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Analysis of lactase processing in rabbit
Author(s) -
Rossi Mauro,
Maiuri Luigi,
Salvati Virginia M.,
Russomanno Concetta,
Auricchio Salvatore
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80824-e
Subject(s) - brefeldin a , colchicine , glycosylation , golgi apparatus , biochemistry , lactase , proteolysis , brush border , chemistry , trehalase , biology , microbiology and biotechnology , enzyme , vesicle , endoplasmic reticulum , membrane , genetics
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).