Structure, Expression and Functions of Bovine Alpha-Tocopherol Transfer Protein (α-TTP) | Chapter 07 | Recent Advances in Biological Research Vol. 5
α-tocopherol transfer protein (α-TTP)
of bovine consists of 282 amino acids with 98% and 83% identities to sheep and
rat orthologs, respectively. Bovine α-TTP has an additional 5 amino acids
(GEEVT) at the C terminus, which rat, human, mouse α-TTPs do not have. The
Blast research suggested that the C-terminal sequences of α-TTP are specific
for Cetartiodactyla animals. Bovine α-TTP mRNA and protein were expressed most
strongly in liver, and also in 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. 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.
Author(s) Details
Dr. Yoshitomo Taguchi
Department of Genetic
Engineering, Faculty of Biology-Oriented Science and Technology, Kindai
University, Wakayama 649-6493, Japan.
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