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Umasuthan, Navaneethaiyer,Whang, Ilson,Saranya Revathy, Kasthuri,Oh, Myung-Joo,Jung, Sung-Ju,Choi, Cheol Young,Lee, Jeong-Ho,Noh, Jae Koo,Lee, Jehee Elsevier 2012 FISH AND SHELLFISH IMMUNOLOGY Vol.32 No.5
<P><B>Abstract</B></P><P>Angiotensinogen (AGT) is the precursor of the renin-angiotensin system and contributes to osmoregulation, acute-phase and immune responses. A full-length cDNA of the <I>AGT</I> (2004 bp with a 1389 bp coding region) was isolated from rock bream (Rb), <I>Oplegnathus fasciatus</I>. The encoded polypeptide of 463 amino acids had a predicted molecular mass of 51.6 kDa. <I>RbAGT</I> possessed a deduced signal peptide of 22 residues upstream of a putative angiotensin I sequence (<SUP>23</SUP>NRVYVHPFHL<SUP>32</SUP>). <I>RbAGT</I> possessed a specific domain profile and a signature motif which are characteristics of the serpin family. Sequence homology and phylogenetic analysis indicated that <I>RbAGT</I> was evolutionarily closest to AGT of <I>Rhabdosargus sarba</I>. The mRNA expression profile of <I>RbAGT</I> was determined by quantitative RT-PCR and it demonstrated a constitutive and tissue-specific expression with the highest transcript level in the liver. Significantly up-regulated <I>RbAGT</I> expression was elicited by systemic injection of a lipopolysaccharide, rock bream iridovirus (RBIV) and bacteria (<I>Edwardsiella tarda</I> and <I>Streptococcus iniae</I>), revealing its pathogen inducibility. <I>RbAGT</I> manifested a down-regulated response to systemic injury, contemporaneously with two other serpins, protease nexin-1 (<I>PN-</I>1), and heparin cofactor II (<I>HCII</I>). In addition, a synchronized expression pattern was elicited by <I>RbAGT</I> and <I>RbTNF-α</I> in response to injury, suggesting that TNF-α might be a potential modulator of <I>AGT</I> transcription.</P> <P><B>Graphical abstract</B></P><P><ce:figure id='dfig1'></ce:figure></P><P><B>Highlights</B></P><P>► Molecular characterization of angiotensinogen from rock bream (<I>RbAGT</I>). ► Tissue-specific transcriptional profile of <I>RbAGT.</I> ► Response of hepatic <I>RbAGT</I> against LPS, bacteria and iridovirus. ► Temporal expression of hematic <I>RbAGT</I> upon injury. ► Expressional relationship between <I>RbAGT</I>, <I>HCII</I>, <I>PN-1</I> and <I>TNF-α</I>.</P>
Oh, Chulhong,Nikapitiya, Chamilani,Lee, Youngdeuk,Whang, Ilson,Kang, Do-Hyung,Heo, Soo-Jin,Choi, Young-Ung,Lee, Jehee Sociedade Brasileira de Microbiologia 2010 Brazilian journal of microbiology Vol.41 No.4
<P>An agar-degrading <I>Pseudoalteromonas</I> sp. AG52 bacterial strain was identified from the red seaweed <I>Gelidium amansii</I> collected from Jeju Island, Korea. A β-agarase gene which has 96.8% nucleotide identity to <I>Aeromonas</I> β-agarase was cloned from this strain, and was designated as a<I>ga</I>A. The coding region is 870 bp, encoding 290 amino acids and possesses characteristic features of the glycoside hydrolase family (GHF)-16. The predicted molecular mass of the mature protein was 32 kDa. The recombinant β-agarase (rAgaA) was overexpressed in <I>Escherichia coli</I> and purified as a fusion protein. The optimal temperature and pH for activity were 55 °C and 5.5, respectively. The enzyme had a specific activity of 105.1 and 79.5 unit/mg toward agar and agarose, respectively. The pattern of agar hydrolysis demonstrated that the enzyme is an endo-type β-agarase, producing neoagarohexaose and neoagarotetraose as the final main products.</P><P>Since, <I>Pseudoalteromonas</I> sp. AG52 encodes an a<I>ga</I>A gene, which has greater identity to <I>Aeromonas</I> β-agarase, the enzyme could be considered as novel, with its unique bio chemical characteristics. Altogether, the purified rAgaA has potential for use in industrial applications such as development of cosmetics and pharmaceuticals.</P>