Calmodulin of the tropical sea cucumber: Gene structure, inducible expression and contribution to nitric oxide production and pathogen clearance during immune response. Issue 2 (August 2015)
- Record Type:
- Journal Article
- Title:
- Calmodulin of the tropical sea cucumber: Gene structure, inducible expression and contribution to nitric oxide production and pathogen clearance during immune response. Issue 2 (August 2015)
- Main Title:
- Calmodulin of the tropical sea cucumber: Gene structure, inducible expression and contribution to nitric oxide production and pathogen clearance during immune response
- Authors:
- Chen, Ting
Ren, Chunhua
Li, Wuhu
Jiang, Xiao
Xia, Jianjun
Wong, Nai-Kei
Hu, Chaoqun - Abstract:
- <abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">Calmodulin (CaM) is an essential second messenger protein that transduces calcium signals by binding calcium ions (Ca<sup>2+</sup>) and modulating its interactions with various target proteins. In contrast to vertebrates, where CaM is well established as a cofactor for Ca<sup>2+</sup>-dependent physiological and cellular functions including host defense, there is a paucity of understanding on CaM in invertebrates (such as echinoderms) in response to immune challenge or microbial infections. In this study, we obtained and described the gene sequence of <italic>CaM</italic> from the tropical sea cucumber <italic>Stichopus monotuberculatus</italic>, a promising yet poorly characterized aquacultural species. mRNA expression of <italic>StmCaM</italic> could be detected in the intestine and coelomic fluid after <italic>Vibrio alginolyticus</italic> injection. Transcriptional and translational expression of <italic>Stm</italic>CaM was inducible in nature, as evidenced by the expression patterns in primary coelomocytes following <italic>Vibrio</italic> challenge. This response could be mimicked by the <italic>Vibrio</italic> cells membrane components or lipopolysaccharides (LPS), and blocked by co-treatment of the LPS-neutralizing agent polymyxin B (PMB). Furthermore, inhibition of CaM activity by incubation with its inhibitor trifluoroperazine<abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">Calmodulin (CaM) is an essential second messenger protein that transduces calcium signals by binding calcium ions (Ca<sup>2+</sup>) and modulating its interactions with various target proteins. In contrast to vertebrates, where CaM is well established as a cofactor for Ca<sup>2+</sup>-dependent physiological and cellular functions including host defense, there is a paucity of understanding on CaM in invertebrates (such as echinoderms) in response to immune challenge or microbial infections. In this study, we obtained and described the gene sequence of <italic>CaM</italic> from the tropical sea cucumber <italic>Stichopus monotuberculatus</italic>, a promising yet poorly characterized aquacultural species. mRNA expression of <italic>StmCaM</italic> could be detected in the intestine and coelomic fluid after <italic>Vibrio alginolyticus</italic> injection. Transcriptional and translational expression of <italic>Stm</italic>CaM was inducible in nature, as evidenced by the expression patterns in primary coelomocytes following <italic>Vibrio</italic> challenge. This response could be mimicked by the <italic>Vibrio</italic> cells membrane components or lipopolysaccharides (LPS), and blocked by co-treatment of the LPS-neutralizing agent polymyxin B (PMB). Furthermore, inhibition of CaM activity by incubation with its inhibitor trifluoroperazine dihydrochloride (TFP) blunted the production of <italic>Vibrio</italic>-induced nitric oxide (NO) and augmented the survival of invading <italic>Vibrio</italic> in coelomocytes. Collectively, our study here supplied the first evidence for echinoderm CaM participation in innate immunity, and provided a functional link between CaM expression and antibacterial NO production in sea cucumber.</p> </sec> </abstract> … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 45:Issue 2(2015:Aug.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 45:Issue 2(2015:Aug.)
- Issue Display:
- Volume 45, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 45
- Issue:
- 2
- Issue Sort Value:
- 2015-0045-0002-0000
- Page Start:
- 231
- Page End:
- 238
- Publication Date:
- 2015-08
- Subjects:
- Fishes -- Immunology -- Periodicals
Shellfish -- Immunology -- Periodicals
Poissons -- Immunologie -- Périodiques
Crustacés -- Immunologie -- Périodiques
571.9617 - Journal URLs:
- http://www.sciencedirect.com/science/journal/10504648 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1050-4648;screen=info;ECOIP ↗
http://www.sciencedirect.com/science/journal/latest/10504648 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fsi.2015.04.013 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3643.xml