title: Ascidian homologs of mammalian thyroid peroxidase genes are expressed in the thyroid-equivalent region of the endostyle.
abstract: The endostyle is a pharyngeal organ for the internal filter feeding of urochordates, cephalochordates, and larval lamprey. This organ is also considered to be homologous to the follicular thyroid gland of higher vertebrates. Thyroglobulin (Tg) and thyroid peroxidase (TPO) are specifically expressed in the thyroid gland of higher vertebrates, and they play an important role in iodine metabolism for the synthesis of thyroid hormones. Previous histochemical observations showed that iodine-concentrating and peroxidase activities were detected in zones 7, 8, and 9 of the ascidian endostyle, suggesting that these zones contains cells that are equivalent to those in the vertebrate follicular thyroid. In order to investigate the molecular developmental mechanisms involved in the formation and function of the endostyle, with special reference to the evolution of the thyroid gland, in the present study, we isolated and characterized cDNA clones for TPO genes, CiTPO from Ciona intestinalis and HrTPO from Halocynthia roretzi. Northern blot and in situ hybridization analyses revealed that the expression of the ascidian TPO genes was restricted to zone 7, one of the elements equivalent to the thyroid. These results provide the first evidence at the gene expression level for shared function between a part of the ascidian endostyle and the vertebrate follicular thyroid gland. J. Exp. Zool. ( Mol. Dev. Evol. ) 285:158-169, 1999.
authors.affiliation: Department of Zoology, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan. ogasawara@ascidian.zool.kyoto-u.ac.jp
authors.forename: M
authors.initials: M
authors.lastname: Ogasawara
authors.forename: R
authors.initials: R
authors.lastname: Di Lauro
authors.forename: N
authors.initials: N
authors.lastname: Satoh
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002938:Ciona intestinalis / Q000033:anatomy & histology / Q000201:enzymology / Q000235:genetics; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004330:Drosophila / Q000201:enzymology; D006801:Humans; D007453:Iodide Peroxidase / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D008322:Mammals; D051379:Mice; D008969:Molecular Sequence Data; D009928:Organ Specificity; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D012617:Sea Urchins / Q000201:enzymology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013954:Thyroglobulin / Q000032:analysis / Q000235:genetics; D013961:Thyroid Gland / Q000201:enzymology*; D014561:Urochordata / Q000033:anatomy & histology / Q000201:enzymology / Q000235:genetics*
chemical_list: D018076:DNA, Complementary; D011994:Recombinant Proteins; D013954:Thyroglobulin; D007453:Iodide Peroxidase