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Inhibition of the post‐translational processing of microvillar hydrolases is associated with a specific decreased expression of sucrase‐isomaltase and an increased turnover of glucose in Caco‐2 cells treated with monensin
Author(s) -
Rousset Monique,
Trugnan Germain,
Brun Jean-Louis,
Zweibaum Alain
Publication year - 1986
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(86)81526-5
Subject(s) - monensin , chemistry , sucrase , lactic acid , biochemistry , methionine , enzyme , endocrinology , biology , amino acid , bacteria , genetics
The biosynthesis and post‐translational processing of sucrase‐isomaltase and dipeptidylpeptidase IV were studied by L‐[ 35 S]methionine labeling, immunoisolation with monoclonal antibodies and SDS‐PAGE in post‐confluent Caco‐2 cells treated with monensin (10 μM, 48 h). In addition to its classical effect on the post‐translational processing of both hydrolases, i.e. an inhibition of the conversion of the high‐mannose to the complex glycosylated form of the enzymes, monensin was found to have two other effects: a marked decrease of sucrase‐isomaltase expression, but not of dipeptidylpeptidase IV; an increased turnover of glucose, as substantiated by increased rates of glucose consumption and lactic acid production and a decreased glycogen content. Whether these two effects are related to the particular differentiation and metabolic status of Caco‐2 cells is discussed, as well as a possible role for the drug‐induced modifications of glucose turnover on the decreased expression of sucrase‐isomaltase.