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J. Biol. Chem., Vol. 264, Issue 9, 4762-4765, Mar, 1989
F Tietze, LD Kohn, AD Kohn, I Bernardini, HC Andersson, MD Adamson, GS Harper and WA Gahl
Monoiodotyrosine (MIT) crosses the lysosomal membrane of rat FRTL-5 thyroid
cells by a carrier-mediated process. In egress studies, MIT lost from
inside lysosomes was quantitatively recovered outside lysosomes as MIT,
indicating that the compound was transported intact across the lysosomal
membrane. In uptake studies, [125I]MIT entry required intact lysosomes and
exhibited saturation kinetics. The apparent Km for MIT was approximately
1.5 microM and the Vmax was approximately 0.24 pmol/unit
hexosaminidase/min. Countertransport of MIT was demonstrated, with an
initial velocity of [125I]MIT uptake which reached a maximum at high
intralysosomal MIT loading. Nonradioactive MIT and diiodotyrosine competed
to approximately equivalent extents with [125I]MIT for uptake in
countertransport experiments. The existence of a lysosomal MIT carrier in
thyroid cells may explain how this product of thyroglobulin catabolism is
transported to the cytosol for iodine salvage and reutilization.
Carrier-mediated transport of monoiodotyrosine out of thyroid cell lysosomes
Laboratory of Molecular and Cell Biology, National Institute of Diabetes and Digestive and Kidney Disease, Bethesda, Maryland 20892.
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