Inhibition of N-linked glycosylation of the human type 1α metabotropic glutamate receptor by tunicamycin: effects on cell-surface receptor expression and function
| Autor: | Nimesh Mody, Stefan R. Nahorski, R. A. J. Challiss, Emmanuel Hermans |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Glycosylation
Inositol Phosphates Receptor expression Interleukin 5 receptor alpha subunit CHO Cells Biology Phosphatidylinositols Receptors Metabotropic Glutamate Transfection Interleukin 10 receptor alpha subunit Cellular and Molecular Neuroscience Estrogen-related receptor alpha chemistry.chemical_compound Cricetinae Animals Humans 5-HT5A receptor Pharmacology Tunicamycin Cell Membrane Quisqualic Acid Molecular biology Recombinant Proteins Gene Expression Regulation chemistry Retinoic acid receptor alpha Interleukin-21 receptor Lithium Chloride |
| Zdroj: | Neuropharmacology. 38:1485-1492 |
| ISSN: | 0028-3908 |
| DOI: | 10.1016/s0028-3908(99)00099-4 |
| Popis: | The potential role of N-linked glycosylation of the human type 1 alpha metabotropic glutamate (mGlu1 alpha) receptor was studied in a recombinant, inducible expression system, where receptor expression was induced in the absence and presence of tunicamycin. In the absence of tunicamycin the mGlu1 alpha receptor appeared to be expressed, at least in part, as a dimer consisting of monomers of approx. 145 and 160 KDa relative molecular mass (M-r). In the presence of tunicamycin only a single monomeric protein could be detected approximating the M-r predicted for the human mGlu1 alpha receptor based on its primary amino acid sequence (130 KDa). Exposure to tunicamycin during receptor induction did not appear to affect the cell surface expression of the mGlu1 alpha receptor as determined immunocytochemically or using a cell-surface biotinylation strategy, but reduced agonist-stimulated phosphoinositide hydrolysis by approximately 50% compared to control cell populations. Our data suggest that non-N-glycosylated human mGlu1 alpha receptors can traffic to the cell surface and activate phospholipase C. (C) 1999 Elsevier Science Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
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