Identification of a minor Tg mRNA transcript in RNA from normal and goitrous thyroids

@article{Targovnik1992IdentificationOA,
  title={Identification of a minor Tg mRNA transcript in RNA from normal and goitrous thyroids},
  author={H{\'e}ctor Manuel Targovnik and Pascale Cochaux and Daniel Corach and Gilbert Vassart},
  journal={Molecular and Cellular Endocrinology},
  year={1992},
  volume={84},
  pages={R23-R26}
}
A 138-nucleotide deletion in the thyroglobulin ribonucleic acid messenger in a congenital goiter with defective thyroglobulin synthesis.
TLDR
Two siblings with congenital goitrous hypothyroidism were investigated in terms of clinical, biochemical, and molecular biology and it is conceivable that the excision of this segment of the Tg molecule could affect the protein structure, resulting in its premature degradation, very low colloid storage, and diminished thyroid hormone production rate.
Identification of a new thyroglobulin variant: a guanine-to-adenine transition resulting in the substitution of arginine 2510 by glutamine.
TLDR
Thyroglobulin (Tg) reverse transcription polymerase chain reaction (RT-PCR) products from three congenital goiters and three normal thyroid tissues by Taq I digestion established that the glutamine allele is present in normal unrelated individuals, with an allelic frequency of 62%.
Nonsense-Associated Alternative Splicing of the Human Thyroglobulin Gene
TLDR
The hypothesis that the alternative splicing of the mutated exon is driven by the interruption of the reading frame is supported, suggesting that the 4588C>T mutation does not interfere with exon 22 definition and processing in vitro.
A premature stopcodon in thyroglobulin messenger RNA results in familial goiter and moderate hypothyroidism.
TLDR
Clinically, hypothyroidism was not severe in the affected siblings because the truncated Tg glycoprotein was still capable of thyroid hormonogenesis, and the homozygous nonsense mutation cosegregated with the clinical phenotype.
Molecular advances in thyroglobulin disorders.
  • C. Rivolta, H. Targovnik
  • Biology, Medicine
    Clinica chimica acta; international journal of clinical chemistry
  • 2006
New insights in the human thyroglobulin structure
TLDR
All reportedd TG mutations causing dyshormonogenesi s in man and animal are designate dd in the nucleotide and amino acid sequences.
Evidence for the segregation of three different mutated alleles of the thyroglobulin gene in a Brazilian family with congenital goiter and hypothyroidism.
TLDR
A Brazilian family with congenital goiter, hypothyroidism, and marked impairment of thyroglobulin (Tg) synthesis is reported, and it is found that two additional mutations of the Tg gene must segregate in this family to account for the observed phenotypes.
Genomic organization of the 3' region of the human thyroglobulin gene.
TLDR
The genomic organization of the 3' end of the human Thyroglobulin (Tg) gene has not previously been characterized, and it is found that the splicing sequences diverged considerably from the3' and 5' consensus.
Genomic organization of the human thyroglobulin gene: the complete intron-exon structure.
TLDR
The present study shows that the five phages isolated and the amplified fragment include 59.4 kb genomic DNA, covering 1446 nucleotides of exonic sequence distributed over 12 exons, from exon 24 to exon 35 of the thyroglobulin gene.
...
...

References

SHOWING 1-10 OF 11 REFERENCES
Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA.
TLDR
The mRNA encoding human thyroglobulin has been cloned and sequenced and shows an interesting homology with the acetylcholinesterase of Torpedo californica.
Epitope mapping of human thyroglobulin. Heterogeneous recognition by thyroid pathologic sera.
TLDR
Findings show that some autoepitopes overlap accurately with some heteroepitope characterized by a polyclonal immune serum directed against the mature protein.
Structure‐function relationship in thyroglobulin: amino acid sequence of two different thyroxine‐containing peptides from porcine thyroglobulin.
From the cyanogen bromide (CNBr) treatment of porcine thyroglobulin a peptide of mol. wt. 15 000, CNBr‐b1, was purified by gel filtration and ion‐exchange chromatography. CNBr‐b1 contained 50% of the
...
...