Evidence map›Paper›PMID 10789830›Full record

ArticleCellular and molecular neurobiology2000

Functional coupling of G proteins to endothelin receptors is ligand and receptor subtype specific.

Z Shraga-Levine, M Sokolovsky

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular neurobiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 47 citations in OpenAlex.

  1. Endothelin-1 drives COX-2 and prostaglandin EJournal of dental sciences · 2026
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  11. Endothelin receptors and pain.The journal of pain · 2009
    Review
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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.

Z Shraga-LevineDepartment of Neurobiochemistry, Tel Aviv University, Israel.
M Sokolovsky
Tel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. The aims of the present study were (a) to determine the identity of the G proteins with which the endothelin receptor interacts and whether this interaction is subtype specific and (b) to determine whether agonist exposure can result in specific coupling between the endothelin receptor and G proteins. 2. Coupling between endothelin A (ET(A)) or endothelin B (ET(B)) receptors and G proteins was assessed in two fibroblast cell lines, each expressing one receptor subtype. Four ligands, ET-1, ET-3, SRTXb, and SRTXc, were used for receptor stimulation. The G protein alpha-subunit coupled to the receptor was identified by immunoprecipitation with an antibody against the endothelin receptor and immunoblotting with specific antibodies against different G protein alpha-subunits. 3. Unstimulated ET(A) and ET(B) receptors (ET(A)R and ET(B)R, respectively) were barely coupled to Go(alpha). The unstimulated ET(A)R coimmunoprecipitated with Gi3alpha, whereas the unstimulated ETBR was much less strongly coupled to Gi3alpha. The coupling of ETBR to Gi1Gi2 alpha-subunits was much stronger than the coupling of ET(A)R to these alpha-subunits. Stimulation with the different ET agonists also resulted in differential coupling of G proteins to the receptor subtypes. All four ligands caused a strong increase in coupling of the ET(B)R to Gi3alpha, whereas coupling of the ET(A)R to this subunit was not affected by ET-1 and was even decreased by SRTXc. On the other hand, all four ligands caused a much greater increase in the coupling of ET(A)R to G(q)alpha/G11alpha than in the coupling of ET(B)R to these alpha-subunits. Ligand-induced coupling between the receptors and the Gi1 and Gi2 alpha-subunits is similar for the two receptor subtypes. The same was true for ligand-induced coupling of the receptors to Go(alpha), except that ET-3 increased the coupling of this alpha-subunit to ET(B)R and decreased the coupling to ET(A)R. Taken together, the results of this study show that coupling between ET receptors and G proteins is ligand and receptor subtype specific. 4. It remains to be established whether this diversity of receptor-G protein coupling is of relevance for the various endothelin signaling pathways and/or pathological states.

Indexed as

AnimalsBlotting, WesternCells, CulturedCricetinaeCricetulusEndothelin-1Endothelin-3FibroblastsGTP-Binding Protein alpha Subunit, Gi2GTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsLigandsLungPeptidesEndothelin-1Endothelin-3GTP-Binding Protein alpha Subunit, Gi2GTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsLigandsPeptidesProto-Oncogene ProteinsReceptor, Endothelin AReceptor, Endothelin BReceptors, Endothelinsarafotoxin-csarafotoxins s6Vasoconstrictor AgentsViper Venoms

Identifiers

PMID10789830
PMCPMC11537521
OpenAlexW1553847697

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.