Tocopherol (Alpha) Transfer Protein Proteins (TTPA)

Human Tocopherol (Alpha) Transfer Protein (TTPA) interaction partners

1. These findings provide the basis for a proposed mechanistic model that describes TTP (show ADAMTS13 Proteins)-facilitated trafficking of alpha-tocopherol through hepatocytes.

2. Single-nucleotide polymorphisms that are commonly found in healthy humans dramatically affect promoter activity of the TTPA gene.

3. The crystal structure of the alpha-TTP-phosphatidylinositol phosphates (PIPs (show GPRASP1 Proteins)) complex revealed that the familial vitamin E deficiency-related arginine residues interacted with phosphate groups of the PIPs (show GPRASP1 Proteins) and that the PIPs (show GPRASP1 Proteins) binding caused the lid of the alpha-tocopherol-binding pocket to open.

4. Data show that reduction ("knockdown") of tocopherol transfer protein (TTP (show ADAMTS13 Proteins)) expression resulted in resistance to the vitamin E.

5. 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.

6. First case of a mutated form of the TTPA gene in a patient also carrying a spinocerebellar ataxia type 8 expansion.

7. 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

8. Findings suggest the possibility that ataxia with vitamin E deficiency syndrome (AVED) may not arise from an inability of TTP (show ADAMTS13 Proteins) to bind or to transfer alpha tocopherol, but rather from defects in other activities of the protein.

9. Nuclear localization of TTPA in in trophoblast, fetal capillaries' endothelium and amnion epithelium of human term placentamay represent a novel function of TTPA

10. 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.

Mouse (Murine) Tocopherol (Alpha) Transfer Protein (TTPA) interaction partners

1. Results suggest that lipid peroxidation due to depletion of alpha-tocopherol impairs Abeta (show APP Proteins) clearances from the brain and from the blood, possibly causing increased Abeta (show APP Proteins) accumulation in Ttpa(-/-)APPsw brain and plasma.

2. Endogenous TTPA, through the enhancement of MMP 9 (show MMP9 Proteins) expression and proteolytic activation, plays an essential role in the pathogenesis of heparin-produced cerebral hemorrhage.

3. TTP (show ZFP36 Proteins) transports alpha-TCP and oral administration of TTP (show ZFP36 Proteins) compensates for TTP (show ZFP36 Proteins) in TTP (show ZFP36 Proteins)-deficient mice

4. These data suggest that in vivo network of alpha-tocopherol (AT), AT-metabolites and ATTP (show UEVLD Proteins) affects the transcription of genes driven by AhR (show AHR Proteins), Nrf2 (show NFE2L2 Proteins) and NF-kappaB (show NFKB1 Proteins), transcription factor networks.

5. p75(NTR (show NGFR Proteins))is up-regulated after tissue injury, blocks fibrinolysis by down-regulating the serine protease (show F2 Proteins), tissue plasminogen activator (show PLAT Proteins), and up-regulating PAI-1 (show SERPINE1 Proteins).

6. changes in hepatic TTP (show ZFP36 Proteins) concentrations were minimal in response to dietary vitamin E levels or environmental tobacco smoke-related oxidative stress

7. Increase expression of tPA implicate fibrinolysis in ALD progression.