performed based on the derived P5-P3' consensus: Arg-Val-Thr-Gly-Met(down arrow)Ser-Leu-Val. Channel catfish caspase 6 was one very interesting potential target identified. This site was present in an adjacent position to the classic caspase activation site (Asp179 in human caspase 6). Cleavage of this site (hence potential activation) by the catfish granzyme-like I could reveal a novel mechanism of caspase 6 activation. This poses an interesting idea that the role of granzyme-like proteases in the activation of caspase dependent apoptosis mechanisms has been conserved for over 400 million years. (C) 2016 Elsevier Ltd. All rights reserved.

Keywords

Fish; Serine protease; Cleavage specificity; Metase; NK cell; Caspase; Evolution

Published in

Developmental and Comparative Immunology
2016, Volume: 63, pages: 84-95
Publisher: ELSEVIER SCI LTD

UKÄ Subject classification

Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.1016/j.dci.2016.05.013

Permanent link to this page (URI)

https://res.slu.se/id/publ/110816