Full-length cDNA cloning, molecular characterization and differential expression analysis of peroxiredoxin 6 from Ovis aries

Liu, Nannan; Liu, Zengshan; Lu, Shiying; Hu, Pan; Li, Yansong; Xia, Feng; Zhang, Shou-yin; Wang, Nan; Meng, Qing-Feng; Yang, Yongjie; Tang, Feng; Xu, Yun-Ming; Zhang, Wenhui; Guo, Xing; Chen, Xiaofeng; Zhou, Yu; Ren, Hong-Lin

doi:10.1016/j.vetimm.2015.01.006

Cited by 19 publications

(18 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Infection by both the live attenuated vaccines and by the virulent strain will cause similar immune responses, such as stimulation of Th1 responses [47]. As a consequence, it is impossible to distinguish between vaccinated animals and infected ones using the available serological tests at present [48]. …”

Section: Discussionmentioning

confidence: 99%

“…Total RNA was isolated as described previously [48]. Briefly, the anticoagulant-containing blood collected from O. aries was centrifuged at 800× g for 15 min at 4 °C to extract the buffy coats.…”

Section: Methodsmentioning

confidence: 99%

“…Protein expression of OaLypla1H in 200 mL fresh LB medium was induced by adding IPTG at a final concentration of 1.5 mM at 37 °C for 6.5 h. The induced pET-30a-LYPLA1-H cells were harvested and resuspended in binding buffer (20 mM sodium phosphate, 30 mM imidazole, 0.5 M NaCl, pH 7.4) [48]. The supernatant was collected by centrifugation at 12,000× g for 30 min at 4 °C after the resuspended cells were sonicated.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Full-Length cDNA Cloning, Molecular Characterization and Differential Expression Analysis of Lysophospholipase I from Ovis aries

Liu

et al. 2016

IJMS

Self Cite

View full text Add to dashboard Cite

Lysophospholipase I (LYPLA1) is an important protein with multiple functions. In this study, the full-length cDNA of the LYPLA1 gene from Ovis aries (OaLypla1) was cloned using primers and rapid amplification of cDNA ends (RACE) technology. The full-length OaLypla1 was 2457 bp with a 5′-untranslated region (UTR) of 24 bp, a 3′-UTR of 1740 bp with a poly (A) tail, and an open reading frame (ORF) of 693 bp encoding a protein of 230 amino acid residues with a predicted molecular weight of 24,625.78 Da. Phylogenetic analysis showed that the OaLypla1 protein shared a high amino acid identity with LYPLA1 of Bos taurus. The recombinant OaLypla1 protein was expressed and purified, and its phospholipase activity was identified. Monoclonal antibodies (mAb) against OaLypla1 that bound native OaLypla1 were generated. Real-time PCR analysis revealed that OaLypla1 was constitutively expressed in the liver, spleen, lung, kidney, and white blood cells of sheep, with the highest level in the kidney. Additionally, the mRNA levels of OaLypla1 in the buffy coats of sheep challenged with virulent or avirulent Brucella strains were down-regulated compared to untreated sheep. The results suggest that OaLypla1 may have an important physiological role in the host response to bacteria. The function of OaLypla1 in the host response to bacterial infection requires further study in the future.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Full-Length cDNA Cloning, Molecular Characterization and Differential Expression Analysis of Lysophospholipase I from Ovis aries

Liu

et al. 2016

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…The expression profiles of the OaPrdx6 in the white blood cells of sheep challenged with Brucella are changed. Compared with the Brucella vaccine strain S2, the virulent field strain of Brucella melitensis can up-regulate the mRNA transcription level of OaPrdx6 (7).…”

Section: Introductionmentioning

confidence: 98%

“…The full-length cDNA of the Prdx6 gene from Ovis aries (OaPrdx6) was identified and analysed for the first time by our group (7). The OaPrdx6 mRNA is composed of a 5′-untranslated region (UTR) of 93 bp, a 3′-UTR of 985 bp with a poly (A) tail, and an open reading frame (ORF) of 675 bp encoding a 25.1 kDa protein of 224 amino acid residues.…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterisation of peroxiredoxin 6 promoter from sheep (Ovis aries)

Liu

et al. 2016

Journal of Veterinary Research

Self Cite

View full text Add to dashboard Cite

Introduction: Peroxiredoxin 6 (Prdx6) is a bifunctional protein and a unique 1-Cys Prdx of the peroxiredoxin family. The expression and regulation of Prdx6 are implicated in numerous physiological and pathological processes. Material and Methods: Eight stepwise truncated DNA fragments obtained from the 5′-flank region of the Prdx6 gene were prepared and subcloned into the pSEAP2-Enhancer vectors. To investigate the transcriptional activity of the truncated DNA fragments, the recombinant plasmids were transfected into the COS-1 cells and the transcriptional activity was measured via assaying the expression of the reporter gene of the secreted alkaline phosphatase. Results: A 3.4 kb 5′-upstream flank region of the Prdx6 gene was cloned and sequenced. The region from -108 nt to -36 nt of the 5′-flanking region of the Prdx6 gene contained basal transcriptional activity. Conclusion: This result provides the basis for further studies on the gene regulation of the Prdx6-mediated biological processes and on screening for the transacting factors that interact with cis-acting elements of the Prdx6 gene promoter.

show abstract

Peroxiredoxin 6 from the Antarctic emerald rockcod: molecular characterization of its response to warming

et al. 2015

View full text Add to dashboard Cite

In the present study, we describe the purification and molecular characterization of two peroxiredoxins (Prdxs), referred to as Prdx6A and Prdx6B, from Trematomus bernacchii, a teleost widely distributed in many areas of Antarctica, that plays a pivotal role in the Antarctic food chain. The two putative amino acid sequences were compared with Prdx6 orthologs from other fish, highlighting a high percentage of identity and similarity with the respective variant, in particular for the residues that are essential for the characteristic peroxidase and phospholipase activities of these enzymes. Phylogenetic analyses suggest the appearance of the two prdx6 genes through a duplication event before the speciation that led to the differentiation of fish families and that the evolution of the two gene variants seems to proceed together with the evolution of fish orders and families. The temporal expression of Prdx6 mRNA in response to short-term thermal stress showed a general upregulation of prdx6b and inhibition of prdx6a, suggesting that the latter is the variant most affected by temperature increase. The variations of mRNA accumulation are more conspicuous in heart than the liver, probably related to behavioral changes of the specimens in response to elevated temperature. These data, together with the peculiar differences between the molecular structures of the two Prdx6s in T. bernacchii as well as in the tropical species Stegastes partitus, suggest an adaptation that allowed these poikilothermic aquatic vertebrates to colonize very different environments, characterized by different temperature ranges.

show abstract

Full-length cDNA cloning, molecular characterization and differential expression analysis of peroxiredoxin 6 from Ovis aries

Cited by 19 publications

References 46 publications

Full-Length cDNA Cloning, Molecular Characterization and Differential Expression Analysis of Lysophospholipase I from Ovis aries

Full-Length cDNA Cloning, Molecular Characterization and Differential Expression Analysis of Lysophospholipase I from Ovis aries

Isolation and characterisation of peroxiredoxin 6 promoter from sheep (Ovis aries)

Peroxiredoxin 6 from the Antarctic emerald rockcod: molecular characterization of its response to warming

Contact Info

Product

Resources

About