The role of N53Q mutation on the rat mu-opioid receptor function.
Glycosylation of the mu-opioid receptor may play an important role on its function. Using nested PCR, N53Q mutation was prepared in the N-terminal region of the rat mu-opioid receptor cDNA and cloned into the pcDNA3 vector. The plasmids containing the wild-type and mutated receptor cDNA were transfected into the COS-7 cells. Intracellular cAMP was measured in the morphine-treated and untreated transfected cells using an ELISA kit. Plasmid expression was evaluated using X-gal staining. Intracellular concentration of cAMP in the N53Q-mutated cells was not significantly different from the wild-type. The expression of the transfected plasmids was confirmed. Therefore, based on these results, it seems that glycosylation at the N53 site of the rat mu-opioid receptor does not influence the function of this receptor significantly.
Rostami
A
A
Department of Physiology and Pharmacology, School of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran. rostami@zums.ac.ir
Rabbani
M
M
Mir-Mohammad-Sadeghi
M
M
D019943:Amino Acid Substitution / Q000235:genetics*; D000818:Animals; D001681:Biological Assay; D019556:COS Cells; D002522:Chlorocebus aethiops; D000242:Cyclic AMP / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D009020:Morphine / Q000008:administration & dosage / Q000494:pharmacology; D009154:Mutation / Q000235:genetics*; D051381:Rats; D017450:Receptors, Opioid, mu / Q000235:genetics* / Q000378:metabolism*; D013194:Staining and Labeling; D014162:Transfection
D017450:Receptors, Opioid, mu; D009020:Morphine; D000242:Cyclic AMP