ArticleBritish journal of pharmacology2001
Evidence for functionally active protease-activated receptor-4 (PAR-4) in human vascular smooth muscle cells.
Article in British journal of pharmacology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 56 citations in OpenAlex.
- PAR4 overexpression promotes colorectal cancer cell proliferation and migration.Oncology letters · 2018Article
- Thrombin-Induced Podocyte Injury Is Protease-Activated Receptor Dependent.Journal of the American Society of Nephrology : JASN · 2017Article
- Multiple Signaling Pathways Contribute to the Thrombin-induced Secretory Phenotype in Vascular Smooth Muscle Cells.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2015Article
- Review
- New insights into protease-activated receptor 4 signaling pathways in the pathogenesis of inflammation and neuropathic pain: a literature review.Channels (Austin, Tex.) · 2015Review
- Thrombin-inhibiting perfluorocarbon nanoparticles provide a novel strategy for the treatment and magnetic resonance imaging of acute thrombosis.Journal of thrombosis and haemostasis : JTH · 2011Article
- Activation of protease-activated receptors 3 and 4 accelerates tissue factor-induced thrombin generation on the surface of vascular smooth muscle cells.Arteriosclerosis, thrombosis, and vascular biology · 2010Article
- Proteinases and signalling: pathophysiological and therapeutic implications via PARs and more.British journal of pharmacology · 2008Review
- Protease-activated receptor-4: a novel mechanism of inflammatory pain modulation.British journal of pharmacology · 2007Article
- Evidence for the presence of functional protease activated receptor 4 (PAR4) in the rat colon.Gut · 2004Article
- Expression of protease-activated receptor-1, -2, -3, and -4 in control and experimentally inflamed mouse bladder.The American journal of pathology · 2003Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. This study investigates, whether in addition to the protease-activated receptor-1 (PAR-1), PAR-4 is present in vascular smooth muscle cells (SMC) of the human saphenous vein and whether this receptor is functionally active. PAR-1 and PAR-4 are stimulated by thrombin and by the synthetic peptides SFLLRN and GYPGQV, respectively. 2. mRNAs for both, PAR-1 and PAR-4, were detected in the SMC by using reverse transcriptase polymerase chain reaction (RT - PCR). 3. Treatment of the SMC with GYPGQV (200 microM) resulted in a transient increase in free intracellular calcium. This calcium signal was completely abolished after a preceding challenge with thrombin (10 nM), indicating homologous receptor desensitization. 4. Stimulation of the SMC with 10 nM thrombin or 200 microM SFLLRN caused a time-dependent activation of the extracellular signal-regulated kinases-1/2 (ERK-1/2) with a maximum at 5 min. In contrast, 100 nM thrombin as well as 200 microM of GYPGQV induced a prolonged phosphorylation of ERK-1/2 with a maximum at 60 min. These data suggest that PAR-1 and PAR-4 are activated by thrombin at distinct concentrations and with distinct kinetics. 5. GYPGQV stimulated [(3)H]-thymidine incorporation in SMC. At 500 microM, the peptide increased DNA synthesis 2.5 fold above controls. A comparable mitogenic effect was obtained after stimulation of the SMC by 10 nM thrombin or 100 microM SFLLRN, respectively. 6. These data indicate that a functionally active PAR-4 is present in SMC and, in addition to PAR-1, might contribute to thrombin-induced mitogenesis.
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