Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence

Cheng, Sheue-yann; Pages, Robert A.; Saroff, H. A.; Edelhoch, Harold; Robbins, Jacob

doi:10.1021/bi00635a031

Cited by 72 publications

(75 citation statements)

References 20 publications

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“…8, A and B, insets) yielded K d values of 1.2 M for the WT-TTR tetramer and 2.6 M for the V30M-TTR tetramer, in agreement with previous studies on WT-TTR (24). Competition studies have shown that ANS binds to the same sites as thyroxine in WT-TTR (24). The thyroxine-binding site is highly apolar, which justifies the increase in fluorescence quantum yield and the blue shift of the emission maximum of ANS upon binding to tetrameric TTR.…”

Section: Resultssupporting

confidence: 91%

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The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution

Quintas¹,

Saraiva²,

Brito³

1999

Journal of Biological Chemistry

171

130

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In amyloidosis, normally innocuous soluble proteins polymerize to form insoluble fibrils. Amyloid fibril formation and deposition have been associated with a wide range of diseases, including spongiform encephalopathies, Alzheimer's disease, and familial amyloid polyneuropathies (FAP). In certain forms of FAP, the amyloid fibrils are mostly constituted by variants of transthyretin (TTR), a homotetrameric plasma protein implicated in the transport of thyroxine and retinol. The most common amyloidogenic TTR variant is V30M-TTR, and L55P-TTR is the variant associated with the most aggressive form of FAP. Recently, we reported that TTR dissociates to a monomeric species at pH 7.0 and nearly physiological ionic strengths (Quintas, A., Saraiva, M. J., and Brito, R. M. (1997) FEBS Lett. 418, 297-300). Here, we show that the tetramer dissociation is apparently irreversible; and based on intrinsic tryptophan fluorescence and fluorescence quenching experiments, we show that the monomeric species formed upon tetramer dissociation is non-native. We also show, based on 1-anilino-8-naph-thalenesulfonate binding studies, that this monomeric species appears not to behave like a molten globule. These data allowed us to propose a model for TTR amyloidogenesis based on tetramer dissociation occurring naturally under commonly observed physiological solution conditions.

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Section: Resultssupporting

confidence: 91%

“…A nonlinear fit to the binding data (Fig. 8, A and B, insets) yielded K d values of 1.2 M for the WT-TTR tetramer and 2.6 M for the V30M-TTR tetramer, in agreement with previous studies on WT-TTR (24). Competition studies have shown that ANS binds to the same sites as thyroxine in WT-TTR (24).…”

Section: Resultssupporting

confidence: 88%

The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution

Quintas¹,

Saraiva²,

Brito³

1999

Journal of Biological Chemistry

171

130

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“…Ligand-binding studies with TTR have generally been carried out using compounds structurally similar to T 4 , such as the fluorescent probes 8-anilinonaphthalene-1-sulphonate (Cheng et al, 1977) and 1-dimethylaminonaphthalene-5-sulphonate (Nilsson et al, 1975). Such binding studies are unlikely to mirror perfectly the binding of T 4 to TTR and in vivo the blood concentrations of the hormone are not high enough for the second hormone-binding site to be occupied.…”

Section: Tablementioning

confidence: 99%

Evolution of the Thyroid Hormone-Binding Protein, Transthyretin

Power

Elias

Richardson

et al. 2000

General and Comparative Endocrinology

190

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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“…Two mol of T4 are bound per mol of protein with binding constants two orders of magnitude different for each tool. This is interpreted in terms of a negative cooperativity between the sites [6,7]. The study described here was undertaken with the intention of using TTR Trp-41 and Trp-79 fluorescence which can give structural information, to detect conformational changes associated to its interaction with T4.…”

Section: Introductionmentioning

confidence: 99%

Fluorescence study of the thyroxine‐dependent conformational changes in human serum transthyretin

González

Tapia

1992

FEBS Letters

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Fluorescence studies of transthyretin (TTR) were conducted to detect structural changes associated with the environment of its two tryptophans, induced by binding of thyroxine (T~). Non-radiative tryptophans relaxation rate has an activation energy of 6.4 kcal/mol for TTR, which is decreased to 4.4 Real/reel for TTR-T~ complex. The maximum fl uore~'~nce wavelength was red-shifted as the excitation wavelength was increased. 1"4 changed the magnitude of this shill 1"4 binding per se changed the emission maximum reflecting different environments of the tryptophans. Doublequenching experiments also showed that Ta produces changes in the trl,'ptophans environments. These findings were interpreted as the result of structural alterations in the protein matrix induced by T~ which contribute in part to explain the negative ¢ooperativity associated with the occupancy of the second binding site.

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Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence

Cited by 72 publications

References 20 publications

The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution

The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution

Evolution of the Thyroid Hormone-Binding Protein, Transthyretin

Fluorescence study of the thyroxine‐dependent conformational changes in human serum transthyretin

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