Molecular identification and expression analysis of cathepsins O and S from rock bream, Oplegnathus fasciatus

Kim, Juwon; Jeong, Ji-Min; Park, Hyoung-Jun; Kim, Eun-Gyeong; Kim, Hana; Chae, Young-Sun; Kim, Do-Hyung; Park, Chan-Il

doi:10.1016/j.fsi.2011.07.007

Cited by 18 publications

(5 citation statements)

References 37 publications

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“…In mammals, cathepsin S was found predominantly expressed in professional antigen presenting cells, i.e., dendritic cells and B cells [29]. In teleost fish, cathepsin S mRNA was detected in multiple tissues [14,17], which is consistent with our observations. Human cathepsin S was reported to contribute to microvessel development [30].…”

Section: Expression Of Socats Under Different Conditionssupporting

confidence: 91%

“…In mammals, cathepsin S is regarded as an important protease in host immunity, especially in the processes of antigen presenting [1,29]. In teleost fish, the expression of cathepsin S homologues were reported to be positively responsive to bacterial or LPS stimulations in several species, such as Lutjanus argentimaculatus [14], O. fasciatus [17], and P. olivaceus [16]. In the present work, we discovered that the mRNA levels of SoCatS in multiple tissues were significantly induced by experimental challenge with the pathogenic bacterium E. tarda in time dependent manners, which points to an implication of SoCatS in immune response of red drum to bacterial infection.…”

Section: Expression Of Socats Under Different Conditionsmentioning

confidence: 99%

“…10.037 0141-8130/© 2015 Elsevier B.V. All rights reserved. [15], Paralichthys olivaceus [16] and Oplegnathus fasciatus [17]. Several studies have pointed to possible involvements of cathepsin S homologues in piscine immune response to bacterial infection [14,16,17].…”

Section: Introductionmentioning

confidence: 99%

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Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity

Sun

Chi

2016

International Journal of Biological Macromolecules

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Section: Expression Of Socats Under Different Conditionssupporting

confidence: 91%

Section: Expression Of Socats Under Different Conditionsmentioning

confidence: 99%

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Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity

Sun

Chi

2016

International Journal of Biological Macromolecules

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“…The heat shock proteins (HSPs) are some of the proteins that show increased abundance during heat stress and other stress conditions. In addition to acting as molecular chaperones, the HSPs play important role in immunomodulation, apoptosis, and various aspects of the inflammatory process [8]. In an earlier investigation, to study the response of different HSPs to high temperature, we studied the expression profiles of a battery of hsp genes in the liver of Channa striatus exposed to high temperature (36°C for various time periods) and compared with that of fish collected from aquaculture ponds (25°C; control) and a hot spring runoff (36-38°C) (described later in discussion) [9,10].…”

Section: Introductionmentioning

confidence: 99%

Proteomic changes in the liver ofChanna striatusin response to high temperature stress

et al. 2016

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The present study was undertaken to investigate the proteomic changes in the liver of murrel Channa striatus exposed to high temperature stress. Fishes were exposed to 36°C for 4 days and liver proteome changes were analyzed using gel- based proteomics, i.e. 2DE, MALDI-TOF/TOF-MS, and validation by transcript analysis. The study showed, besides others, increased abundance of two sets of proteins, the antioxidative enzymes superoxide dismutase (SOD), ferritin, cellular retinol binding protein (CRBP), glutathione-S-transferase (GST), and the chaperones HSP60 and protein disulfide isomerase; this was validated by transcript analysis. The proteome data are available via ProteomeXchange with identifier PXD002608. Further, gene expression analysis was also carried out in the fishes exposed to thermal stress for longer durations (30 days experimental exposure in laboratory and for 30 days beyond, taking Channa collected from a hot spring runoff at 36-38°C); sod, gst, crbp, and hsp60 were found to continue to remain upregulated at eight-, 2.5-, 2.4-, and 2.45-fold, respectively, in the hot spring runoff fish. Pathway analysis showed that the upregulations of the antioxidant enzymes as well as molecular chaperones are induced by the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2). Thus, while short-term heat stress tolerance involves the antioxidative enzymes SOD, ferritin, CRBP, GST, and chaperones HSP60 and protein disulfide isomerase, adaptation under chronic heat stress is associated with SOD, CRBP, GST, and HSP60.

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“…The specific activity of CsCath L in spleen after challenged with fungus and bacterium showed its involvement in the immune process of striped murrel. As stated by Press & Evensen (1999), Dong et al (2007) and Kim et al (2011) the results of CsCath L enzyme activity analyses in spleen after fungal and bacterial infection indicate that the haematopoietic and lymphoid organs are closely related to the immune response in fish. Hence it is possible to suggest that cathepsin L may play multifunctional roles in murrels.…”

Section: Discussionmentioning

confidence: 75%

A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity

et al. 2014

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Cathepsin L, a lysosomal endopeptidase, is a member of the peptidase C1 family (papain-like family) of cysteine proteinases that cleave peptide bonds of lysosomal proteins. In this study, we report a cathepsin L sequence identified from the constructed cDNA library of striped murrel Channa striatus (designated as CsCath L) using genome sequencing FLX TM technology. The full-length CsCath L contains three eukaryotic thiol protease domains at positions 134-145, 278-288 and 299-318. Phylogenetic analysis revealed that the CsCath L was clustered together with other cathepsin L from teleosts. The three-dimensional structure of CsCath L modelled by the I-Tasser program was compared with structures deposited in the Protein Data Bank to find out the structural similarity of CsCath L with experimentally identified structures. The results showed that the CsCath L exhibits maximum structural identity with pro-cathepsin L from human. The RNA fold structure of CsCath L was predicted along with its minimum free energy (-471.93 kcal/mol). The highest CsCath L gene expression was observed in liver, which was also significantly higher (P < 0.05) than that detected in other tissues taken for analysis. In order to investigate the mRNA transcription profile of CsCath L during infection, C. striatus were injected with fungus (Aphanomyces invadans) and bacteria (Aeromonas hydrophila) and its expression was up-regulated in liver at various time points. Similar to gene expression studies, the highest CsCath L enzyme activity was also observed in liver and its activity was up-regulated by fungal and bacterial infections.

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Molecular identification and expression analysis of cathepsins O and S from rock bream, Oplegnathus fasciatus

Cited by 18 publications

References 37 publications

Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity

Cathepsin S of Sciaenops ocellatus: Identification, transcriptional expression and enzymatic activity

Proteomic changes in the liver ofChanna striatusin response to high temperature stress

A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity

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