Retinol-binding protein: the transport protein for vitamin A in human plasma

Kanai, Masamitsu; Raz, Amiram; Goodman, DeWitt S.

doi:10.1172/jci105889

Cited by 823 publications

(323 citation statements)

References 36 publications

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“…We therefore undertook this study in order to find an easier and less time-consuming way of preparing the protein in highly purified form. The method was based on the earlier observation that retinol binding protein under physiological conditions is firmly bound to prealbumin [ 1,2], and that the two proteins dissociate a t a low ionic strength [23]. Thus the isolation of retinol binding protein by affinity chromatography by using a gel prepared by coupling prealbumin to Sepharose, appeared advantagous.…”

Section: Discussionmentioning

confidence: 99%

Isolation of the Human Retinol Binding Protein by Affinity Chromatography

Vahlquist¹,

Nilsson²,

Peterson³

1971

European Journal of Biochemistry

113

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The human retinol binding protein, which in plasma is bound to thyroxine binding prealbumin, has been isolated in free form from urine of patients with tubular proteinuria and from normal serum. The isolation procedure for urinary retinol binding protein involved gel chromatography and affinity chromatography on a column of prealbumin coupled to Sepharose, whereas the isolation of serum retinol binding protein required three fractionation steps : DEAESephadex chromatography, gel chromatography, and affinity chromatography.The retinol binding protein from urine and serum was obtained in a yield of 31 o/o and 42 Oi0, respectively. The relatively low yield of the urinary protein was explained by the fact that two forms of retinol binding protein were present in the urine, one of which did not bind to prealbumin. The purity of the retinol binding protein isolated from urine and serum was established by the following criteria : immunoelectrophoresis, polyacrylamide gel electrophoresis, amino acid analyses, and sedimentation equilibrium ultracentrifugations.The use of affinity chromatography offers a simple and rapid procedure for the isolation of moderate quantities of highly purified retinol binding protein from urine and serum.

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Section: Discussionmentioning

confidence: 99%

Isolation of the Human Retinol Binding Protein by Affinity Chromatography

Vahlquist¹,

Nilsson²,

Peterson³

1971

European Journal of Biochemistry

113

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“…RBP is a single polypeptide chain of 182 amino acid residues of 21 kDa (Goodman, 1984) that forms a complex with tetrameric TTR under physiological conditions and that prevents glomerular filtration of RBP in the kidney (Kanai et al, 1968;Peterson, 1971). The presence of retinol bound to RBP is essential for the formation of Transthyretin Evolution a stable complex with TTR and crystallographic studies have established the stoichiometry of the complex as a maximum of two RBP molecules per TTR tetramer (Noy et al, 1992;van Jaarsveld et al, 1973;Monaco et al, 1995).…”

Section: Transthyretin and Retinol-binding Protein Interactionmentioning

confidence: 99%

Evolution of the Thyroid Hormone-Binding Protein, Transthyretin

Power

Elias

Richardson

et al. 2000

General and Comparative Endocrinology

188

119

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Transthyretin (TTR) belongs to a group of proteins, which includes thyroxine-binding globulin and albumin, that bind to and transport thyroid hormones in the blood. TTR is also indirectly implicated in the carriage of vitamin A through the mediation of retinol-binding protein (RBP). It was first identified in 1942 in human serum and cerebrospinal fluid and was formerly called prealbumin for its ability to migrate faster than serum albumin on electrophoresis of whole plasma. It is a single polypeptide chain of 127 amino acids (14,000 Da) and is present in the plasma as a tetramer of noncovalently bound monomers. The major sites of synthesis of TTR in eutherian mammals, marsupials, and birds are the liver and choroid plexus but in reptiles it is synthesised only in the choroid plexus. The observation that TTR is strongly expressed in the choroid plexus but not in the liver of the stumpy-tailed lizard and the strong conservation of expression in the choroid plexus from reptiles to mammals have been taken as evidence to suggest that extrahepatic synthesis of TTR evolved first. The identification and cloning of TTR from the liver of an amphibian, Rana catesbeiana, and a teleost fish, Sparus aurata, and its absence from the choroid plexus of both species suggest an alternative model for its evolution. Protein modelling studies are presented that demonstrate differences in the electrostatic characteristics of the molecule in human, rat, chicken, and fish, which may explain why, in contrast to TTR from human and rat, TTR from fish and birds preferentially binds triiodo-L-thyronine.

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“…T for thermal unfolding and all of them unm folded and dissociated simultaneously, obeying a two-state mechanism between the folded tetrameric state and the unfolded monomeric state, according to the scheme N ¡ 4U. 4 …”

Section: Introductionmentioning

confidence: 99%

Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin

Shnyrov

Villar

Zhadan

et al. 2000

Biophysical Chemistry

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Ž. Familial amyloidotic polyneuropathy FAP is an autosomal dominant hereditary type of amyloidosis involving Ž . amino acid substitutions in transthyretin TTR . V30M-TTR is the most frequent variant, and L55P-TTR is the variant associated with the most aggressive form of FAP. The thermal stability of the wild-type, V30M-TTR, L55P-TTR and a non-amyloidogenic variant, T119M-TTR, was studied by high-sensitivity differential scanning Ž . calorimetry DSC . The thermal unfolding of TTR is a spontaneous reversible process involving a highly co-operative transition between folded tetramers and unfolded monomers. All variants of transthyretin are very stable to the thermal unfolding that occurs at very high temperatures, most probably because of their oligomeric structure. The data presented in this work indicated that for the homotetrameric form of the wild-type TTR and its variants, the order of stability is as follows: wild-type TTRR T119M-TTR) L55P-TTR) V30M-TTR, which does not correlate with their known amyloidogenic potential. ᮊ 2000 Elsevier Science B.V. All rights reserved.

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Retinol-binding protein: the transport protein for vitamin A in human plasma

Cited by 823 publications

References 36 publications

Isolation of the Human Retinol Binding Protein by Affinity Chromatography

Isolation of the Human Retinol Binding Protein by Affinity Chromatography

Evolution of the Thyroid Hormone-Binding Protein, Transthyretin

Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin

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