| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Institut de Recherche Interdisciplinaire en Biologie Humaine et Nucleaire (R.E., G.V., M.L.) and Service de Génétique Medicale (G.V.), Uniuersité Libre de Bruxelles Brussels, Belgium
Address all correspondence and requests for reprints to: Dr. M. Ludgate, Institut de Recherche Interdisciplinaire en Biologie Humaine et Nucleaire, Université Libre de Bruxelles, Hopital Erasme, B-1070 Brussels, Belgium.
We have investigated whether the alternatively spliced form of thyroid peroxidase (TPO), which has been shown clearly to occur in Graves thyroid, is present in normal thyroid. We have performed a polymerase chain reaction on cDNAs prepared from normal thyroid mRNAs using primers 100 bases up-stream and down-stream from the 171 nucleotides that have been shown to be spliced out. Size analysis of the polymerase chain reaction products by agarose gel electrophoresis revealed bands at 0.2 and 0.37 kilobases (kb), sizes predicted to be obtained when the two forms of TPO cDNA are present. This was confirmed by hybridization with a 32P-labeled probe corresponding to the 20 nucleotides of the junction site. After stringent washing, the 0.2-kb band gave a clear positive signal, which was stronger than that of the 0.37-kb band despite the latter cDNA being more abundant. This demonstrates clearly that the alternatively spliced form of TPO exists in normal thyroid. Its significance is discussed.
* This work was supported by grants from Ministero della Pubblica Istruzione Italia, the Wellcome Foundation, and NIH Sciences de la Vie.
Received July 16, 1990.
This article has been cited by other articles:
![]() |
J Di Cristofaro, M Silvy, A Lanteaume, M Marcy, P Carayon, and C De Micco Expression of tpo mRNA in thyroid tumors: quantitiative PCR analysis and correlation with alterations of ret, Braf , ras and pax8 genes. Endocr. Relat. Cancer, June 1, 2006; 13(2): 485 - 495. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. Le Fourn, M. Ferrand, and J.-L. Franc Endoproteolytic Cleavage of Human Thyroperoxidase: ROLE OF THE PROPEPTIDE IN THE PROTEIN FOLDING PROCESS J. Biol. Chem., February 11, 2005; 280(6): 4568 - 4577. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Ferrand, V. Le Fourn, and J.-L. Franc Increasing Diversity of Human Thyroperoxidase Generated by Alternative Splicing. CHARACTERIZATION BY MOLECULAR CLONING OF NEW TRANSCRIPTS WITH SINGLE- AND MULTISPLICED mRNAs J. Biol. Chem., January 31, 2003; 278(6): 3793 - 3800. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Niccoli, L. Fayadat, V. Panneels, J. Lanet, and J.-L. Franc Human Thyroperoxidase in Its Alternatively Spliced Form (TPO2) Is Enzymatically Inactive and Exhibits Changes in Intracellular Processing and Trafficking J. Biol. Chem., November 21, 1997; 272(47): 29487 - 29492. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Gardas, A. Lewartowska, B. J. Sutton, Z. Pasieka, A. M. McGregor, and J. P. Banga Human Thyroid Peroxidase (TPO) Isoforms, TPO-1 and TPO-2: Analysis of Protein Expression in Graves' Thyroid Tissue J. Clin. Endocrinol. Metab., November 1, 1997; 82(11): 3752 - 3757. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Endocrinology | Endocrine Reviews | J. Clin. End. & Metab. |
| Molecular Endocrinology | Recent Prog. Horm. Res. | All Endocrine Journals |