Functional Coupling between Secretory and Cytosolic Phospholipase A2 Modulates Tumor Necrosis Factor-α- and Interleukin-1β-induced NF-κB Activation

Anthonsen, Marit W.; Solhaug, Anita; Johansen, Berit

doi:10.1074/jbc.m008481200

Cited by 76 publications

(84 citation statements)

References 95 publications

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“…However, secretory phospholipase A2 (sPLA2) is reported to be more potently inhibited by BPB than are type C phospholipases (Marshall et al, 1991). Studies in our laboratory with more selective sPLA2 inhibitors strongly indicate that sPLA2 is involved in TNFR1 mediated NFκB activation in human keratinocytes (Thommesen et al, 1998) and recently a functional coupling between sPLA2 and cytosolic (c) PLA2 in TNF-mediated NFκB activation was reported (Anthonsen et al, 2001). The effect of BPB in the present study may suggest that sPLA2 play a role in TNFR1 signaling, also in SW480/β-gal cells.…”

Section: Discussionsupporting

confidence: 68%

“…RIP, originally identified as a Fas-associating molecule (Stanger et al, 1995), interacts with both TNFR1/TNFR2 Liu et al, 1996). TNFR1-mediated NFκB activation has been reported to involve phosphatidylcholine specific phospholipase C (PC-PLC), sphingomyelinase (SMase), phospholipase A2 (Schutze et al, 1992;Yang et al, 1993;Thommesen et al, 1998) atypical PKCs (Anthonsen et al, 2001) and protein kinase C -ζ (PKC-ζ) activated by ceramide (Lozano et al, 1994;Folgueira et al, 1996). TNFR2-mediated signaling is less studied even though a TNFR2 specific signaling component, the tyrosine kinase Etk/Bmx, has recently been identified to be involved in TNF-induced angiogenesis (Pan et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

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Distinct Differences between TNF Receptor 1- and TNF Receptor 2- mediated Activation of NFκB

Thommesen¹,

Lægreid²

2005

BMB Reports

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Tumor necrosis factor (TNF) signaling is mediated via two distinct receptors, TNFR2 and TNFR1, which shows partially overlapping signaling mechanisms and biological roles. In the present study, TNFR2 and TNFR1 signal transduction mechanisms involved in activation of NFκB and CMV promoter-enhancer were compared with respect to their susceptibility towards inhibitors of intracellular signaling. For this, we used SW480 cells, where we have shown that TNF-signaling can occur independently through each of the two receptors. The TNFR1 response was inhibited by D609, bromophenacyl bromide (BPB), nordihydroguararetic acid (NDGA), and by sodium salicylate, while TNFR2-mediated activation of NFκB and CMV promoter-enhancer was resistant to these compounds. The signaling mechanisms known to be affected by these inhibitors include phospholipases as well as redox-and pH-sensitive intracellular components. Our results imply that TNFR2 signaling involved in NFκB activation proceeds independently of these inhibitor-sensitive signaling components, indicating distinct signaling pathways not shared with TNFR1.

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Section: Discussionsupporting

confidence: 68%

Section: Introductionmentioning

confidence: 99%

Distinct Differences between TNF Receptor 1- and TNF Receptor 2- mediated Activation of NFκB

Thommesen¹,

Lægreid²

2005

BMB Reports

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“…We have recently reported the involvement of snpPLA 2 , LTB 4 , and cPLA 2 in TNF-␣ and IL-1␤-induced NF-B activation in human keratinocytes (28,29). We also found that a functional coupling between snpPLA 2 and cPLA 2 , in which cPLA 2 phosphorylation and activation was preceded by snpPLA 2 /5-LO/LTB 4 activity, was of importance for cytokineinduced NF-B activation (29).…”

mentioning

confidence: 88%

“…The generation of HaCaT cells stably expressing the plasmid pBIIX with two copies of an HIV-NF-B sequence cloned upstream of the mouse fos promoter and the Photinus pyralis luciferase coding sequence (31) has been described previously (29). Isolation of NIH-3T3 fibroblasts stably transfected with v-ras or doubly transfected with v-ras-dn/PKC, which was grown in the presence of hygromycin (0.3 mg/ml), has been reported previously (32,33 Assay of cPLA 2 Activity-NIH-3T3 cells were cultured in DMEM with 4.5 g of glucose/liter and 10% FCS to 50% confluency in 6-round multiwell plates and starved in 0.5% FCS-containing DMEM for 24 h. Stimulated NIH-3T3 cells were scraped into lysis buffer (10 mM Hepes, pH 7.5, 0.34 M sucrose, 0.8 mM Triton X-100, 1 mM EDTA, 1 mM EGTA, 10 g/ml leupeptin, 1 mM phenylmethylsulfonyl fluoride, 1 M pepstatin), homogenized by 10 passes through a 26-gauge needle, and centrifuged (14,000 rpm, 10 min, 4°C).…”

Section: Methodsmentioning

confidence: 99%

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Atypical λ/ιPKC Conveys 5-Lipoxygenase/Leukotriene B4-mediated Cross-talk between Phospholipase A2s Regulating NF-κB Activation in Response to Tumor Necrosis Factor-α and Interleukin-1β

Anthonsen

Andersen

Solhaug

et al. 2001

Journal of Biological Chemistry

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PTH and phospholipase A2 in the aging process of intestinal cells

Gentili

Morelli

Boland

2004

J of Cellular Biochemistry

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In this study we analyzed, for the first time, alterations in phospholipase A2 (PLA2) activity and response to parathyroid hormone (PTH) in rat enterocytes with aging. We found that PTH, rapidly stimulate arachidonic acid (AA) release in rat duodenal cells (+1- to 2-fold), an effect that is greatly potentiated by aging (+4-fold). We also found that hormone-induced AA release in young animals is Ca2+-dependent via cPLA2, while AA released by PTH in cells from aged rats is due to the activation of cPLA2 and the Ca2+-independent PLA2 (iPLA2). In enterocytes from 3 months old rats, PTH induced, in a time and dose-dependent fashion, the phosphorylation of cPLA2 on serine 505, with a maximum at 10 min (+7-fold). Basal levels of cPLA2 serine-phosphorylation were higher in old enterocytes, affecting the hormone response which was greatly diminished (+2-fold at 10 min). cPLA2 phosphorylation impairment in old animals was not related to changes of cPLA2 protein expression and did not explain the substantial increase on PTH-induced AA release with aging, further suggesting the involvement of a different PLA2 isoform. Intracellular Ca2+ chelation (BAPTA-AM, 5 microM) suppressed the serine phosphorylation of cPLA2 in both, young and aged rats, demonstrating that intracellular Ca2+ is required for full activation of cPLA2 in enterocytes stimulated with PTH. Hormone effect on cPLA2 was suppressed to a great extent by the MAP kinases ERK 1 and ERK2 inhibitor, PD 98059 (20 microM), the cAMP antagonist, Rp-cAMP, and the PKC inhibitor Ro31820 both, in young and aged animals. Enterocytes exposure to PTH also resulted in phospho-cPLA2 translocation from cytosol to nuclei and membrane fractions, where phospholipase substrates reside. Hormone-induced enzyme translocation is also modified by aging where, in contrast to young animals, part of phospho-cPLA2 remained cytosolic. Collectively, these data suggest that PTH activates in duodenal cells, a Ca2+-dependent cytosolic PLA2 and attendant AA release and that this activation requires prior stimulation of intracellular ERK1/2, PKA, and PKC. cPLA2 is the major enzyme responsible for AA release in young enterocytes while cPLA2 and the Ca2+-independent iPLA2, potentiate PTH-induced AA release in aged cells. Impairment of PTH activation of PLA2 isoforms upon aging may result in abnormal hormone regulation of membrane fluidity and permeability and thereby affecting intestinal cell membrane function.

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Functional Coupling between Secretory and Cytosolic Phospholipase A2 Modulates Tumor Necrosis Factor-α- and Interleukin-1β-induced NF-κB Activation

Cited by 76 publications

References 95 publications

Distinct Differences between TNF Receptor 1- and TNF Receptor 2- mediated Activation of NFκB

Distinct Differences between TNF Receptor 1- and TNF Receptor 2- mediated Activation of NFκB

Atypical λ/ιPKC Conveys 5-Lipoxygenase/Leukotriene B4-mediated Cross-talk between Phospholipase A2s Regulating NF-κB Activation in Response to Tumor Necrosis Factor-α and Interleukin-1β

PTH and phospholipase A2 in the aging process of intestinal cells

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