H. Sano, T. Higashi, Y. Jinnouchi, R. Nagai, Kenshi Matsumoto, Zhuo Qin, K. Ikeda, Y. Ebina, H. Makino, S. Horiuchi
{"title":"Insulin Accelerates the Endocytic Uptake and Degradation of Advanced Glycation End-Products Mediated by The Macrophage Scavenger Receptor","authors":"H. Sano, T. Higashi, Y. Jinnouchi, R. Nagai, Kenshi Matsumoto, Zhuo Qin, K. Ikeda, Y. Ebina, H. Makino, S. Horiuchi","doi":"10.1533/9781845698447.7.386","DOIUrl":null,"url":null,"abstract":"Summary The macrophage scavenger receptor (MSR), one of the receptors for advanced glycation end-products (AGEs), mediates endocytic uptake and degradation of AGE-proteins in several cell types. In the present study, we examined whether MSR function was regulated by insulin signaling. Co-expression of human insulin receptor (IR) with MSR in Chinese hamster ovary (CHO) cells showed that insulin accelerated the degradation of AGE proteins to 160% of the control. The insulin-enhanced endocytic uptake of AGE-proteins was significantly inhibited by phosphatidylinositol-3-OH kinase (PI(3)K) inhibitors, wortmannin and LY294002. Thus, insulin signaling through the PI(3)K pathway may regulate MSR-mediated endocytic uptake of AGE-proteins.","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"22 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Maillard Reaction in Foods and Medicine","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1533/9781845698447.7.386","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Summary The macrophage scavenger receptor (MSR), one of the receptors for advanced glycation end-products (AGEs), mediates endocytic uptake and degradation of AGE-proteins in several cell types. In the present study, we examined whether MSR function was regulated by insulin signaling. Co-expression of human insulin receptor (IR) with MSR in Chinese hamster ovary (CHO) cells showed that insulin accelerated the degradation of AGE proteins to 160% of the control. The insulin-enhanced endocytic uptake of AGE-proteins was significantly inhibited by phosphatidylinositol-3-OH kinase (PI(3)K) inhibitors, wortmannin and LY294002. Thus, insulin signaling through the PI(3)K pathway may regulate MSR-mediated endocytic uptake of AGE-proteins.