Propranolol-induced inhibition of rat brain cytoplasmic phosphatidate phosphohydrolase

Pappu, Anuradha S.; Hauser, George

doi:10.1007/bf00964158

Cited by 92 publications

(51 citation statements)

References 37 publications

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“…5F). An identical effect on capillary formation, was also produced by culturing wild-type allantoises in the presence of 75 µM propranolol, a potent inhibitor of LPP activity (Pappu and Hauser, 1983) (data not shown). …”

Section: Disruption Of Allantois Morphogenesis Leads To Defective Plamentioning

confidence: 77%

The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning

et al. 2003

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Bioactive phospholipids, which include sphingosine-1-phosphate,lysophosphatidic acid, ceramide and their derivatives regulate a wide variety of cellular functions in culture such as proliferation, apoptosis and differentiation. The availability of these lipids and their products is regulated by the lipid phosphate phosphatases (LPPs). Here we show that mouse embryos deficient for LPP3 fail to form a chorio-allantoic placenta and yolk sac vasculature. A subset of embryos also show a shortening of the anterior-posterior axis and frequent duplication of axial structures that are strikingly similar to the phenotypes associated with axin deficiency,a critical regulator of Wnt signaling. Loss of LPP3 results in a marked increase in β-catenin-mediated TCF transcription, whereas elevated levels of LPP3 inhibit β-catenin-mediated TCF transcription. LPP3 also inhibits axis duplication and leads to mild ventralization in Xenopusembryo development. Although LPP3 null fibroblasts show altered levels of bioactive phospholipids, consistent with loss of LPP3 phosphatase activity, mutant forms of LPP3, specifically lacking phosphatase activity, were able to inhibit β-catenin-mediated TCF transcription and also suppress axis duplication, although not as effectively as intact LPP3. These results reveal that LPP3 is essential to formation of the chorio-allantoic placenta and extra-embryonic vasculature. LPP3 also mediates gastrulation and axis formation, probably by influencing the canonical Wnt signaling pathway. The exact biochemical roles of LPP3 phosphatase activity and its undefined effect on β-catenin-mediated TCF transcription remain to be determined.

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Section: Disruption Of Allantois Morphogenesis Leads To Defective Plamentioning

confidence: 77%

The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning

et al. 2003

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“…3B). Propranolol, --'~" 100 ~T A which inhibits the hydrolysis of PA to DG [26], also reduced arachidonic acid release by fMLP-stimulated PMN, with an 80 IC50 of 25 txM (Fig. 3C).…”

Section: Aacocf3 (Nm)mentioning

confidence: 89%

“…These results suggest genates decreased from 0.368 + 0.050 pmol/min/106 cell that in rat PMN PLD is functionally linked to cPLA2, but not equivalents (n = 4) to 0.226 + 0.019 (P < 0.05) and to DG lipase. Propranolol, generally used as a PA phospha-0.174+0.017 pmol/min/106 cell equivalents (P<0.01) when tase inhibitor [26], also suppressed arachidonic acid release, the cells were treated with fMLP in the presence of 0.5 and suggesting that certain products generated after the PLD/PA 1% ethanol, respectively, cPLA2 activity in homogenates of phosphatase pathway are involved in cPLAz activation. Since PMN exposed to fMLP in the presence of 1% ethanol, which DG, a product of the PLD/PA phosphatase pathway, is a was comparable to that in homogenates of unstimulated potent activator of protein kinase C [32], subsequent kinases, PMN, was insensitive to acid phosphatase treatment (data such as MAP kinase, may be responsible for cPLA2 activanot shown).…”

Section: Aacocf3 (Nm)mentioning

confidence: 95%

Phospholipase D is involved in cytosolic phospholipase A₂‐dependent selective release of arachidonic acid by fMLP‐stimulated rat neutrophils

et al. 1996

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The production of phosphatidic acid (PA) from phosphoAbstract When rat polymorphonuclear neutrophils (PMN) were treated with N-formyI-Met-Leu-Phe (fMLP), the release lipase D (PLD)-catalyzed hydrolysis of phosphatidylcholine is of araehidonie acid in preference to other fatty acids was a rapid and widespread response of cells stimulated with diobserved. Levels of arachidonic acid reached a plateau within verse agonists, and is implicated in a broad spectrum of 5 rain, and were accompanied by an ,-~ 4-fold increase in in vitro physiological and pathological processes, such as exocytosis, phospholipase (PL) A2 and PLD activities in PMN lysates, mitogenesis, oncogenesis and inflammation (reviewed in [4]). Treatment of PMN with ethanol (an inhibitor of PLD-mediatedThere are also several lines of evidence to suggest that arachiphosphatidic acid formation), propranolol (a phosphatiflic acid donic acid release correlates with PLD activation. Arachidonphosphatase inhibitor), or 4-bromophenaeylbromide (a PLA2 ic acid release by activated cells is reported to be accompanied inhibitor), each suppressed fMLP-stimulated araehidonate reby the increase in PLD activity and inhibition of PLD by lease. Treatment with RHC-80267 (a diaeylglyeerol lipase ethanol is associated with the decrease in arachidonic acid inhibitor), however, had no such effect. The eytosolie PLA2 release [5][6][7][8][9][10]. To account for these observations, some inves-(ePLA2) inhibitor, araehidonoyl trifluoromethyl ketone, suppressed PLA2 activity in PMN homogenates and araehidonate tigators have proposed that the PA generated by the PLD release by fMLP-treated PMN. These results suggest that reaction is converted to diacylglycerol (DG) by PA phosphatfMLP-elicited arachidonate release is mediated by cPLA2 but ase, and that arachidonic acid is released from DG by DG not diacylglycerol lipase, and that the activation of cPLA2 is lipase [6,7]. In contrast to this 'indirect' model for arachidonic downstream of the PLD-dependent signaling pathway, acid release via DG, other investigators have proposed that arachidonic acid is 'directly' released from phospholipids by

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“…BEL has recently been reported to inhibit Mg 2+ -dependent cytosolic phosphatidate phosphohydrolase-1 (PAP-1) (Balsinde and Dennis, 1996). To determine whether PAP-1 is involved in BEL-induced inhibition of cell proliferation, we treated the cells with propranolol, a well-known PAP-1-specific inhibitor (Fuentes et al, 2003;Pappu and Hauser, 1983). In accordance Journal of Cell Science 119 (6) (2ϫ10 5 ) were transfected with ARD-iPLA 2 -GFP (5 g/100 mm plate), then counted daily, starting 24 hours after transfection.…”

Section: G1mentioning

confidence: 99%

Disruption of G1-phase phospholipid turnover by inhibition of Ca2+-independent phospholipase A2 induces a p53-dependent cell-cycle arrest in G1 phase

Zhang

Zhao

Seleznev

et al. 2006

Journal of Cell Science

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The G1 phase of the cell cycle is characterized by a high rate of membrane phospholipid turnover. Cells regulate this turnover by coordinating the opposing actions of CTP:phosphocholine cytidylyltransferase and the group VI Ca2+-independent phospholipase A2 (iPLA2). However, little is known about how such turnover affects cell-cycle progression. Here, we show that G1-phase phospholipid turnover is essential for cell proliferation. Specific inhibition of iPLA2 arrested cells in the G1 phase of the cell cycle. This G1-phase arrest was associated with marked upregulation of the tumour suppressor p53 and the expression of cyclin-dependent kinase inhibitor p21cip1. Inactivation of iPLA2 failed to arrest p53-deficient HCT cells in the G1 phase and caused massive apoptosis of p21-deficient HCT cells, suggesting that this G1-phase arrest requires activation of p53 and expression of p21cip1. Furthermore, downregulation of p53 by siRNA in p21-deficient HCT cells reduced the cell death, indicating that inhibition of iPLA2 induced p53-dependent apoptosis in the absence of p21cip1. Thus, our study reveals hitherto unrecognized cooperation between p53 and iPLA2 to monitor membrane-phospholipid turnover in G1 phase. Disrupting the G1-phase phospholipid turnover by inhibition of iPLA2 activates the p53-p21cip1 checkpoint mechanism, thereby blocking the entry of G1-phase cells into S phase.

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Propranolol-induced inhibition of rat brain cytoplasmic phosphatidate phosphohydrolase

Cited by 92 publications

References 37 publications

The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning

The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning

Phospholipase D is involved in cytosolic phospholipase A₂‐dependent selective release of arachidonic acid by fMLP‐stimulated rat neutrophils

Disruption of G1-phase phospholipid turnover by inhibition of Ca2+-independent phospholipase A2 induces a p53-dependent cell-cycle arrest in G1 phase

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Propranolol-induced inhibition of rat brain cytoplasmic phosphatidate phosphohydrolase

Cited by 92 publications

References 37 publications

The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning

The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning

Phospholipase D is involved in cytosolic phospholipase A2‐dependent selective release of arachidonic acid by fMLP‐stimulated rat neutrophils

Disruption of G1-phase phospholipid turnover by inhibition of Ca2+-independent phospholipase A2 induces a p53-dependent cell-cycle arrest in G1 phase

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Phospholipase D is involved in cytosolic phospholipase A₂‐dependent selective release of arachidonic acid by fMLP‐stimulated rat neutrophils