Evidence map›Paper›PMID 21864297›Full record

ArticleThe Biochemical journal2012

A common single nucleotide polymorphism A118G of the μ opioid receptor alters its N-glycosylation and protein stability.

Peng Huang, Chongguang Chen, Stephen D Mague, Julie A Blendy, Lee-Yuan Liu-Chen

Abstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 3 pooled it
4.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 3 syntheses or guidelines pooled it, 113 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Trial
  5. Trial
  6. Article
  7. Do Diabetes and Genetic Polymorphisms in theJournal of clinical medicine · 2025
    Article
  8. Review
  9. Frontiers in pharmacology · 2025
    Article
  10. Article
  11. Neural Network Connectivity Following Opioid Dependence is Altered by a Common Genetic Variant in the µ-Opioid Receptor,The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  12. Review
  13. Article
  14. Review
  15. Translational Research in Nicotine Addiction.Cold Spring Harbor perspectives in medicine · 2021
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Peng HuangDepartment of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Chongguang Chen
Stephen D Mague
Julie A Blendy
Lee-Yuan Liu-Chen
Temple University · USUniversity of Pennsylvania · US

Funding

Pilot Projects Core (PPC)P30DA013429 · NIDA · TEMPLE UNIV OF THE COMMONWEALTH · PI Anjali M Rajadhyaksha · 2000 to 2026
$34.6M
Cellular Pharmacology of Kappa Opioid ReceptorR01DA017302 · NIDA · TEMPLE UNIV OF THE COMMONWEALTH · PI LIU-CHEN, LEE-YUAN · 2004 to 2013
$3.1M
Functional Characterization of OPRM1 A118G in Nicotine DependenceR21DA027066 · NIDA · UNIVERSITY OF PENNSYLVANIA · PI BLENDY, JULIE A, LERMAN, CARYN · 2009 to 2010
$1.0M
NIDA NIH HHS DA027066NIDA NIH HHS DA17302NIDA NIH HHS P30 DA013429NIDA NIH HHS P30 DA13429NIDA NIH HHS R01 DA017302NIDA NIH HHS R21 DA027066
6 · The paper itself

Abstract

The A118G SNP (single nucleotide polymorphism) of the hMOPR [human MOPR (μ opioid receptor)] gene OPRM1 results in an amino acid substitution (N40D). Subjects homozygous for the 118G allele have been reported to require higher morphine doses to achieve adequate analgesia, and the 118G allele is more prevalent among drug abusers. However, changes in the MOPR protein associated with this SNP are unknown. Using a knockin mouse model (G/G mice; mice homozygous for the 112G allele of MOPR) that possesses the equivalent nucleotide/amino acid substitution (A112G; N38D) of the A118G SNP in the hMOPR gene, we investigated the N-linked glycosylation status of thalamic and striatal MOPR in G/G mice compared with A/A mice (wild-type mice homozygous for the 112A allele of MOPR). The molecular mass of MOPR determined by immunoblotting was lower in G/G mice than in A/A mice. Following treatment with peptide N-glycosidase F, which removes all N-linked glycans, both MOPR variants had an identical molecular mass, indicating that this discrepancy was due to a lower level of N-glycosylation of the MOPR in G/G mice. In Chinese-hamster ovary cells stably expressing hMOPRs, 118G/Asp40-hMOPR had a lower molecular mass than 118A/Asn40-hMOPR, which was similarly due to differential N-glycosylation. Pulse-chase studies revealed that the half-life of the mature form of 118G/Asp40-hMOPR (~12 h) was shorter than that of 118A/Asn40-hMOPR (~28 h). Thus the A118G SNP reduces MOPR N-glycosylation and protein stability.

Indexed as

Polymorphism, Single NucleotideAmino Acid SequenceAnimalsCHO CellsCricetinaeGene Expression RegulationGlycosylationHumansMiceMice, KnockoutProtein StabilityReceptors, Opioid, muOPRM1 protein, humanOprm protein, mouseReceptors, Opioid, mu

Identifiers

PMID21864297
PMCPMC3923516
OpenAlexW1989254187

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.