scholarly journals Effect of TLR4/MyD88 Signaling Pathway on Expression of IL-1βand TNF-αin Synovial Fibroblasts from Temporomandibular Joint Exposed to Lipopolysaccharide

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Xuefen Lin ◽  
Jingjing Kong ◽  
Qingting Wu ◽  
Yingying Yang ◽  
Ping Ji
Keyword(s):  
Signal Transduction ◽  
Temporomandibular Joint ◽  
Interleukin 1 ◽  
Signal Transduction Pathway ◽  
Synovial Fibroblasts ◽  
Signal Pathways ◽  
Transduction Pathway ◽  
Inhibitory Peptide ◽  
Surface Receptors ◽  
Protein Levels

Accumulating evidence from previous studies suggested that interleukin-1 (IL-1β) and tumor necrosis factor-α(TNF-α) play an important role in pathogenesis of temporomandibular disorders (TMD). However, the cell surface receptors and the intracellular signal pathways leading to these cytokines expression are not fully understood. In the current study, we investigated the roles of Toll-like receptor 4 (TLR4) and its adaptor myeloid differentiation factor 88 (MyD88) in the expression of IL-1βand TNF-αin synovial fibroblasts (SFs) separated from rat temporomandibular joint (TMJ) with lipopolysaccharide (LPS) stimulation. The results showed that treatment with LPS could increase TLR4, MyD88, IL-1β, and TNF-αexpression at both mRNA and protein levels. In addition, increased expression of IL-1βand TNF-αcould be blocked by treatment with TAK-242, a blocker of TLR4 signaling, and also by MyD88 inhibitory peptide (MIP). These findings suggested that maybe TLR4/MyD88 signal transduction pathway participates in enhanced expression of IL-1 and TNF-αin patients with TMD. The activation of TLR4/MyD88 signal transduction pathway which results in production of proinflammatory factors may play a role in the pathogenesis of TMD.

Involvement of cyclic AMP-dependent protein kinases in the signal transduction pathway for interleukin-1

1990 ◽  
Vol 10 (7) ◽  
pp. 3824-3827
Author(s):  
M Chedid ◽  
S B Mizel
Keyword(s):  
Signal Transduction ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Gene Transcription ◽  
Interleukin 1 ◽  
Signal Transduction Pathway ◽  
Cell Types ◽  
Specific Protein ◽  
Transduction Pathway ◽  
Dependent Protein

Expression of a highly specific protein inhibitor for cyclic AMP-dependent protein kinases in interleukin-1 (IL-1)-responsive cells blocked IL-1-induced gene transcription that was driven by the kappa immunoglobulin enhancer or the human immunodeficiency virus long terminal repeat. This inhibitor did not affect protein kinase C-mediated gene transcription, suggesting that cyclic AMP-dependent protein kinases are involved in the signal transduction pathway for IL-1 in a number of responsive cell types.

scholarly journals Calcium/calmodulin transduces thrombin-stimulated secretion: studies in intact and minimally permeabilized human umbilical vein endothelial cells.

1992 ◽  
Vol 118 (6) ◽  
pp. 1501-1510 ◽  
Author(s):  
K A Birch ◽  
J S Pober ◽  
G B Zavoico ◽  
A R Means ◽  
B M Ewenstein
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Phorbol Esters ◽  
Umbilical Vein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Inhibitory Peptide ◽  
Permeabilized Cells ◽  
Calmodulin Binding ◽  
Umbilical Vein Endothelial Cells

Thrombin stimulates cultured endothelial cells (EC) to secrete stored von Willebrand factor (vWF), but the signal transduction pathways are poorly defined. Thrombin is known to elevate the concentration of intracellular calcium ([Ca2+]i) and to activate protein kinase C (PKC) in EC. Since both calcium ionophores and phorbol esters release vWF, both second messenger pathways have been postulated to participate in vWF secretion in response to naturally occurring agonists. We find that in intact human EC, vWF secretion stimulated by either thrombin or by a thrombin receptor activating peptide, TR(42-55), can be correlated with agonist-induced elevations of [Ca2+]i. Further evidence implicating calcium in the signal transduction pathway is suggested by the finding that MAPTAM, a cell-permeant calcium chelator, in combination with the extracellular calcium chelator EGTA, can inhibit thrombin-stimulated secretion. In contrast, the observation that staurosporine (a pharmacological inhibitor of PKC) blocks phorbol ester- but not thrombin-stimulated secretion provides evidence against PKC-mediated signal transduction. To examine further the signal transduction pathway initiated by thrombin, we developed novel conditions for minimal permeabilization of EC with saponin (4-8 micrograms/ml for 5-15 min at 37 degrees C) which allow the introduction of small extracellular molecules without the loss of large intracellular proteins and which retain thrombin-stimulated secretion. These minimally permeabilized cells secrete vWF in response to exogenous calcium, and EGTA blocks thrombin-induced secretion. Moreover, in these cells, thrombin-stimulated secretion is blocked by a calmodulin-binding inhibitory peptide but not by a PKC inhibitory peptide. Taken together, these findings demonstrate that thrombin-stimulated vWF secretion is transduced by a rise in [Ca2+]i and provide the first evidence for the role of calmodulin in this process.

CK2 Is Acting Upstream of MEK3/6 as a Part of the Signal Control of ERK1/2 and p38 MAPK during Keratinocytes Autocrine Differentiation

2011 ◽  
Vol 66 (1-2) ◽  
pp. 83-86 ◽  
Author(s):  
Antonia R. Isaeva ◽  
Vanio I. Mitev
Keyword(s):  
Signal Transduction ◽  
P38 Mapk ◽  
Mammalian Cells ◽  
Protein Kinase Ck2 ◽  
Cell Signalling ◽  
Signal Transduction Pathway ◽  
Signal Control ◽  
Transduction Pathway ◽  
Protein Levels ◽  
Kinase Ck2

Protein kinase CK2 (formerly termed “casein kinase II”) is a ubiquitously in mammalian cells distributed Ser/Thr kinase, with global role in cell regulation. Although, the involvement of CK2 in cell signalling is vast-investigated, virtually nothing is known about its contribution to signal control of keratinocytes differentiation. Here we show that, in autocrine differentiating keratinocytes, inhibition of the CK2 activity induced by 4,5,6,7-tetrabromobenzotriazole (TBB) causes reciprocal changes in the activities of major signal transduction regulators of keratinocytes differentiation, i.e. ERK1/2 and p38 MAPK, without affecting their protein levels. The ERK1/2 activity is strongly suppressed, while the activity of p38 is increased. We have also found that the activity of upstream and specifi c for p38 MAPK kinase MEK3/6 is also stimulated by TBB. These original results clearly demonstrate the participation of CK2 in the signal transduction pathway controlling MEK3/6, p38 MAPK, and ERK1/2 in the used model system.

scholarly journals Involvement of cyclic AMP-dependent protein kinases in the signal transduction pathway for interleukin-1.

1990 ◽  
Vol 10 (7) ◽  
pp. 3824-3827 ◽  
Author(s):  
M Chedid ◽  
S B Mizel
Keyword(s):  
Signal Transduction ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Gene Transcription ◽  
Interleukin 1 ◽  
Signal Transduction Pathway ◽  
Cell Types ◽  
Specific Protein ◽  
Transduction Pathway ◽  
Dependent Protein

Expression of a highly specific protein inhibitor for cyclic AMP-dependent protein kinases in interleukin-1 (IL-1)-responsive cells blocked IL-1-induced gene transcription that was driven by the kappa immunoglobulin enhancer or the human immunodeficiency virus long terminal repeat. This inhibitor did not affect protein kinase C-mediated gene transcription, suggesting that cyclic AMP-dependent protein kinases are involved in the signal transduction pathway for IL-1 in a number of responsive cell types.

scholarly journals The Mechanism of MAPK Signal Transduction Pathway Involved with Electroacupuncture Treatment for Different Diseases

2019 ◽  
Vol 2019 ◽  
pp. 1-10 ◽  
Author(s):  
Weibin Du ◽  
Huahui Hu ◽  
Jiangsong Zhang ◽  
Guanai Bao ◽  
Rongliang Chen ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Electrical Stimulation ◽  
Molecular Mechanisms ◽  
Signal Transduction Pathway ◽  
Cerebrovascular Diseases ◽  
Mitogen Activated Protein Kinase ◽  
Signal Pathways ◽  
Transduction Pathway ◽  
Analgesic Effects ◽  
Electroacupuncture Treatment

The mitogen-activated protein kinase (MAPK) signal transduction pathway plays an important role in the regulation of various diseases, such as cardiovascular and cerebrovascular diseases, and takes part in anti-inflammatory effects, analgesic effects, protection against injury, and maintenance of gastrointestinal functions. Electroacupuncture therapy is an external therapy used in traditional Chinese medicine. By adding external electrical stimulation to traditional acupuncture, the stimulus gets doubled and the therapeutic efficacy gets enhanced accordingly. It combines the benefits of both acupuncture and electrical stimulation. In recent years, some studies have explored the molecular mechanisms of MAPK signal pathways involved with electroacupuncture treatment. Based on these recent studies, this article summarizes the mechanisms of MAPK signal transduction pathways involved with electroacupuncture treatment. This adds great value to the studies of molecular mechanisms of electroacupuncture treatment and also provides an effective reference for its clinical use.

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