Evidence map›Paper›PMID 22759073›Full record

ArticleJournal of thrombosis and haemostasis : JTH2012

Transmembrane domains are critical to the interaction between platelet glycoprotein V and glycoprotein Ib-IX complex.

X Mo, L Liu, J A López, R Li

Open access · bronzeAbstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. [Molecular dynamics simulation of force-regulated interaction between glycoprotein IbSheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2023
    Article
  4. Article
  5. Review
  6. Structure-function of platelet glycoprotein Ib-IX.Journal of thrombosis and haemostasis : JTH · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The organizing principle of the platelet glycoprotein Ib-IX-V complex.Journal of thrombosis and haemostasis : JTH · 2013
    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

4 authors at 4 institutions in 2 countries.

X MoShanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
L Liu
J A López
R Li
Emory University · USShanghai Children's Medical Center · CNThe University of Texas Health Science Center at Houston · USUniversity of Washington · US

Funding

Structure and Function of Platelet Glycoprotein lb-IX-V ComplexR01HL082808 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, RENHAO · 2006 to 2023
$6.4M
Specific Inhibition of Ectodomain Shedding of GPIb-alphaR21HL097226 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, RENHAO · 2011 to 2012
$409k
NHLBI NIH HHS HL082808NHLBI NIH HHS HL097226NHLBI NIH HHS R01 HL082808NHLBI NIH HHS R21 HL097226
6 · The paper itself

Abstract

backgroundThe glycoprotein (GP) Ib-IX-V complex, the von Willebrand factor receptor on the platelet surface, is critically involved in hemostasis and thrombosis. The GPV subunit interacts with GPIb-IX to form the GPIb-IX-V complex, but the underlying molecular basis remains unclear. It was observed earlier that efficient expression of GPV in the plasma membrane requires co-expression of GPIb-IX. OBJECTIVES AND

methodsHypothesizing that GPIb-IX stabilizes GPV through direct interaction and consequently enhances GPV surface expression, we aim in this study to identify structural elements in the complex that mediate the interaction between GPV and GPIb-IX by analyzing mutational effects on GPV surface expression in transfected Chinese hamster ovary cells.

resultsEnhancement of GPV surface expression by GPIb-IX requires transmembrane domains of both GPV and GPIbα, as replacing the GPV transmembrane domain with an unrelated poly-leucine-alanine sequence abolished the enhancing effect of GPIb-IX. Additional mutagenesis analysis of the GPV transmembrane helix identified three helical sides containing conserved polar residues as critical to efficient GPV surface expression. Similarly, replacing residues in three sides (Gly495/Ala502/Leu509, Phe491/Trp498/Val505, and Y492/L499/L506) of the GPIbα transmembrane domain with leucines preserved the surface expression level of GPIb-IX but significantly altered that of GPV.

conclusionsOur results demonstrate for the first time the importance of transmembrane domains for efficient surface expression of GPV and suggest that GPV and GPIbα transmembrane domains interact with each other, contributing to assembly of the GPIb-IX-V complex.

Indexed as

Amino Acid SequenceAnimalsCHO CellsCricetinaeCricetulusHEK293 CellsHumansMolecular Sequence DataMutagenesisPlatelet Glycoprotein GPIb-IX ComplexPlatelet Membrane GlycoproteinsProtein BindingSequence Homology, Amino AcidPlatelet Glycoprotein GPIb-IX ComplexPlatelet Membrane Glycoproteins

Identifiers

PMID22759073
PMCPMC3499136
OpenAlexW1724407454

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.