Evidence map›Paper›PMID 24106270›Full record

ArticleThe Journal of biological chemistry2013

RhoG protein regulates platelet granule secretion and thrombus formation in mice.

Robert Goggs, Matthew T Harper, Robert J Pope, Joshua S Savage, Christopher M Williams, Stuart J Mundell, Kate J Heesom, Mark Bass, Harry Mellor, Alastair W Poole

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

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  10. Frontiers in cellular and infection microbiology · 2020
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  18. Receptor-interacting protein kinase 3 promotes platelet activation and thrombosis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
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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

10 authors at 1 institution in 1 country.

Robert GoggsSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom.
Matthew T HarperSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom.
Robert J PopeSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom.
Joshua S SavageSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom.
Christopher M WilliamsSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom.
Stuart J MundellSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom.
Kate J HeesomProteomics Facility, University of Bristol, Bristol BS8 1TD, United Kingdom.
Mark BassSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Harry MellorSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Alastair W PooleSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom. Electronic address: a.poole@bris.ac.uk.
University of Bristol · GB

Funding

British Heart Foundation PG/11/68/29074British Heart Foundation RG/05/083British Heart Foundation RG/10/006/28299Medical Research Council G1000432Wellcome TrustWellcome Trust WT090093MA
6 · The paper itself

Abstract

Rho GTPases such as Rac, RhoA, and Cdc42 are vital for normal platelet function, but the role of RhoG in platelets has not been studied. In other cells, RhoG orchestrates processes integral to platelet function, including actin cytoskeletal rearrangement and membrane trafficking. We therefore hypothesized that RhoG would play a critical role in platelets. Here, we show that RhoG is expressed in human and mouse platelets and is activated by both collagen-related peptide (CRP) and thrombin stimulation. We used RhoG(-/-) mice to study the function of RhoG in platelets. Integrin activation and aggregation were reduced in RhoG(-/-) platelets stimulated by CRP, but responses to thrombin were normal. The central defect in RhoG(-/-) platelets was reduced secretion from α-granules, dense granules, and lysosomes following CRP stimulation. The integrin activation and aggregation defects could be rescued by ADP co-stimulation, indicating that they are a consequence of diminished dense granule secretion. Defective dense granule secretion in RhoG(-/-) platelets limited recruitment of additional platelets to growing thrombi in flowing blood in vitro and translated into reduced thrombus formation in vivo. Interestingly, tail bleeding times were normal in RhoG(-/-) mice, suggesting that the functions of RhoG in platelets are particularly relevant to thrombotic disorders.

Indexed as

Blood CoagulationAdenosine DiphosphateAnimalsBlood PlateletsCarrier ProteinsFemaleGTP PhosphohydrolasesHemostaticsHumansMaleMiceMice, KnockoutPeptidesPlatelet Activationrho GTP-Binding ProteinsSecretory VesiclesAdenosine DiphosphateCarrier Proteinscollagen-related peptideGTP PhosphohydrolasesHemostaticsPeptidesRhog protein, mouserho GTP-Binding ProteinsThrombinPlateletsProteomicsRho GTPasesSecretionThrombosisTransgenic Mice

Identifiers

PMID24106270
PMCPMC3837162
OpenAlexW2068160415

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.