Expression and Refolding of Recombinant Human α-Tocopherol Transfer Protein Capable of Specific α-Tocopherol Binding

Panagabko, Candace; Morley, Samantha; Neely, Steve; Lei, Huangshu; Manor, Danny; Atkinson, Jeffrey

doi:10.1006/prep.2001.1576

Cited by 23 publications

(17 citation statements)

References 34 publications

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“…An important cautionary note was that a functional domain called the CRAL-TRIO domain was found in sheep α-TTP, the CRAL-TRIO domain was a Sec14p-like lipid-binding domain. This result was also in agreement with previous report that the α-TTP was first associated with the CRAL-TRIO family of proteins and then included into the Sec14 superfamily (Panagabko et al, 2002;Regina, 2009). …”

Section: Discussionsupporting

confidence: 94%

“…α-TTP has been purified from rat (Sato et al, 1991;Yoshida et al, 1992) and human livers (Arita et al, 1995) and the amino acid sequences have been reported (Arita et al, 1995;Sato et al, 1993). Based on sequence analysis, α-TTP was classified as a member of the SEC14-like protein family, with a characteristic CRAL-TRIO lipid-binding domain (Bella et al, 2006;Kalikin et al, 2001;Panagabko et al, 2002;Regina, 2009). Close biochemical examination revealed that of all related lipidbinding proteins from the CRAL-TRIO family, only α-TTP bound α-tocopherol with high affinity and selectivity (Bella et al, 2006;Panagabko et al, 2003), it was therefore generally accepted that α-TTP function in the liver was the key specific biochemical determinant of α-tocopherol levels in humans and rodents (Kaempf-Rotzoll et al, 2003;Thakur et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Molecular cloning and characterization of the sheep α-TTP gene and its expression in response to different vitamin E status

Liu¹,

Luo²,

Yue³

et al. 2012

Gene

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Section: Discussionsupporting

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Molecular cloning and characterization of the sheep α-TTP gene and its expression in response to different vitamin E status

Liu¹,

Luo²,

Yue³

et al. 2012

Gene

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“…Recombinant wildtype human TTP was expressed in bacteria as described and purified as described [11], [33]. Briefly, GST-TTP fusion protein was isolated from over-expressing bacteria using glutathione affinity chromatography, cleaved with thrombin, re-purified by two ammonium sulfate precipitations and stored at −20°C in 20 mM Tris pH 8.0, 150 mM NaCl, 50% (v/v) glycerol, 1 mM DTT.…”

Section: Methodsmentioning

confidence: 99%

The α-Tocopherol Transfer Protein Is Essential for Vertebrate Embryogenesis

et al. 2012

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The hepatic α-tocopherol transfer protein (TTP) is required for optimal α-tocopherol bioavailability in humans; mutations in the human TTPA gene result in the heritable disorder ataxia with vitamin E deficiency (AVED, OMIM #277460). TTP is also expressed in mammalian uterine and placental cells and in the human embryonic yolk-sac, underscoring TTP’s significance during fetal development. TTP and vitamin E are essential for productive pregnancy in rodents, but their precise physiological role in embryogenesis is unknown. We hypothesize that TTP is required to regulate delivery of α-tocopherol to critical target sites in the developing embryo. We tested to find if TTP is essential for proper vertebrate development, utilizing the zebrafish as a non-placental model. We verify that TTP is expressed in the adult zebrafish and its amino acid sequence is homologous to the human ortholog. We show that embryonic transcription of TTP mRNA increases >7-fold during the first 24 hours following fertilization. In situ hybridization demonstrates that Ttpa transcripts are localized in the developing brain, eyes and tail bud at 1-day post fertilization. Inhibiting TTP expression using oligonucleotide morpholinos results in severe malformations of the head and eyes in nearly all morpholino-injected embryos (88% compared with 5.6% in those injected with control morpholinos or 1.7% in non-injected embryos). We conclude that TTP is essential for early development of the vertebrate central nervous system.

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“…This method can also benefit from the use of LArgHCl. The yield of active -tocopherol transfer protein, e.g., could be optimized by matrix-assisted refolding on an immobilized metal affinity column in the presence of 0.5 M L-ArgHCl [38].…”

Section: Column Chromatographymentioning

confidence: 99%

Suppression of Protein Aggregation by L-Arginine

Lange

Rudolph

2009

CPB

108

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L-Arginine is one of the most commonly used and most generally applicable suppressors of protein aggregation. Its effect as enhancer of in vitro protein refolding was serendipitously discovered two decades ago. This article aims at giving a brief overview about the discovery of the arginine effect, the range of its applications that have been explored over the past two decades, and of the current state of the discussion regarding the mechanisms responsible for the action of L-arginine as suppressor of aggregation.

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Expression and Refolding of Recombinant Human α-Tocopherol Transfer Protein Capable of Specific α-Tocopherol Binding

Cited by 23 publications

References 34 publications

Molecular cloning and characterization of the sheep α-TTP gene and its expression in response to different vitamin E status

Molecular cloning and characterization of the sheep α-TTP gene and its expression in response to different vitamin E status

The α-Tocopherol Transfer Protein Is Essential for Vertebrate Embryogenesis

Suppression of Protein Aggregation by L-Arginine

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