Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity
Cathepsin S is a member of cysteine cathepsins and belongs to the cathepsin L-like family. In mammals, it is known to participate in various physiological processes and host immune defense. In teleost fish, the function of cathepsin S is less investigated. In the present work, we characterized a cat...
Published in: | International Journal of Biological Macromolecules |
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/86650 2023-05-15T18:06:02+02:00 Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity Sun, Bo-guang Chi, Heng 2016 http://ir.qdio.ac.cn/handle/337002/86650 https://doi.org/10.1016/j.ijbiomac.2015.10.037 英语 eng INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES Sun, Bo-guang,Chi, Heng. Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2016,82(2016):76-82. http://ir.qdio.ac.cn/handle/337002/86650 doi:10.1016/j.ijbiomac.2015.10.037 Cathepsin s Sciaenops Ocellatus Teleost Fish Article 期刊论文 2016 ftchinacasciocas https://doi.org/10.1016/j.ijbiomac.2015.10.037 2022-06-27T05:37:26Z Cathepsin S is a member of cysteine cathepsins and belongs to the cathepsin L-like family. In mammals, it is known to participate in various physiological processes and host immune defense. In teleost fish, the function of cathepsin S is less investigated. In the present work, we characterized a cathepsin S homologue (SoCatS) from red drum (Sciaenops ocellatus), a commercially valuable fish in Chinese mariculture. Like all cathepsin S, SoCatS possesses a peptidase domain with four catalytically essential residues (Gln140, Cys146, His285, and Asn305) conserved in the cathepsin S of different organisms. SoCatS shares 60-90% overall sequence identities with known teleost cathepsin S. Phylogenetic profiling indicated that SoCatS is evolutionally close to the cathepsin S of other teleost fish, especially Miichthys miiuy, a member of Sciaenidae family like red drum. SoCatS expression was detected in various tissues and was enhanced by bacterial infection. Purified recombinant SoCatS exhibited apparent peptidase activity with maximum at 50 degrees C and pH 7.5. This activity depended on the catalytic residue Cys146 and was severely reduced by the cathepsin inhibitor E-64. Our results suggest that SoCatS functions as a cysteine protease which is probably involved in the antibacterial immunity of red drum. (C) 2015 Elsevier B.V. All rights reserved. Article in Journal/Newspaper Red drum Sciaenops ocellatus Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR International Journal of Biological Macromolecules 82 76 82 |
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Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
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ftchinacasciocas |
language |
English |
topic |
Cathepsin s Sciaenops Ocellatus Teleost Fish |
spellingShingle |
Cathepsin s Sciaenops Ocellatus Teleost Fish Sun, Bo-guang Chi, Heng Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity |
topic_facet |
Cathepsin s Sciaenops Ocellatus Teleost Fish |
description |
Cathepsin S is a member of cysteine cathepsins and belongs to the cathepsin L-like family. In mammals, it is known to participate in various physiological processes and host immune defense. In teleost fish, the function of cathepsin S is less investigated. In the present work, we characterized a cathepsin S homologue (SoCatS) from red drum (Sciaenops ocellatus), a commercially valuable fish in Chinese mariculture. Like all cathepsin S, SoCatS possesses a peptidase domain with four catalytically essential residues (Gln140, Cys146, His285, and Asn305) conserved in the cathepsin S of different organisms. SoCatS shares 60-90% overall sequence identities with known teleost cathepsin S. Phylogenetic profiling indicated that SoCatS is evolutionally close to the cathepsin S of other teleost fish, especially Miichthys miiuy, a member of Sciaenidae family like red drum. SoCatS expression was detected in various tissues and was enhanced by bacterial infection. Purified recombinant SoCatS exhibited apparent peptidase activity with maximum at 50 degrees C and pH 7.5. This activity depended on the catalytic residue Cys146 and was severely reduced by the cathepsin inhibitor E-64. Our results suggest that SoCatS functions as a cysteine protease which is probably involved in the antibacterial immunity of red drum. (C) 2015 Elsevier B.V. All rights reserved. |
format |
Article in Journal/Newspaper |
author |
Sun, Bo-guang Chi, Heng |
author_facet |
Sun, Bo-guang Chi, Heng |
author_sort |
Sun, Bo-guang |
title |
Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity |
title_short |
Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity |
title_full |
Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity |
title_fullStr |
Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity |
title_full_unstemmed |
Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity |
title_sort |
cathepsin s of sciaenops ocellatus: identification, transcriptional expression and enzymatic activity |
publishDate |
2016 |
url |
http://ir.qdio.ac.cn/handle/337002/86650 https://doi.org/10.1016/j.ijbiomac.2015.10.037 |
genre |
Red drum Sciaenops ocellatus |
genre_facet |
Red drum Sciaenops ocellatus |
op_relation |
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES Sun, Bo-guang,Chi, Heng. Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2016,82(2016):76-82. http://ir.qdio.ac.cn/handle/337002/86650 doi:10.1016/j.ijbiomac.2015.10.037 |
op_doi |
https://doi.org/10.1016/j.ijbiomac.2015.10.037 |
container_title |
International Journal of Biological Macromolecules |
container_volume |
82 |
container_start_page |
76 |
op_container_end_page |
82 |
_version_ |
1766177594331365376 |