ArticleImmunology2002
Signalling pathways induced by protease-activated receptors and integrins in T cells.
Article in Immunology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- Proteinase-activated receptor-2 mediates itch: a novel pathway for pruritus in human skin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Trial
- The role of protease-activated receptor 1 signaling in CD8 T cell effector functions.iScience · 2021Article
- Transcriptome Analysis and Emerging Driver Identification of CD8+ T Cells in Patients with Vitiligo.Oxidative medicine and cellular longevity · 2019Article
- Activated protein C protects from GvHD via PAR2/PAR3 signalling in regulatory T-cells.Nature communications · 2017Article
- Importance of mast cell Prss31/transmembrane tryptase/tryptase-γ in lung function and experimental chronic obstructive pulmonary disease and colitis.The Journal of biological chemistry · 2014Article
- Modulation of protease activated receptor 1 influences human metapneumovirus disease severity in a mouse model.PloS one · 2013Article
- Cytoprotective signaling by activated protein C requires protease-activated receptor-3 in podocytes.Blood · 2012Article
- Proteinases and signalling: pathophysiological and therapeutic implications via PARs and more.British journal of pharmacology · 2008Review
- A role for proteinase-activated receptor-1 in inflammatory bowel diseases.The Journal of clinical investigation · 2004Article
- Tethered ligand-derived peptides of proteinase-activated receptor 3 (PAR3) activate PAR1 and PAR2 in Jurkat T cells.Immunology · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent characterization of the thrombin receptor indicates that it plays a role in T-cell signalling pathways. However, little is known regarding the signalling events following stimulation of additional members of the protease-activated receptor (PAR) family, i.e. PAR2 and PAR3. Most of the postligand cascades are largely unknown. Here, we illustrate that in Jurkat T-leukaemic cells, activation of PAR1, PAR2 and PAR3 induce tyrosine phosphorylation of Vav1. This response was impaired in Jurkat T cells deficient in p56lck (JCaM1.6). Activation of PARs also led to an increase in tyrosine phosphorylation of ZAP-70 and SLP-76, two key proteins in T-cell receptor (TCR) signalling. We also demonstrated that p56lck is meaningful for integrin signalling. Thus, JCaM1.6 cells exhibited a marked reduction in their adherence to fibronectin-coated plates, as compared to the level of adherence of Jurkat T cells. While the phosphorylation of Vav1 in T cells is augmented following adhesion, no additional increase was noted following treatment of the adhered cells with PARs. Altogether, we have identified key components in the postligand-signalling cascade of PARs and integrins. Furthermore, we have identified Lck as a critical and possibly upstream component of PAR-induced Vav1 phosphorylation, as well as integrin activation, in Jurkat T cells.
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Registered trials
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.