Interaction between thyroid hormones and cellular constituents

Tata, Jamshed R.; Ernster, Lars; Suranyi, Eva M.

doi:10.1016/0006-3002(62)90867-3

Cited by 24 publications

(5 citation statements)

References 15 publications

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“…Unlike the cytosolic retinoid-binding proteins CRABP and CRBP which do not show any variability (see MorrissKay, 1992), CTBPs from different sources or studied in different laboratories, exhibit a wide range of properties (Tata et al, 1962;Hashizume et al, 1989a;Jaffe, 1978;Kato et al, 1989;Kobayashi et al, 1991;Fanjul and Farias, 1991;Yoshizato et al, 1975;Lennon, 1992). These include a size variation of 25 -200 kDa, activation by NADPH, metal ions or -SH reagents, endogenous enzyme activities and T,-binding affinities ranging over Kd 10-10-10-5 M. Since a CTBP from Xenopus cells had not previously been described, it became important to precisely characterize the properties of xCTBP in whole cytosol and to monitor these at every step of the purification procedure.…”

Section: Discussionmentioning

confidence: 99%

“…Since the first reports of a cytosolic L-thyroxine-(TJ-binding protein in rat skeletal muscle (Tata, 1958;Tata et al, 1962), multiple CTBPs with varying characteristics, depending on the species, tissue and method of characterization, have been reported (Kitagawa et al, 1987;Dillman et al, 1974;Defer et al, 1975;Lennon, 1992;Hashizume et al, 1989b;Kobayashi et al, 1991). Interestingly, one of these has been found to be homologous to a subunit of pyruvate kinase, while another CTBP-like protein, activated by NADPH, has also been described (Kato et al, 1989;Ashizawa and Cheng, 1992;Lennon, 1992;Hashizume et al, 1989b;Kobayashi et al, 1991).…”

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confidence: 99%

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Purification and Characterization of a Cytosolic Thyroid‐Hormone‐Binding Protein (CTBP) inXenopusLiver

Yamauchi¹,

Tata²

1994

European Journal of Biochemistry

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A variety of cytosolic thyroid-hormone-binding proteins with different characteristics have previously been reported. Here, we first describe the thyroid-hormone-binding characteristics of adult Xenopus liver cytosol, then a novel procedure for purifying cytosolic thyroid-hormone-binding protein (CTBP) from Xenopus liver (xCTBP). The procedure consists of combining preparative isoelectrofocusing, FPLC cation-exchange chromatography, HPLC hydrophobic-interaction chromatography and ultraviolet light cross-linking of '251-labeled 3,3'5-triiodo-~-thyronine (T,). The isolated xCTBP thus prepared retained all the characteristics of the major thyroid-hormone-(TH)-binding component of the unfractionated cytosol. It is a monomeric protein of approximately 59 kDa with an isoelectric point of 7.020.1, binds T, with a higher affinity than its analogs with a Kd of approximately 9 nM, and is sensitive to sulfhydryl agents but not to NADPH. In several respects, xCTBP differs from most CTBP-like preparations from other sources described hitherto. Microsequencing of a 23-amino-acid peptide generated from xCTBP by cyanogen bromide digestion revealed 92-100% identity of a 23-amino-acid sequence of several mammalian (amino acids 236-258) and avian (amino acids 245 -267) cytosolic aldehyde dehydrogenases (ALDH) ; xCTBP also exhibited significant similarity of amino acid composition with rat ALDH. This novel finding of sequence identity between a CTBP and ALDH, and the diversity of CTBPs from different sources, suggest that a variety of cytosolic proteins, depending on the species and tissue, can function as thyroid-hormone-binding proteins.The kinetics and nature of response to hormones and other biologically active signals that act via nuclear receptors, such as thyroid and steroid hormones, vitamin D, and retinoic acid, are determined by intracellular components with which these molecules interact before reaching their receptors. These have been well characterized for glucocorticoid hormone, progesterone and retinoids, the interaction between retinoids and cytosolic retinoic acid and retinol-binding proteins (CRABP and CRBP) being well documented, but their exact physiological function is not clear (Maden et al., 1989;Maden, 1991;Ruberte et al., 1991;Morriss-Kay, 1992). In a different type of interaction, glucocorticoids and progesterone are now known to move into the nucleus associated with a complex in the cytoplasm formed between the relevant receptor and the heat-shock protein hsp-90 (Catelli et al., 1985;Kost et al., 1989;Pratt, 1993).Although the presence of cytosolic thyroid-hormonebinding proteins (CTBPs) has been known for some time, there seems to be no concensus about their identity or their Correspondence to J. R. Tata,

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Purification and Characterization of a Cytosolic Thyroid‐Hormone‐Binding Protein (CTBP) inXenopusLiver

Yamauchi¹,

Tata²

1994

European Journal of Biochemistry

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“…Studies in vitro also do not account for the 'latent' period, which is so characteristic of action in vivo, especially as the time for hormones to enter into tissues appears to be comparatively short (see Tata, 1960). Further, isolated subcellular particles exhibit an intense thyroxine-binding in vitro which may be misinterpreted, since endogenous thyroid hormone is not exclusively concentrated in any given subcellular fraction (Tata, Ernster & Suranyi, 1962b; see Tata, 1962).…”

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The action of thyroid hormones at the cell level

Tata¹,

Ernster²,

Lindberg³

et al. 1963

Biochemical Journal

536

168

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“…Different cellular components seem to be associated with binding and deiodination of both hormones (Tata et al 1962;Stanbury et al I960;Oppenheimer et al 1970). It has not been established unequi¬ vocally whether both iodothyronines are bound and degraded by the same cell site, although recent studies seem to indicate that T4 and T3 share cellular bonds (Samuel 8c Tsai 1974;Oppenheimer et al 1974;DeGroot 8c Torresani 1975).…”

Section: Discussionmentioning

confidence: 97%

Reciprocal Effects of Thyroxine and Triiodothyronine on Their Deiodination by Rat Tissues in Vitro

Zaninovich

1976

Acta Endocrinologica

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The reciprocal effects of loading doses of thyroxine (T4) or triiodothyronine (T3) on the deiodination of their 125iodine-labelled isotopes by rat muscle and liver homogenates were studied. In 21 experiments muscle homogenates deiodinated a mean 45.0 % of a tracer dose of [125I]T4 and 18.0% of [125I]T3. On addition of graded amounts of nonradioactive T4 or T3 the percentual deiodination of both labelled hormones progressively declined. This effect was significantly greater in homogenates incubated with non-radioactive T4, thus reflecting a stronger affinity of this hormone for muscle deiodinating sites. This correlate with the greater displacement of [125I]T3 as revealed by the percentage of recovered labelled hormone. In 18 experiments liver homogenates deiodinated a mean 14.6% of a tracer amount of [125I]T4 and 8.5% of [125I]T3. The addition of a T4-or a T3-load was followed by a smaller decrease in percentual deiodination of both labelled hormones as compared to muscle homogenates. Unlike the effects observed in muscle, the breakdown of [125I]T4 and [125I]T3 by liver homogenates was equally affected by similar amounts of stable T4 or T3. It is concluded that in the present in vitro system T4 and T3 share cellular sites of deiodination * Career Investigator, Consejo Nacional de Investigaciones Científices y Técnicas of Argentina (CONICET).

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Interaction between thyroid hormones and cellular constituents

Cited by 24 publications

References 15 publications

Purification and Characterization of a Cytosolic Thyroid‐Hormone‐Binding Protein (CTBP) inXenopusLiver

Purification and Characterization of a Cytosolic Thyroid‐Hormone‐Binding Protein (CTBP) inXenopusLiver

The action of thyroid hormones at the cell level

Reciprocal Effects of Thyroxine and Triiodothyronine on Their Deiodination by Rat Tissues in Vitro

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