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Analysis of lactase processing in rabbit

FEBS letters / v.336 no.2. 1993, pp.299-303

http://dx.doi.org/10.1016/0014-5793(93)80824-E

Author : Rossi, M. ; Maiuri, L. ; Salvati, V.M. ; Russomanno, C. ; Auricchio, S.

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 [1]. 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 in the brush border fraction indicating that proteolytic events depend on intact microtubule (transport).

Keyword : Lactase . Biosynthesis . Proteolysis inhibition . Suckling . Rabbit

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