Abstract
α-Tocopherol transfer protein (αTTP), which specifically binds this vitamin and enhances its transfer between separate membranes, was previously isolated from rat liver cytosol. In the current study we demonstrated the presence of αTTP in human liver by isolating its cDNA from a human liver cDNA library. The cDNA for human αTTP predicts 278 amino acids with a calculated molecular mass of 31749, and the sequence exhibits 94% similarity with rat αTTP at the amino acid level. The recombinant human αTTP expressed in Escherichia coli exhibits both α-tocopherol transfer activity in an in vitro assay and crossreactivity to the anti-(rat αTTP) monoclonal antibody. Northern blot analysis revealed that human αTTP is expressed in the liver like rat αTTP. The human and rat αTTPs show structural similarity with other apparently unrelated lipid-binding/transfer proteins, i.e, retinaldehyde-binding protein present in retina, and yeast SEC14 protein, which possesses phosphatidylinositol/phosphatidylcholine transfer activity. Both Southern-blot hybridization of human-hamster somatic cell hybrid lines and fluorescence in situ hybridization revealed a single αTTP gene corresponding to the 8q13.1-13.3 region of chromosome 8, which is identical to the locus of a recently described clinical disorder, ataxia with selective vitamin E deficiency (AVED). The relationship between αTTP and AVED will be discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 437-443 |
| Number of pages | 7 |
| Journal | Biochemical Journal |
| Volume | 306 |
| Issue number | 2 |
| Publication status | Published - 1995 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Medicine(all)
- Molecular Biology
- Cell Biology
Cite this
Human α-tocopherol transfer protein : cDNA cloning, expression and chromosomal localization. / Arita, Makoto; Sato, Y.; Miyata, A.; Tanabe, T.; Takahashi, E.; Kayden, H. J.; Arai, H.; Inoue, K.
In: Biochemical Journal, Vol. 306, No. 2, 1995, p. 437-443.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Human α-tocopherol transfer protein
T2 - cDNA cloning, expression and chromosomal localization
AU - Arita, Makoto
AU - Sato, Y.
AU - Miyata, A.
AU - Tanabe, T.
AU - Takahashi, E.
AU - Kayden, H. J.
AU - Arai, H.
AU - Inoue, K.
PY - 1995
Y1 - 1995
N2 - α-Tocopherol transfer protein (αTTP), which specifically binds this vitamin and enhances its transfer between separate membranes, was previously isolated from rat liver cytosol. In the current study we demonstrated the presence of αTTP in human liver by isolating its cDNA from a human liver cDNA library. The cDNA for human αTTP predicts 278 amino acids with a calculated molecular mass of 31749, and the sequence exhibits 94% similarity with rat αTTP at the amino acid level. The recombinant human αTTP expressed in Escherichia coli exhibits both α-tocopherol transfer activity in an in vitro assay and crossreactivity to the anti-(rat αTTP) monoclonal antibody. Northern blot analysis revealed that human αTTP is expressed in the liver like rat αTTP. The human and rat αTTPs show structural similarity with other apparently unrelated lipid-binding/transfer proteins, i.e, retinaldehyde-binding protein present in retina, and yeast SEC14 protein, which possesses phosphatidylinositol/phosphatidylcholine transfer activity. Both Southern-blot hybridization of human-hamster somatic cell hybrid lines and fluorescence in situ hybridization revealed a single αTTP gene corresponding to the 8q13.1-13.3 region of chromosome 8, which is identical to the locus of a recently described clinical disorder, ataxia with selective vitamin E deficiency (AVED). The relationship between αTTP and AVED will be discussed.
AB - α-Tocopherol transfer protein (αTTP), which specifically binds this vitamin and enhances its transfer between separate membranes, was previously isolated from rat liver cytosol. In the current study we demonstrated the presence of αTTP in human liver by isolating its cDNA from a human liver cDNA library. The cDNA for human αTTP predicts 278 amino acids with a calculated molecular mass of 31749, and the sequence exhibits 94% similarity with rat αTTP at the amino acid level. The recombinant human αTTP expressed in Escherichia coli exhibits both α-tocopherol transfer activity in an in vitro assay and crossreactivity to the anti-(rat αTTP) monoclonal antibody. Northern blot analysis revealed that human αTTP is expressed in the liver like rat αTTP. The human and rat αTTPs show structural similarity with other apparently unrelated lipid-binding/transfer proteins, i.e, retinaldehyde-binding protein present in retina, and yeast SEC14 protein, which possesses phosphatidylinositol/phosphatidylcholine transfer activity. Both Southern-blot hybridization of human-hamster somatic cell hybrid lines and fluorescence in situ hybridization revealed a single αTTP gene corresponding to the 8q13.1-13.3 region of chromosome 8, which is identical to the locus of a recently described clinical disorder, ataxia with selective vitamin E deficiency (AVED). The relationship between αTTP and AVED will be discussed.
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M3 - Article
VL - 306
SP - 437
EP - 443
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 2
ER -