Tumor necrosis factor-α-induced cyclooxygenase-2 expression in human tracheal smooth muscle cells: involvement of p42/p44 and p38 mitogen-activated protein kinases and nuclear factor-κB

Lin, Chih‐Chung; Hsiao, Li-Der; Chien, Chin-Sung; Lee, Chiang‐Wen; Hsieh, Jen-Tsung; Yang, Che‐Hua

doi:10.1016/j.cellsig.2003.10.002

Cited by 58 publications

(62 citation statements)

References 37 publications

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“…17 Lin et al reported that tumor necrosis factor-␣-induced COX-2 expression is partly mediated through p38, leading to prostaglandin production in tracheal smooth muscle cells. 31 These findings may support the possibility that PDGF-BB-induced p38 phosphorylation may influence the chronic inflammatory process in the progression of atherosclerosis, especially in diabetic patients.…”

Section: Yamaguchi Et Al Role Of Pdgf-bb-induced P38 Activation In DIsupporting

confidence: 75%

Altered PDGF-BB–Induced p38 MAP Kinase Activation in Diabetic Vascular Smooth Muscle Cells

Yamaguchi

Inamori

Hirata

et al. 2004

ATVB

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Objective-We investigated the regulation of p38 mitogen-activated protein kinase (MAPK) by platelet-derived growth factor (PDGF)-BB and its biological effects in cultured normal and diabetic rat vascular smooth muscle cells (VSMCs). Methods and Results-VSMC growth from diabetic rats was faster than that from normal rats. The expression of the PDGF ␤-receptor in diabetic VSMCs was significantly elevated compared with that in normal cells, and PDGF-BB-induced p38 phosphorylation in diabetic cells was more enhanced via MAPK kinase (MKK) 3/6. The level of PKC activity in diabetic cells increased more than that in normal cells with or without PDGF-BB. Although protein kinase C (PKC)-␤II and PKC-␦ were activated by diabetes, PDGF-BB could further enhance the level of PKC-␦ alone. PDGF-BB-induced cell migration was more elevated in diabetic VSMCs, and the increase was significantly inhibited by SB-203580, rottlerin, and antisense oligodeoxynucleotides for PKC-␦. PDGF-BB-induced p38 phosphorylation also regulated cell growth, cyclooxygenase-2 levels, and arachidonic acid release, but not apoptosis. These levels were more elevated in diabetic cells, which were inhibited by SB-203580. Conclusions-Our study established that PDGF-BB phosphorylated p38 via PKC-␦ and the subsequent MKK 3/6, leading to cell growth regulation and the progression of a chronic inflammatory process in diabetic VSMCs. Key Words: p38 Ⅲ PDGF-BB Ⅲ VSMC Ⅲ PKC Ⅲ migration D iabetes mellitus is a most crucial risk factor for atherosclerosis. 1,2 Several hypotheses, such as hyperosmolarity, 3 advanced glycation end products, 4 oxidant formation, 5 abnormality of sorbitol and myoinositol metabolism, 6 and diacylglycerol protein kinase C (PKC) activation, 7 have been proposed to explain the various pathological changes induced by hyperglycemia in vasculature. Glucose and its metabolites possibly mediate their adverse effects by altering the various signal transduction pathways used by vascular cells to perform their functions and maintain cellular integrity. Some changes in vascular cells include increases in contractility, cellular proliferation, migration, and extracellular matrix production, which are abnormal in diabetes. 7 We and other investigators recently identified that the activation of p38 mitogen-activated protein kinase (MAPK) could be responsible for some vascular dysfunctions observed in the diabetic state. 8 -11 However, it has not been determined whether hyperglycemia and its metabolites can affect other signal transduction systems and/or the cellular targets of p38 activation.In contrast, the platelet-derived growth factor (PDGF) is recognized as a major mitogen in serum and one of the most important growth factors that promote atherogenesis, including the proliferation of vascular smooth muscle cells (VSMCs). 12-15 PDGF-BB can bind all types of receptors and activate the GTPase-activating protein of Ras (Ras-GTP) and, subsequently, extracellular-regulated protein kinase (extracellular signal regulated kinase [ERK]) 1/2, leading to cellul...

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Section: Yamaguchi Et Al Role Of Pdgf-bb-induced P38 Activation In DIsupporting

confidence: 75%

Altered PDGF-BB–Induced p38 MAP Kinase Activation in Diabetic Vascular Smooth Muscle Cells

Yamaguchi

Inamori

Hirata

et al. 2004

ATVB

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“…Thus, TNFa-induced signaling pathways coupled with activation of cPLA 2 a are not fully elucidated. TNFainduced responses were regulated by a protein kinase C (PKC) pathway (12,13) and a role for PKC in the regulation of cPLA 2 a and AA release has been shown (8,14,15). Activation of PKC can trigger a kinase cascade leading to activation of ERK1 / 2 and the resulting release of AA (8,15,16), but the relationship between PKC and the MAPK pathways in AA release is still largely unknown.…”

Section: +mentioning

confidence: 99%

Expression of Cytosolic Phospholipase A2α in Murine C12 Cells, a Variant of L929 Cells, Induces Arachidonic Acid Release in Response to Phorbol Myristate Acetate and Ca2+ Ionophores, but Not to Tumor Necrosis Factor-α

et al. 2004

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Abstract. Tumor necrosis factor-a (TNFa)-induced cell death is regulated through the release of arachidonic acid (AA) by group IVA cytosolic phospholipase A 2 (cPLA 2 a ) in the murine fibroblast cell line L929. However, the signaling pathway by which TNFa activates cPLA 2 a remained to be solved. We examined AA release in L929 cells, in a variant of L929 (C12 cells) lacking cPLA 2 a, and in C12 cells transfected with cPLA 2 a expression vectors. In transient and stable clones of C12 cells expressing cPLA 2 a, Ca 2+ ionophore A23187 and phorbol myristate acetate (PMA) stimulated AA release within 90 min, although no response to TNFa was observed within 6 h. These results suggest that C12 cells may lack the components necessary for TNFa -induced AA release, in addition to cPLA 2 a. PMA is known to stimulate AA release via phosphorylation of Ser 505 in cPLA 2 a by activating extracellular signal-regulated kinases (ERK1 / 2). However, PMA-induced AA release from C12 cells expressing mutant cPLA 2 a S505A (mutation of Ser 505 to Ala), which is not phosphorylated by ERK1 / 2, was similar to that from L929 cells and C12 cells expressing wild-type cPLA 2 a . The role of Ser 505 phosphorylation in AA release induced by PMA is also discussed.

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“…PC-PLC, associated with cell proliferation, apoptosis and differentiation, is a molecule that produces DAG and phosphorylcholine from phosphatidylcholine (PC) hydrolysis. Many cytokines such as TNF-a, LPS and IFN-c induce inflammatory response and apoptosis through activating PC-PLC in different types of cells [26][27][28]. It has been reported that TNF-a increases the production of IP3R1 through PC-PLC activation in human neural cells and mesangial cells, leading to higher calcium-releasing activity [24,29].…”

Section: Discussionmentioning

confidence: 99%

“…PC-PLC, a molecule that produces DAG and phosphorylcholine from phosphatidylcholine (PC) hydrolysis, is reported to mediate TNF-a signaling in various cells [26][27][28]. Then we wondered whether the enzyme participates in stimulatory effect of TNF-a during osteoclast differentiation.…”

Section: Pc-plc Inhibitor D609 Doesn't Inhibit Osteoclastogenesis Indmentioning

confidence: 99%

PC‐PLC is involved in osteoclastogenesis induced by TNF‐α through upregulating IP3R1 expression

et al. 2012

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a b s t r a c tThe precise mechanism of how TNF-a promotes osteoclast formation is not clear. Previous reports show TNF-a targets molecules that regulate calcium signaling. Inositol-1,4,5-trisphosphate receptors (IP3Rs) are important calcium channel responsible for evoking intracellular calcium oscillation. We found that TNF-a increased the expression of IP3R1 and promoted osteoclastogenesis in RANKLinduced mouse BMMs. Phosphatidylcholine-specific phospholipase C (PC-PLC) specific inhibitor D609 eliminated the upregulation of IP3R1 by TNF-a, and decreased the autoamplification of nuclear factor of activated T-cells 1 (NFATc1), thus resulted in less osteoclasts formation. However, D609 did not inhibit RANKL-induced osteoclastogenesis. Our data suggest TNF-a promotes RANKL-induced osteoclastogenesis, at least partially, through PC-PLC/IP3R1/NFATc1 pathway.

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Tumor necrosis factor-α-induced cyclooxygenase-2 expression in human tracheal smooth muscle cells: involvement of p42/p44 and p38 mitogen-activated protein kinases and nuclear factor-κB

Cited by 58 publications

References 37 publications

Altered PDGF-BB–Induced p38 MAP Kinase Activation in Diabetic Vascular Smooth Muscle Cells

Altered PDGF-BB–Induced p38 MAP Kinase Activation in Diabetic Vascular Smooth Muscle Cells

Expression of Cytosolic Phospholipase A2α in Murine C12 Cells, a Variant of L929 Cells, Induces Arachidonic Acid Release in Response to Phorbol Myristate Acetate and Ca2+ Ionophores, but Not to Tumor Necrosis Factor-α

PC‐PLC is involved in osteoclastogenesis induced by TNF‐α through upregulating IP3R1 expression

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