Replacement of Serine363 and Serine375 Codons by Alanine in Rat μ-Opioid Receptor cDNA

Authors

  • Ali Omidsalary Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
  • Fatemeh Moazen Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
  • Hamid Mir Mohammad Sadeghi Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
  • Jahangir Langari Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
  • Mohammad Rabbani Department of Pharmacology and Toxcicology,Isfahan Pharmaceutical Sciences Research Centre
Abstract:

     The aim of this study was to use site directed mutagenesis technique to construct a vector in which serine363 and serine375 residues of the COOH-terminal portion of the μ-opioid receptor (MOR) were substituted by alanine. These constructs are essential in studying G-protein coupled receptor kinase-mediated MOR desensiti-zation. The nested PCR carried out for conversion of serine363 and serine375 to alanine resulted in the production of a band comparable to the expected size of 1400 bp. Restriction analysis of these bands confirmed the integrity of the PCR products. Ligation of the mutated PCR product into pcDNA3 and its digestion with appropriate restriction enzymes further confirmed the integrity of the PCR product and its orientation into the vector.

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Journal title

volume 3  issue 1

pages  13- 18

publication date 2007-01-01

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