Characterisation of the adiponectin receptors: The non-conserved N-terminal region of AdipoR2 prevents its expression at the cell-surface
| Autor: | Felicity J. Rose, Hayley K. Charlton, Julie Webster, Sahar Keshvari, Nicole L. Scheiber, Yu Hee Kim, Choaping Ng, Jonathan P. Whitehead, Robert G. Parton |
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| Rok vydání: | 2013 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Cell Biophysics Adipokine CHO Cells Biology Biochemistry Protein structure Cricetinae medicine Animals Humans Amino Acid Sequence Receptor Molecular Biology Peptide sequence Indirect immunofluorescence Adiponectin Chinese hamster ovary cell Cell Membrane Cell Biology Molecular biology Protein Structure Tertiary medicine.anatomical_structure Protein Multimerization Receptors Adiponectin |
| Zdroj: | Biochemical and Biophysical Research Communications. 432:28-33 |
| ISSN: | 0006-291X |
| Popis: | Adiponectin is a beneficial adipokine with insulin-sensitizing, anti-inflammatory and anti-atherogenic effects. These effects are mediated by two poorly characterised, closely related, atypical seven-transmembrane receptors. In the current report we have used C-terminal, epitope-tagged AdipoR1 and AdipoR2 constructs to monitor cell-surface expression by indirect immunofluorescence microscopy and quantitative plate-based analysis. We demonstrate that only AdipoR1 is constitutively expressed on the cell-surface. Further investigations, involving characterisation of a number of chimeric and truncated constructs, show the non-conserved region of AdipoR2 (residues 1-81) restricts its cell-surface expression. Introduction or deletion of this region, into AdipoR1 or AdipoR2, resulted in inhibition or promotion of cell-surface expression, respectively. We also confirmed that AdipoR1 and AdipoR2 can form heterodimers when co-expressed and that co-expression leads to the cell-surface expression of AdipoR2. Collectively these studies demonstrate that the non-conserved region of AdipoR2 restricts its cell-surface expression and raise the possibility that the majority of cell-surface AdipoR2 may be present in the form of heterodimers. |
| Databáze: | OpenAIRE |
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