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Analysis of lactase processing in rabbit.

M Rossi·L Maiuri·V M Salvati·C Russomanno·S Auricchio
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Abstract

The proteolytic processing of rabbit intestinal lactase-phlorizin-hydrolase (LPH) was studied by pulse-chase and continuous labeling experiments in organ culture from 15-day-old rabbits in the presence of glycosylation and processing inhibitors. Monensin and brefeldin A inhibited the two proteolytic cleavages of the precursor indicating that they are post-Golgi events as previously reported for the unique cleavage of LPH in man. The inhibition was not related to a concomitant alteration glycosylation; in fact, if trimming was blocked by MDNM the abnormal glycosylated precursor was proteolytically processed normally. Finally the use of the anti-microtubular drug colchicine strongly inhibited both cleavages and caused accumulation of the complex-glycosylated precursor form the brush border fraction indicating that proteolytic events depend on intact microtubule (transport).

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AnimalsBrefeldin ACell FractionationColchicineCyclopentanesEnzyme PrecursorsGlycosylationGolgi ApparatusHydrolysisLactase-Phlorizin HydrolaseMicrovilliMonensinOrgan Culture TechniquesProtein Processing, Post-TranslationalRabbitsJournal Article

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M Rossi, L Maiuri, V M Salvati, C Russomanno, S Auricchio. 1993-12-27. Analysis of lactase processing in rabbit.. https://doi.org/10.1016/0014-5793(93)80824-e

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