期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 40, 页码 35061-35070出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.261073
关键词
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资金
- National Institutes of Health, NIAMS [AR048120]
- AstraZeneca, Inc.
Receptor for advanced glycation end products (RAGE), an immunoglobin superfamily cell surface receptor, contributes to the vascular pathology associated with multiple disorders, including Alzheimer disease (AD), diabetic complications, and inflammatory conditions. However, the underlying mechanisms remain largely unclear. Here, using the human umbilical vein endothelial cell line (ECV-304) expressing human RAGE, we report that RAGE expression leads to an altered F-actin organization and impaired membrane resealing. To investigate the underlying mechanisms, we showed that RAGE expression increases beta-catenin level, which decreases F-actin stress fibers and attenuates plasma membrane resealing. These results thus suggest a negative function for RAGE in endothelial cell membrane repair and reveal a new mechanism underlying RAGE regulation of F-actin remodeling and membrane resealing.
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