Recombinant Human Alpha-tocopherol transfer protein (TTPA)

1. alphaTTP does not appear to regulate the uptake and intracellular localization of different vitamin E congeners in cultured liver cells. PMID: 30098456
2. These findings provide the basis for a proposed mechanistic model that describes TTP-facilitated trafficking of alpha-tocopherol through hepatocytes. PMID: 27307040
3. Current results show that alphaTTP plays a role in endometrial carcinoma. Possibly endometrial cancer cells attempt to protect themselves from increasing oxidative stress by up-regulating alphaTTP. PMID: 28213729
4. Single-nucleotide polymorphisms that are commonly found in healthy humans dramatically affect promoter activity of the TTPA gene. PMID: 23079030
5. The crystal structure of the alpha-TTP-phosphatidylinositol phosphates (PIPs) complex revealed that the familial vitamin E deficiency-related arginine residues interacted with phosphate groups of the PIPs and that the PIPs binding caused the lid of the alpha-tocopherol-binding pocket to open. PMID: 23599266
6. study demonstrated that alpha -TTP can be upregulated in case of oxidative stress in BeWo trophoblast cells; speculate that possibly, alpha -TTP is notonly involved in normal pregnancy, but also in cases of pregnancy disorders with intense oxidative stress PMID: 22752767
7. Data show that reduction ("knockdown") of tocopherol transfer protein (TTP) expression resulted in resistance to the vitamin E. PMID: 20826775
8. Substitution of residues in helices A8 (F165A and F169A) and A10 (I202A, V206A and M209A) decreased the rate of intermembrane ligand transfer as well as protein adsorption to phospholipid bilayers. PMID: 21110980
9. First case of a mutated form of the TTPA gene in a patient also carrying a spinocerebellar ataxia type 8 expansion. PMID: 12470185
10. crystal structure reveals two conformations PMID: 12899840
11. the positively charged surface of TTPA may serve to orient an interacting protein, which might function to regulate the release of alpha-T through an induced change in conformation of ATTP PMID: 14657365
12. Findings suggest the possibility that ataxia with vitamin E deficiency syndrome (AVED) may not arise from an inability of TTP to bind or to transfer alpha tocopherol, but rather from defects in other activities of the protein. PMID: 15065857
13. Nuclear localization of TTPA in in trophoblast, fetal capillaries' endothelium and amnion epithelium of human term placentamay represent a novel function of TTPA PMID: 15190938
14. In Ataxia with vitamin E deficiency two TTPA mutations were identified: a truncating mutation in a homozygous patient, and a Gly246Arg missense mutation in a compound heterozygous patient associated with a mild and slowly progressive form of the disease. PMID: 15300460
15. The physiological role of TTP is anchored in its ability to direct vitamin E trafficking from the endocytic compartment to transport vesicles that deliver the vitamin to the site of secretion at the plasma membrane. PMID: 16819822
16. analysis of ligand transfer by the hepatic tocopherol transfer protein PMID: 18458085
17. in first-trimester extravillous trophoblast, syncytiotrophoblast and amniotic epithelium PMID: 18511174
18. The vitamin E deficiency with hereditary motor neuropathy was found to be homozygous for a 513insTT mutation in exon 3 of the alpha-tocopherol transfer protein gene. PMID: 18984846
19. Total deletion of the TTPA gene is expected to be associated with severe phenotype in AVED patients. PMID: 19102053
20. Genetic variation in TTPA and SEC14L2 is associated with serum alpha-tocopherol but does not have a direct effect on prostate cancer when vitamin E is administered. PMID: 19190344
21. Hydrophobic features of alpha-TTP dominating the binding energy between protein and membrane. PMID: 19458973

Show More

Hide All

HGNC: 12404

OMIM: 277460

KEGG: hsa:7274

STRING: 9606.ENSP00000260116

UniGene: Hs.69049