Isolation of a Gene Encoding Human Thyrotropin Beta Subunit

Whitfield, G. Kerr; Powers, Robin E.; Gurr, James A.; Wolf, Ofra; Kourides, Ione A.

doi:10.1007/978-1-4684-5260-0_26

Cited by 2 publications

(4 citation statements)

References 21 publications

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“…CG/3 contains a unique 30 amino acid hydrophilic carboxyl-terminal extension which contains four O-linked oligosaccharides (17)(18)(19) whereas human LHj8 and TSH/3 contain short hydrophobic stretches at their termini. These LH/3 and TSH/3 carboxyl-terminal stretches were deduced from gene sequencing (7,8,20) but not found by sequencing of the mature peptide (21,22). A similar carboxylterminal extension is seen on both mouse (23) and bovine (24) TSH/3.…”

Section: Discussionmentioning

confidence: 96%

“…In each case, a 17-kilodalton TSH/3-protein accumulates intracellularly (lanes 5, 7, and 9). Analysis of the media from these clones reveals that secretion of TSH/3 (lanes 6, 8, or 10) is similar to LH/3, and is immunoprecipitated only from the cell lysate (lanes 5,7,9). Thus, while LH/3 and TSH/3 are secreted poorly, CG/3 is secreted efficiently.…”

Section: Comparison Of Tsh/? Lh/3 and Cg/s-producing Clonesmentioning

confidence: 91%

“…was constructed by inserting the human TSH/3 gene(7,8) containing exons II and III (exon I contains nontranslatedFig. 1.…”

mentioning

confidence: 99%

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The Glycoprotein α-Subunit is Critical for Secretion and Stability of the Human Thyrotropin β-Subunit

Matzuk¹,

Kornmeier²,

Whitfield³

et al. 1988

Molecular Endocrinology

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TSH is a member of a family of heterodimeric glycoprotein hormones which have a common alpha-subunit but differ in their hormone-specific beta-subunit. To study the posttranslational processing and assembly of human TSH, eukaryotic expression vectors were constructed that contained either the human TSH beta gene only or both the TSH beta and alpha-genes. These vectors were transfected into Chinese hamster ovary cells and stable cell lines synthesizing TSH beta or TSH dimer were isolated. The kinetics of secretion of TSH beta and the rate of assembly of TSH dimer were compared to the known secretion and assembly of human LH and human CG. In the absence of the alpha-subunit, CG beta is secreted efficiently, but TSH and LH beta-subunits are slowly degraded intracellularly (t1/2 approximately equal to 6 h) and less than 10% is secreted into the medium. In the presence of the alpha-subunit CG beta was also secreted efficiently as dimer but only 50% of the LH beta appeared in the medium as LH dimer. However, unlike LH beta, the alpha-subunit efficiently combines with TSH beta since greater than 95% was secreted as TSH dimer. Thus, the determinants for human TSH beta secretion and assembly are unique from the other human glycoprotein hormone beta-subunits.

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