Clinical Observations on Serum Globulin Thyroxine-Binding Capacity, Using a Simplified Technique*

Tanaka, Shigeru; Starr, Paul

doi:10.1210/jcem-19-1-84

Cited by 39 publications

(17 citation statements)

References 4 publications

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“…Subsequently, Beierwaltes, Carr and Hunter reported similar findings in other members of this family (12). The converse situation of low serum PBI and low TBG but presumably normal free thyroxine has been reported by Tanaka and Starr (13) and studied in detail by Ingbar and Freinkel (7,14).…”

Section: Discussionsupporting

confidence: 73%

Measurement of Free Thyroxine Concentration in Human Serum*

Sterling¹,

Hegedus²

1962

J. Clin. Invest.

111

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Section: Discussionsupporting

confidence: 73%

Measurement of Free Thyroxine Concentration in Human Serum*

Sterling¹,

Hegedus²

1962

J. Clin. Invest.

111

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“…In addition, the binding capacity of the T4-binding prealbumin (TBPA) is usually diminished (1,7,8). Evidence as to whether a similar decrease in binding capacity occurs in the case of the T4-binding globulin (TBG) has been more variable (1,(8)(9)(10)(11)(12)(13)(14)(15)(16).…”

mentioning

confidence: 99%

Thyroid hormone transport in the serum of patients with thyrotoxic graves' disease before and after treatment

Braverman¹,

Foster²,

Ingbar³

1968

J. Clin. Invest.

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“…TBG deficiency in humans was described by Tanaka and Starr (30), who noted a complete absence of TBG binding of radiolabeled thyroxine in the plasma electrophoretogram. Subsequently, careful study of a number of families with absent or low TBG have provided evidence for X-linked inheritance (31).…”

Section: Discussionmentioning

confidence: 92%

Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases.

Flink¹,

Bailey²,

Gustafson³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

162

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Antibodies directed against thyroxine-binding globulin (TBG) have been used to screen a human liver Xgtll expression library. A 1.46-kilobase clone was identified which encodes nearly the complete amino acid sequence, beginning at amino acid 17 of the mature protein. To complete the protein sequence, the cDNA clone was used to identify a genomic clone coding for TBG in a human X chromosome library. The overlapping recombinant clones contained an open reading frame coding for 415 amino acids followed by a polyadenylylation signal (AATAAA) located 275 nucleotides from a TAG termination codon. Beginning at residue 21, the deduced amino acid sequence agrees closely with the known NH2-terminal sequence of the mature peptide. The preceding 20 amino acid residues are hydrophobic in character and presumably represent a leader sequence. Four glycosylation sites were identified, corresponding to the number determined for the purified protein. DNA blot hybridization revealed a single-copy gene, which by chromosomal analysis was found to be located on the long arm of the X chromosome. Unexpectedly, the nucleotide sequence of TBG is closely homologous to those encoding the plasma serine antiproteases a1-antichymotrypsin and a1-antitrypsin. However, there is little overall homology between TBG and transthyretin (prealbumin), the other major thyroxine-binding protein of human plasma.In most vertebrate species, thyroxine-binding globulin (TBG) has been reported to be the major thyroxine-binding protein (1). It is a glycoprotein (molecular mass about 54 kDa) that is synthesized in the liver as a polypeptide of 45 kDa (2). TBG represents a relatively rare translation product of total liver mRNA, accounting for only about 0.018% of total acidprecipitable radioactivity (2). Efforts to obtain detailed information about the structure of TBG and its thyroxinebinding site have been hampered by the presence of multiple electrophoretic forms and the inability to crystallize the protein (3, 4).In this report, we describe the use of serum containing polyclonal antibodies directed against human TBG to isolate cDNA clones coding for TBG from a human liver Xgtll expression library (5). To complete the coding sequence, one of these clones was used to identify a genomic clone from a human X chromosome library. Residues 21-40 of the deduced amino acid sequence correspond closely to the NH2-terminal amino acid sequence of mature TBG reported by Cheng (6). Amino acids 1-20 are very hydrophobic in nature and presumably represent the leader sequence of the propeptide. Unexpectedly, TBG shows a high degree of homology to a1-antichymotrypsin and a1-antitrypsin, and appears to belong to the serpin superfamily, most of which are serine proteinase inhibitors (7,8

show abstract

Clinical Observations on Serum Globulin Thyroxine-Binding Capacity, Using a Simplified Technique*

Cited by 39 publications

References 4 publications

Measurement of Free Thyroxine Concentration in Human Serum*

Measurement of Free Thyroxine Concentration in Human Serum*

Thyroid hormone transport in the serum of patients with thyrotoxic graves' disease before and after treatment

Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases.

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