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Originally published In Press as doi:10.1074/jbc.M209513200 on November 25, 2002

J. Biol. Chem., Vol. 278, Issue 6, 3793-3800, February 7, 2003
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Increasing Diversity of Human Thyroperoxidase Generated by Alternative Splicing
CHARACTERIZATION BY MOLECULAR CLONING OF NEW TRANSCRIPTS WITH SINGLE- AND MULTISPLICED mRNAs*

Mireille Ferrand, Valérie Le FournDagger , and Jean-Louis Franc§

From the U555 INSERM, Faculté de Médecine, Université de la Méditerranée, 27 Boulevard Jean Moulin, 13385 Marseille Cedex 5, France

The human thyroperoxidase (hTPO) gene is composed of 17 exons. The longest complete cDNA sequence determined so far contains a full-length hTPO (TPO1) encoding a 933-amino acid polypeptide. Several mRNA species encoding for hTPO isoforms are present in normal thyroid tissues, including TPO2 with exon 10 deleted and TPOzanelli with exon 16 deleted. In the present study, we established the existence of two new single-spliced transcripts, TPO4 and TPO5, lacking exons 14 and 8, respectively. Upon transfecting the TPO4 cDNA into Chinese hamster ovary cells, it was observed that TPO4 is able to reach the cell surface, is enzymatically active, and is able to be recognized by a panel of 12 monoclonal antibodies directed against hTPO, whereas TPO5 does not fold correctly and is unable to reach the cell surface. In normal tissues, the expression of TPO4 mRNA was examined by performing quantitative reverse transcription PCR. This deleted TPO mRNA amounted to 32 ± 11% of the total TPO mRNAs. In the same tissues, the TPO2, TPOzanelli, and TPO5 amounted to 35 ± 12%, 36 ± 14%, and ~10%, respectively. The sum of these four species (not including TPO1) was more than 100%, possibly due to the presence of multispliced mRNAs. This possibility was tested, and three new variants were identified: TPO2/3, lacking exons 10 and 16, TPO2/4, lacking exons 10 and 14, and an unexpected variant, TPO6, corresponding to the deletion of exons 10, 12, 13, 14, and 16. In conclusion, these results indicate the existence of five new transcripts. One of them, TPO4, codes for an enzymatically active protein, whereas TPO5 is unable to fold correctly. The functional significance of the other newly spliced mRNA variants still remains to be elucidated, but these results might help to explain the heterogeneity of the hTPO purified from the thyroid gland.

* This work was supported by INSERM (U555) and the Ligue Nationale Contre le Cancer.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY136822, AF533528, AF533530, AF533531, and AF533529.

Dagger Supported during this work by the Association pour le Développement des Recherches Médicales.

§ To whom correspondence should be addressed. Tel.: 33-4-91-32- 43-77; Fax: 33-4-91-79-65-11; E-mail: jean-louis.franc@medecine.univ-mrs.fr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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