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Monoiodotyrosine formation during thyroglobulin processing in Golgi vesicles

P Bastiani1, J B Rognoni

  • 1Institut de Chimie Biologique, C.N.R.S. U.A. 202, Université de Provence, Marseille, France.

Cell Biochemistry and Function
|July 1, 1988
PubMed

A golgi-enriched subfraction was obtained from porcine thyroid glands by differential centrifugation. When incubated in a suitable medium, these vesicles were able to concentrate iodide from the medium and bind it to protein. The iodination process was inhibited by methylmercapto-imidazole and was increased by the addition of an H2O2 generating system to the medium. Analysis of the protein content of the vesicles revealed the presence of 18 and 12-13 S thyroglobulin molecules, lacking mannose residues, and containing only monoiodotyrosine. It is concluded that in vitro, iodination can begin before exocytosis, in the smooth-surfaced vesicles derived from the golgi apparatus, as soon as N-acetylglucosamine is incorporated onto the pre-thyroglobulin molecule.

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