Evidence map›Paper›PMID 20926384›Full record

ArticleThe Journal of biological chemistry2010

Adenosine A2A receptor is involved in cell surface expression of A2B receptor.

Kengo Moriyama, Michail V Sitkovsky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.4field-weighted citation impact, top 14% 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

45 citing papers in PubMed, 68 citations in OpenAlex.

  1. Trial
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  8. AJournal for immunotherapy of cancer · 2022
    Article
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  17. Role of Cardiac AFrontiers in pharmacology · 2020
    Review
  18. Expression of Adenosine Receptors in Rodent Pancreas.International journal of molecular sciences · 2019
    Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Kengo MoriyamaNew England Inflammation and Tissue Protection Institute, Department of Pharmaceutical Science, Northeastern University, Boston, Massachusetts 02115, USA.
Michail V Sitkovsky
Northeastern University · US

Funding

Cancer Immunotherapy by Targeting A2 Adenosine ReceptorR01CA111985 · NCI · NORTHEASTERN UNIVERSITY · PI SITKOVSKY, MICHAIL · 2006 to 2016
$2.7M
Mechanisms of Tumor Protection for T Cells by HypoxiaR01CA112561 · NCI · NORTHEASTERN UNIVERSITY · PI SITKOVSKY, MICHAIL · 2005 to 2009
$1.5M
NCI NIH HHS R01 CA111985NCI NIH HHS R01 CA112561
6 · The paper itself

Abstract

The A2A and A2B adenosine receptors (A2AR and A2BR) are implicated in many physiological processes. However, the mechanisms of their intracellular maturation and trafficking are poorly understood. In comparative studies of A2AR versus A2BR expression in transfected cells, we noticed that the levels of cell surface expression of A2BR were significantly lower than those of A2AR. A large portion of the A2BR was degraded by the proteasome. Studies of cell surface expression of A2BR chimeric molecules in transfectants suggested that A2BR does not have the dominant forward transport signal for export from the endoplasmic reticulum to the cell surface. A2BR surface expression was increased in A2BR chimeras where the A2BR carboxyl terminus (CT) was replaced or fused with the A2AR CT. Co-transfection of A2AR with A2BR enhanced surface expression of A2BR though the F(X)(6)LL motif in the A2AR CT. The requirements of A2AR expression for better A2BR cell surface expression was not only established in transfectants but also confirmed by observations of much lower levels of A2BR-induced intracellular cAMP accumulation in response to A2BR-activating ligand in splenocytes from A2AR(-/-) mice than in wild type mice. The results of mechanistic studies suggested that poor A2BR expression at the cell surface might be accounted for mainly by the lack of a dominant forward transport signal from the endoplasmic reticulum to the plasma membrane; it is likely that A2BR forms a hetero-oligomer complex for better function.

Indexed as

Gene Expression RegulationAnimalsBiological TransportCell MembraneEndoplasmic ReticulumHumansMiceMice, Inbred C57BLMice, TransgenicProteasome Endopeptidase ComplexProtein Structure, TertiaryReceptor, Adenosine A2AReceptor, Adenosine A2BSignal TransductionProteasome Endopeptidase ComplexReceptor, Adenosine A2AReceptor, Adenosine A2B

Identifiers

PMID20926384
PMCPMC2998132
OpenAlexW2008884889

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.