A homolog of Kunitz-type serine protease inhibitor from rock bream, Oplegnathus fasciatus: Molecular insights and transcriptional modulation in response to microbial and PAMP stimulation, and tissue injury. Issue 2 (October 2015)
- Record Type:
- Journal Article
- Title:
- A homolog of Kunitz-type serine protease inhibitor from rock bream, Oplegnathus fasciatus: Molecular insights and transcriptional modulation in response to microbial and PAMP stimulation, and tissue injury. Issue 2 (October 2015)
- Main Title:
- A homolog of Kunitz-type serine protease inhibitor from rock bream, Oplegnathus fasciatus: Molecular insights and transcriptional modulation in response to microbial and PAMP stimulation, and tissue injury
- Authors:
- Bathige, S.D.N.K.
Umasuthan, Navaneethaiyer
Godahewa, G.I.
Jayasinghe, J.D.H.E.
Whang, Ilson
Noh, Jae Koo
Lee, Jehee - Abstract:
- <abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">Serine proteases and their inhibitors play vital roles in diverse biological processes. In this study, we identified and characterized cDNA coding for a Kunitz-type serine protease inhibitor (SPI), which we designated as RbKSPI, in a commercially important species, rock bream. The full-length cDNA sequence of <italic>RbKSPI</italic> consisted of 2452 bp with an open reading frame (ORF) of 1521 bp encoding a polypeptide of 507 amino acid (aa) residues. In the RbKSPI protein, MANEC, PKD, LDLa, and two Kunitz domains responsible for various functions were identified as characteristic features. Homology analysis revealed that RbKSPI shared the highest identity with the Kunitz homolog in <italic>Takifugu rubripes</italic> (77.6%). Phylogenetic analysis indicated that RbKSPI clusters with other teleostean KSPIs. In tissue-specific expression analysis, <italic>RbKSPI</italic> transcripts were detected in all the tested tissues, with the highest expression in gill tissue, followed by kidney and intestine. The mRNA expression of <italic>RbKSPI</italic> significantly increased in blood cells upon stimulation with two strains of bacteria (<italic>Edwardsiella tarda</italic> and <italic>Streptococcus iniae</italic>) and two pathogen-associated molecular patterns (PAMPs; LPS and poly I:C). Meanwhile, down-regulated expression of <italic>RbKSPI</italic> was<abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">Serine proteases and their inhibitors play vital roles in diverse biological processes. In this study, we identified and characterized cDNA coding for a Kunitz-type serine protease inhibitor (SPI), which we designated as RbKSPI, in a commercially important species, rock bream. The full-length cDNA sequence of <italic>RbKSPI</italic> consisted of 2452 bp with an open reading frame (ORF) of 1521 bp encoding a polypeptide of 507 amino acid (aa) residues. In the RbKSPI protein, MANEC, PKD, LDLa, and two Kunitz domains responsible for various functions were identified as characteristic features. Homology analysis revealed that RbKSPI shared the highest identity with the Kunitz homolog in <italic>Takifugu rubripes</italic> (77.6%). Phylogenetic analysis indicated that RbKSPI clusters with other teleostean KSPIs. In tissue-specific expression analysis, <italic>RbKSPI</italic> transcripts were detected in all the tested tissues, with the highest expression in gill tissue, followed by kidney and intestine. The mRNA expression of <italic>RbKSPI</italic> significantly increased in blood cells upon stimulation with two strains of bacteria (<italic>Edwardsiella tarda</italic> and <italic>Streptococcus iniae</italic>) and two pathogen-associated molecular patterns (PAMPs; LPS and poly I:C). Meanwhile, down-regulated expression of <italic>RbKSPI</italic> was observed in response to tissue injury. Collectively, these results suggest that the <italic>RbKSPI</italic> may be involved in essential immune defense against microbial pathogens and in the wound-healing process.</p> </sec> </abstract> … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 46:Issue 2(2015:Oct.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 46:Issue 2(2015:Oct.)
- Issue Display:
- Volume 46, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 46
- Issue:
- 2
- Issue Sort Value:
- 2015-0046-0002-0000
- Page Start:
- 285
- Page End:
- 291
- Publication Date:
- 2015-10
- 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.2015.07.004 ↗
- 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
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- 3904.xml