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Isfahan University of Medical Sciences
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| Document Type
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Latin Dissertation
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| Language of Document
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English
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| Record Number
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102613
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| Doc. No
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T10088
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| Call number
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QU,55,R839r,2005
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| Main Entry
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Rostami Shokravi, Ali
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| Title & Author
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The role of glycosylation consensus on the function of M[ u] opioid receptor Ali Rostami Shokravi
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| College
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Schools, Pharmacy
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| Date
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, 2005
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| Degree
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Pharmacology, Ph.D
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| Page No
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XII, 132 p.: ill ( som col ), tab
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| Note
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This Thesis is also a reasearch project with project ID: 83228
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علی رستمی شکروی
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Original Work
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| Abstract
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ntroduction: p-opioid receptor plays an important role in mediating most of the diverse effects of opioids like analgesia, euphoria and dependence. It seems that "glycosylation consensus" has important role in the receptor and also, other cell surface receptors. In this study we try to mutate in two potential glycosylation sites and their role in the iu-opioid receptor function. Materials and methods: Two appropriate primers were designed and using nested PCR two mutations were prepared in the N-terminal region of the receptor cDNA as N46Q and N53Q. The PCR products were sequenced. The products and also, rat p-opioid receptor-containing pcDNA3 was digested using Hindlil and BamHI restriction enzymes. The desired segments were ligated and transformed in E.coli HB101 using heat shock method. The plasmids prepared from the transformed colonies were digested using HindlIl and XbaI restriction enzymes evaluating presence of desired segments. The wild vector and also, the recombinant-containing plasmids prepared in large amounts using midi preparation and the plasmids were transfected into the COS-7 cells. Intracellular cAMP was measured in the morphine-treated and untreated transfected cells using ELISA kit. Plasmid transfection was evaluated using X-gal staining.Results: Sequencing of the PCR products revealed the insertion of the desired substitutions in the exact positions. In restriction enzyme evaluation, presence of the only N53Q mutation was shown. Intracellular concentration of cAMP in the N53Q mutated cells was not significantly different from the wild-type. The transfection of the transfected plasmids was confirmed.Discussion and conclusion: Inhibition of the glycosylation at 53 site of the rat ju-opioid receptor had no significant impression on the function of the receptor. Key words: glycosylation, p-opioid receptor, mutation, cAMP.
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| Descriptor
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1. Receptors, Opioid, mu
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Polymerase Chain Reaction
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Glycosylation
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Mutation
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Analgesics, Opioid
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| Added Entry
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Rabbani, Mohammad, Supervisor
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Mir Mohammad sadeghi, Hamid, Supervisor
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Hajhashemi, Valiollah, Supervisor
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Jafarian- Dehkordi, Abass, Supervisor
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| Translated Title Supplied by Cataloguer
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بررسی نقش glycosylation consensus در عملکرد گیرندههای اپیوئیدی مو
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http://elib.mui.ac.ir/site/catalogue/102613
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