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Strukova, S. M.

doi:10.1023/a:1002869310180

Cited by 79 publications

(31 citation statements)

References 104 publications

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“…The generation of excessive thrombin leads to thrombosis, which is the major cause of morbidity and mortality. Thrombin in close proximity to the active mediators also plays a role in the diverse cellular responses in the vascular and avascular tissues (49). It has been reported that thrombin potentiates both interferon-␥ and tumor necrosis factor-␣-induced NO production in C6 glioma cells (50).…”

Section: Discussionmentioning

confidence: 99%

Thrombin Induces Nitric-oxide Synthase via Gα12/13-coupled Protein Kinase C-dependent I-κBα Phosphorylation and JNK-mediated I-κBα Degradation

Kang

Choi

Cho

et al. 2003

Journal of Biological Chemistry

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An imbalance between thrombin and antithrombin III contributed to vascular hyporeactivity in sepsis, which can be attributed to excess NO production by inducible nitricoxide synthase (iNOS). In view of the importance of the thrombin-activated coagulation pathway and excess NO as the culminating factors in vascular hyporeactivity, this study investigated the effects of thrombin on the induction of iNOS and NO production in macrophages. Thrombin induced iNOS protein in the Raw264.

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Section: Discussionmentioning

confidence: 99%

Thrombin Induces Nitric-oxide Synthase via Gα12/13-coupled Protein Kinase C-dependent I-κBα Phosphorylation and JNK-mediated I-κBα Degradation

Kang

Choi

Cho

et al. 2003

Journal of Biological Chemistry

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“…Within the coagulation cascade, thrombin is a serine protease that also induces the activation of platelets [27]. The activation of the extrinsic coagulation pathway resulting in thrombin generation might thus support a role of platelets in CU pathophysiology.…”

Section: Pathophysiology Of Cumentioning

confidence: 99%

The Role of Platelets in Chronic Urticaria

Veña¹,

Cassano

Marzano

et al. 2016

Int Arch Allergy Immunol

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Background: Platelets are implicated in many pathophysiological processes, including inflammation and immunity. Ever-growing evidence suggests the active involvement of platelets in the pathogenesis of various inflammatory disorders, including cutaneous inflammatory diseases. A limited number of studies have investigated the role of platelets in chronic urticaria (CU). In this review, we summarize the current knowledge regarding the role of platelets in chronic spontaneous and inducible urticarias. Methods: A literature search was performed using PubMed and Google Scholar, and the references of relevant literature were reviewed. Results: Overall, in CU patients, conflicting results have been obtained from the assessment of platelet indices, such as mean platelet volume, platelet count and distribution width, as well as markers of platelet aggregation and activation. Nevertheless, a few studies showed significant changes of such parameters in CU patients compared to controls, in apparent correlation with clinical severity, autoreactivity and/or inflammatory status. Conclusions: In the absence of definitive conclusions, the pathogenic role of platelets in CU needs to be further explored. Platelets might represent a link between inflammation, coagulation and histamine release in the pathophysiological network of CU.

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“…6), whereas p38 kinase inhibitor SB203580 was without effect (data not shown). It is known that upstream of the MAPK pathway the PAR-1 receptor of thrombin is coupled to both pertussis toxin-sensitive and -insensitive G proteins (5,27). In an attempt to determine whether thrombininduced CL-100 is mediated through a G i pertussis toxinsensitive G protein, we pretreated EC with 100 ng/ml of pertussis toxin prior to stimulation with TRAP-1 (100 M).…”

Section: Table I Novel Thrombin-inducible Genes In Ec Identified By Mmentioning

confidence: 99%

Role of CL-100, a Dual Specificity Phosphatase, in Thrombin-induced Endothelial Cell Activation

Chandrasekharan

Yang

Walters

et al. 2004

Journal of Biological Chemistry

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Using a cDNA microarray screening approach, we have identified seven novel thrombin-responsive genes in human umbilical vein endothelial cells that were verifiable by Northern blot analysis. Among them CL-100, a dual-specificity phosphatase also known as MAP kinase phosphatase-1 (MKP-1), showed greatest induction by thrombin. Steady-state levels of CL-100 mRNA induction by thrombin peaked at 1 h and declined rapidly (t1 ⁄2 ϳ45 min). Induction by thrombin was protease-activated receptor-1-mediated, protein synthesis-independent, and transcriptionally regulated. Metabolic labeling followed by immunoprecipitation verified that the thrombininduced CL-100 mRNA was translated into protein. We found that both Src-kinase and p42/p44 ERK activity are critical for thrombin-induced CL-100 expression, whereas phosphatidylinositol 3-kinase and protein kinase C activity were not required. Antisense-mediated inhibition of CL-100 was shown to prolong thrombininduced ERK activity in endothelial cells, concomitant with an inhibition in thrombin-induced PDGF-A (platelet-derived growth factor A) and PDGF-B gene expression and an up-regulation in thrombin-induced VCAM-1 and E-selectin gene expression. Inhibition of ERK activation by PD98059 in endothelial cells was shown to potentiate thrombin-induced expression of PDGF-B (ϳ3-fold) while inhibiting thrombin-induced VCAM-1 and Eselectin gene expression by 60 and 70%, respectively. These results suggested that induced expression of the CL-100 phosphatase and its subsequent regulation of ERK activity play a key regulatory role in the thrombin signaling pathway and in the transcriptional regulation of pathologically important "endothelial cell activation genes."

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Untitled

Cited by 79 publications

References 104 publications

Thrombin Induces Nitric-oxide Synthase via Gα12/13-coupled Protein Kinase C-dependent I-κBα Phosphorylation and JNK-mediated I-κBα Degradation

Thrombin Induces Nitric-oxide Synthase via Gα12/13-coupled Protein Kinase C-dependent I-κBα Phosphorylation and JNK-mediated I-κBα Degradation

The Role of Platelets in Chronic Urticaria

Role of CL-100, a Dual Specificity Phosphatase, in Thrombin-induced Endothelial Cell Activation

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