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

FEBS Letters

Brun, Jean-Louis¹  Trugnan, Germain¹  Zweibaum, Alain¹  Rousset, Monique¹ 

[1] Unité de Recherches sur le Métabolisme et la Différenciation de Cellules en Culture, INSERM U178, 16 avenue Paul Vaillant-Couturier, 94807 Villejuif Cedex, France

关键词: Monensin Microvillar hydrolase Protein glycosylation Glucose consumption Glycolysis Glycogen (Caco-2 cell);   

DOI  :  10.1016/0014-5793(86)81526-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The biosynthesis and post-translational processing of sucrase-isomaltase and dipeptidylpeptidase IV were studied by L-[³⁵S]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.

【 授权许可】

Unknown