Protein Kinase Cδ Mediates Lysophosphatidic Acid-induced NF-κB Activation and Interleukin-8 Secretion in Human Bronchial Epithelial Cells

Cummings, Rhett; Zhao, Yutong; Jacoby, David B.; Spannhake, E. W.; Ohba, Masaaki; Garcia, Joe G.N.; Watkins, Tonya; He, Donghong; Saatian, Bahman; Natarajan, Viswanathan

doi:10.1074/jbc.m404045200

Cited by 120 publications

(189 citation statements)

References 40 publications

(63 reference statements)

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“…Our previous studies showed that PKC δ plays a critical role in LPA-induced IL-8 expression [16] and EGF-R transactivation [20]. Here we examined the role of PKC δ in cross-talk between LPA-Rs and c-Met in HBEpCs.…”

Section: Lpa Induces Serine Phosphorylation Of C-met Via G I and Pkc mentioning

confidence: 90%

“…HBEpCs were isolated from normal human lung obtained from lung transplant donors following previously described procedures [16]. The isolated passage 0 (P 0 ) HBEpCs were cultured in serum free basal essential growth medium (BEGM) and supplemented with growth factors.…”

Section: Cell Culturementioning

confidence: 99%

“…Infection of HBEpCs (∼50 % confluence) with purified adenoviral empty vector or adenoviral vector containing catalytically inactive mutant of human PKC δ (Dn-PKC δ) were carried out in 100 mm-dishes as described previously [16]. Cells were infected with different MOI in 1 ml of BEGM for 48 h.…”

Section: Infection With Adenoviral Constructsmentioning

confidence: 99%

“…We previously showed that LPA treatment induced phosphorylation of PKC δ and translocation of PKC δ to plasma membrane [16]. To further determine the mechanisms of LPA-induced cMet redistribution to plasma membrane, we examined the role of PKC δ in regulating c-Met traffic in response to LPA treatment.…”

Section: Lpa Induces C-met Redistribution Via Pkc δ In Hbepcmentioning

confidence: 99%

“…We have previously shown that human bronchial epithelial cells (HBEpCs) express LPA [1][2][3] and that exposure to LPA stimulated expression and secretion of interleukin-8 (IL-8). The IL-8 expression is also partly regulated by protein kinase C δ (PKC δ), Nuclear factor-κB (NF-κB), and c-Jun-N-terminal Kinase (JNK)/AP-1 transcriptional factors [16][17][18]. Furthermore, LPA induced IL-13 receptor alpha2 (IL-13Rα2) expression and secretion and attenuated IL-13-induced signaling in HBEpCs [19].…”

Section: Introductionmentioning

confidence: 99%

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Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Zhao¹,

He²,

Stern³

et al. 2007

Cellular Signalling

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Previously we demonstrated that ligation of lysophosphatidic acid (LPA) to G protein-coupled LPA receptors induces transactivation of receptor tyrosine kinases (RTKs), such as platelet-derived growth factor receptor beta (PDGF-Rβ) and epidermal growth factor receptor (EGF-R), in primary cultures of human bronchial epithelial cells (HBEpCs). Here we examined the role of LPA on c-Met redistribution and modulation of hepatocyte growth factor ( These results demonstrate that LPA regulates c-Met function through PKC δ-and E-cadherin in HBEpCs, suggesting an alternate function of the cross-talk between G-protein coupled receptors (GPCRs) and RTKs in HBEpCs.

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Section: Lpa Induces Serine Phosphorylation Of C-met Via G I and Pkc mentioning

confidence: 90%

Section: Cell Culturementioning

confidence: 99%

Section: Infection With Adenoviral Constructsmentioning

confidence: 99%

Section: Lpa Induces C-met Redistribution Via Pkc δ In Hbepcmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Zhao¹,

He²,

Stern³

et al. 2007

Cellular Signalling

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Regulation of interleukin‐1β–induced chemokine production and matrix metalloproteinase 2 activation by epigallocatechin‐3‐gallate in rheumatoid arthritis synovial fibroblasts

Ahmed¹,

Pákozdi²,

Koch³

2006

Arthritis & Rheumatism

121

124

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Objective. To evaluate the efficacy of epigallocatechin-3-gallate (EGCG), a potent antiinflammatory molecule, in regulating interleukin-1␤ (IL-1␤)-induced production of the chemokines RANTES (CCL5), monocyte chemoattractant protein 1 (MCP-1/ CCL2), epithelial neutrophil-activating peptide 78 (ENA-78/CXCL5), growth-regulated oncogene ␣ (GRO␣/CXCL1), and matrix metalloproteinase 2 (MMP-2) activity in rheumatoid arthritis (RA) synovial fibroblasts.Methods. Fibroblasts obtained from RA synovium were grown, and conditioned medium was obtained. Cell viability was determined by MTT assay. RANTES, MCP-1, ENA-78, and GRO␣ produced in culture supernatants were measured by enzyme-linked immunosorbent assay. MMP-2 activity was analyzed by gelatin zymography. Western blotting was used to study the phosphorylation of protein kinase C (PKC) isoforms and nuclear translocation of NF-B.Results. EGCG was nontoxic to RA synovial fibroblasts. Treatment with EGCG at 10 M or 20 M significantly inhibited IL-1␤-induced ENA-78, RANTES, and GRO␣, but not MCP-1 production in a concentration-dependent manner. EGCG at 50 M caused a complete block of IL-1␤-induced production of RANTES, ENA-78, and GRO␣, and reduced production of MCP-1 by 48% (P < 0.05). Zymography showed that EGCG blocked constitutive, IL-1␤-induced, and chemokine-mediated MMP-2 activity. Evaluation of signaling events revealed that EGCG preferentially blocked the phosphorylation of PKC␦ and inhibited the activation and nuclear translocation of NF-B in IL-1␤-treated RA synovial fibroblasts.Conclusion. These results suggest that EGCG may be of potential therapeutic value in inhibiting joint destruction in RA.

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Ca²⁺/calmodulin-dependent kinase II contributes to inhibitor of nuclear factor-kappa B kinase complex activation inHelicobacter pyloriinfection

et al. 2013

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Helicobacter pylori, a class I carcinogen, induces a proinflammatory response by activating the transcription factor nuclear factor-kappa B (NF-jB) in gastric epithelial cells. This inflammatory condition could lead to chronic gastritis, which is epidemiologically and biologically linked to the development of gastric cancer. So far, there exists no clear knowledge on how H. pylori induces the NF-jB-mediated inflammatory response. In our study, we investigated the role of Ca 21 /calmodulindependent kinase II (CAMKII), calmodulin, protein kinases C (PKCs) and the CARMA3-Bcl10-MALT1 (CBM) complex in conjunction with H. pylori-induced activation of NF-jB via the inhibitor of nuclear factor-kappa B kinase (IKK) complex. We use specific inhibitors and/or RNA interference to assess the contribution of these components. Our results show that CAMKII and calmodulin contribute to IKK complex activation and thus to the induction of NF-jB in response to H. pylori infection, but not in response to TNF-a. Thus, our findings are specific for H. pylori infected cells. Neither the PKCs a, d, h, nor the CBM complex itself is involved in the activation of NF-jB by H. pylori. The contribution of CAMKII and calmodulin, but not PKCs/CBM to the induction of an inflammatory response by H. pylori infection augment the understanding of the molecular mechanism involved and provide potential new disease markers for the diagnosis of gastric inflammatory diseases including gastric cancer.

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Protein Kinase Cδ Mediates Lysophosphatidic Acid-induced NF-κB Activation and Interleukin-8 Secretion in Human Bronchial Epithelial Cells

Cited by 120 publications

References 40 publications

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Regulation of interleukin‐1β–induced chemokine production and matrix metalloproteinase 2 activation by epigallocatechin‐3‐gallate in rheumatoid arthritis synovial fibroblasts

Ca²⁺/calmodulin-dependent kinase II contributes to inhibitor of nuclear factor-kappa B kinase complex activation inHelicobacter pyloriinfection

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Protein Kinase Cδ Mediates Lysophosphatidic Acid-induced NF-κB Activation and Interleukin-8 Secretion in Human Bronchial Epithelial Cells

Cited by 120 publications

References 40 publications

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Regulation of interleukin‐1β–induced chemokine production and matrix metalloproteinase 2 activation by epigallocatechin‐3‐gallate in rheumatoid arthritis synovial fibroblasts

Ca2+/calmodulin-dependent kinase II contributes to inhibitor of nuclear factor-kappa B kinase complex activation inHelicobacter pyloriinfection

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Ca²⁺/calmodulin-dependent kinase II contributes to inhibitor of nuclear factor-kappa B kinase complex activation inHelicobacter pyloriinfection