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Molecular Cloning and Expression Analysis of Bovine Alpha-tocopherol Transfer Protein (α-TTP)

Yoshitomo Taguchi, Mari Komatsu-Tanaka, Norie Hirose, Yurie Kaji, Kazuhiro Saeki

Annual Research & Review in Biology · pp. 1–7 · Published 16 May 2017

10.9734/ARRB/2017/33400

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.

Vitamin E α-TTP α-tocopherol bovine lung alveolar cells

References (6)

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Cited by 1

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Satoshi Haga, Hiroshi Ishizaki, Sanggun Roh · Animals · 2021

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