Molecular Cloning and Expression Analysis of Bovine Alpha-tocopherol Transfer Protein (α-TTP)
Journal Title: Annual Research & Review in Biology - Year 2017, Vol 12, Issue 5
Abstract
Aims: To understand the mechanisms by which cattle circulate and accumulate vitamin E, we cloned the cDNA for bovine α-tocopherol transfer protein (α-TTP) and examined its expression in different tissues. Methodology: A full length α-TTP cDNA was amplified from bovine liver by RT-PCR. Poly (A)+ RNA obtained from bovine tissues was subjected to RT-PCR analysis to examine α-TTP mRNA expression. Western blot analysis was performed using polyclonal antibody raised against an oligopeptide derived from bovine α-TTP to examine α-TTP protein expression in various bovine tissues. The localization of α-TTP in bovine lung tissue was examined by immunostaining with anti-bovine α-TTP polyclonal antibody. Results: The open reading frame consists of 846 nucleotides encoding 282 amino acids with 98% and 83% identities to sheep and rat orthologs, respectively. Bovine α-TTP mRNA and protein were expressed most strongly in liver and lung, whereas expression of α-TTP mRNA and protein are reported to be very weak or absent in human and rodent lungs. In the lung, immunostaining suggested that α-TTP is expressed specifically in alveolar walls, which consists of alveolar cells, epithelial cells of small bronchi, and endothelial cells of pulmonary blood vessels. Conclusion: These results suggest that, in the lung, α-TTP is involved in supplying vitamin E to alveolar surfactant in order to protect the lung tissue from oxidative stress, and that this role may be more important in bovines than in other mammals.
Authors and Affiliations
Yoshitomo Taguchi, Mari Komatsu Tanaka, Norie Hirose, Yurie Kaji, Kazuhiro Saeki
Keywords
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- EP ID EP313525
- DOI 10.9734/ARRB/2017/33400
- Views 69
- Downloads 0
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