Abstract
Biopsies from human small intestine were studied in organ culture by labelling newly synthesised proteins with 35S-methionine for 6 hours continuous pulse or for 10 minutes pulse followed by chase with excess of cold methionine for different time intervals. Biopsies were further processed by immunoprecipitation with monoclonal antibodies (OKT 9) against human transferrin receptor (TR). Electrophoretic analysis of the precipitates by SDS–PAGE in normal mucosa revealed immature TR-precursor with apparent molecular weight of 87 Kd after 50 minutes of chase. At 80 minutes of chase the mature form of TR with an apparent molecular weight of 90 Kd was noted. When iodinated transferrin (125I) was incubated with microvillar membrane fraction and crosslinked with dimethyl-3-3'-dithiodispropriominidate two bands were visible on SDS-PAGE under nonreducing conditions: one representing the transferrin and the second corresponding to the transferrin-TR-complex. The organ culture of totally flat mucosa from a patient with untreated celiac disease for 6 hours continuous pulse demonstrated no TR molecule on SDS-PAGE in contrast to normal mucosa. Conclusion: TR is synthesised in human intestinal mucosa within 50 minutes in organ culture. TR is absent in acute celiac disease suggesting that this defect might play a role in the pathogenesis of iron deficiency in this condition.
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Lentze, M., Sterchi, E. & Naim, H. BIOSYNTHESIS OF TRANSFERRIN-RECEPTOR IN HUMAN SMALL INTESTINAL CELLS. Pediatr Res 20, 693 (1986). https://doi.org/10.1203/00006450-198607000-00049
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DOI: https://doi.org/10.1203/00006450-198607000-00049