Novel subcellular fractionation procedures and pulse-chase techniques were used to study the intracellular transport of the microvillar membrane hydrolases sucrase-isomaltase and dipeptidylpeptidase IV in the differentiated colon adenocarcinoma cell line Caco-2. The overall rate of transport to the cell surface was two fold faster for dipeptidylpeptidase IV than for sucrase-isomaltase, while no significant differences were observed in transport rates from the site of complex glycosylation to the brush border. The delayed arrival of sucrase-isomaltase in the compartment where complex glycosylation occurs was only in part due to exit from the endoplasmic reticulum. A major slow-down could be ascribed to maturation in and transit of this enzyme through the Golgi apparatus. These results suggest that the observed asynchronism is due to more than one rate-limiting step along the rough endoplasmic reticulum to trans-Golgi pathway.
Dissection of the asynchronous transport of intestinal microvillar hydrolases to the cell surface.
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B Stieger, K Matter, B Baur, K Bucher, M Höchli, H P Hauri; Dissection of the asynchronous transport of intestinal microvillar hydrolases to the cell surface.. J Cell Biol 1 June 1988; 106 (6): 1853–1861. doi: https://doi.org/10.1083/jcb.106.6.1853
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