E-selectin ligand-1 (ESL-1) is a novel adiponectin binding protein on cell adhesion
| Autor: | Nana Kuroda, Iichiro Shimomura, Ikoi Kochi, Hiroyasu Yamamoto, Akane Matsumoto, Shinji Kihara, Tohru Funahashi, Hiromi Uekita, Ryu Niinaga |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
medicine.medical_specialty animal structures Sialoglycoproteins Biophysics 030204 cardiovascular system & hematology Biochemistry Umbilical vein 03 medical and health sciences 0302 clinical medicine Cell–cell interaction Internal medicine Cell Adhesion medicine Humans Binding site Receptor Cell adhesion Molecular Biology Cells Cultured Binding Sites Cell adhesion molecule Chemistry Monocyte Endothelial Cells Hep G2 Cells Cell Biology Receptors Fibroblast Growth Factor Cell biology 030104 developmental biology Endocrinology medicine.anatomical_structure Leukocytes Mononuclear Adiponectin binding Adiponectin Cell Adhesion Molecules hormones hormone substitutes and hormone antagonists Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 470:425-430 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2016.01.023 |
| Popis: | Background Adiponectin (APN) is an adipocyte-derived bioactive molecule with anti-diabetic and anti-atherogenic properties. Although anti-diabetic effects are mostly mediated by the adiponectin receptors AdipoR1 and AdipoR2, the anti-atherogenic mechanisms have not been fully elucidated. Methods and Results In this study, we identified E-selectin ligand (ESL)-1 as a novel APN-binding protein by mass spectrometry analysis of HepG2 cell-derived immunoprecipitant with an anti-APN antibody. Cell adhesion assays using fluorescence-labelled monocyte cell line THP-1 cells and human umbilical vein endothelial cells (HUVECs) revealed that APN-pre-treated THP-1 cells had reduced binding ability to HUVECs. This APN-mediated suppressive effect on monocyte binding to endothelial cells was partially abrogated by targeting ESL-1 with shRNA in THP-1 cells. In addition, serial mutagenesis analysis disclosed that five extracellular amino acids close to the N-terminus of ESL-1 were essential for binding with APN. Conclusion Our results highlight the fact that interaction between APN and ESL-1 could provide a fundamental mechanism underlying the anti-atherogenic properties of APN. |
| Databáze: | OpenAIRE |
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