Contribution of lipid mediators to the regulation of phosphatidylcholine synthesis by angiotensin

Kitos, Theresa E.; Drobnies, Adrienne E.; Ng, Michael; Wen, Yeong-Ray; Cornell, Rosemary B.

doi:10.1016/j.bbalip.2006.02.015

Cited by 11 publications

(8 citation statements)

References 62 publications

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“…These events could be blunted by inhibitors of select lipases. In both studies the inhibition of CCT could be partially reversed by exogenously supplied DAG, but not other lipid mediators, implying a primary role for DAG in the regulation of CCT by growth factors [16,188]. The stimulation of CCTa and PC synthesis by angiotensin or by exogenous DAG required functional protein kinase C and ERK1/2 [177].…”

Section: Cct Relocalization And/or Activation In Response To Agents Tmentioning

confidence: 87%

“…The stimulation of CCTa and PC synthesis by angiotensin or by exogenous DAG required functional protein kinase C and ERK1/2 [177]. Although CCTa activation was blunted by inhibitors of iPLA2, phospholipase C, and phospholipase D [16,188], the link between ERK1/2 activation and release of lipid activators of CCTa by phospholipases has yet to be fully established.…”

Section: Cct Relocalization And/or Activation In Response To Agents Tmentioning

confidence: 94%

“…Treatment of cultured cells with phorbol ester caused a parallel elevation in cellular DAG content and CCTa translocation to membranes [187]. Similarly, treatment of cell-cycle-arrested cells with serum [16] or angiotensin [188] generated multiple lipid mediators, including fatty acids and DAG, and augmented CCT activity and PC synthesis. These events could be blunted by inhibitors of select lipases.…”

Section: Cct Relocalization And/or Activation In Response To Agents Tmentioning

confidence: 99%

See 2 more Smart Citations

CTP:phosphocholine cytidylyltransferase: Function, regulation, and structure of an amphitropic enzyme required for membrane biogenesis

Cornell

Ridgway

2015

Progress in Lipid Research

Self Cite

118

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Section: Cct Relocalization And/or Activation In Response To Agents Tmentioning

confidence: 87%

Section: Cct Relocalization And/or Activation In Response To Agents Tmentioning

confidence: 94%

Section: Cct Relocalization And/or Activation In Response To Agents Tmentioning

confidence: 99%

See 1 more Smart Citation

CTP:phosphocholine cytidylyltransferase: Function, regulation, and structure of an amphitropic enzyme required for membrane biogenesis

Cornell

Ridgway

2015

Progress in Lipid Research

Self Cite

118

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“…A study that examined production of lipid activators during the G 0 -G 1 transition in IIC9 cells concluded that DAG was involved in CCTa activation (45). CCTa activation and cytoplasmic localization were also accompanied by increased DAG mass and lipin1 expression in differentiating B cells (26).…”

Section: Discussionmentioning

confidence: 99%

Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain

Gehrig

Morton

Ridgway

2009

Journal of Lipid Research

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CTP:phosphocholine cytidylyltransferase a (CCTa), the rate-limiting enzyme in the CDP-choline pathway for phosphatidylcholine (PtdCho) synthesis, is activated by translocation to nuclear membranes. However, CCTa is cytoplasmic in cells with increased capacity for PtdCho synthesis and following acute activation, suggesting that nuclear export is linked to activation. The objective of this study was to identify which CCTa domains were involved in nuclear export in response to the lipid activators farnesol (FOH) and oleate. Imaging of CCT-green fluorescent protein (GFP) mutants expressed in CCTa-deficient CHO58 cells showed that FOH-mediated translocation to nuclear membranes and export to the cytoplasm required the membrane binding amphipathic helix (domain M). Nuclear export was reduced by a mutation that mimics constitutive phosphorylation of the CCT phosphorylation (P) domain. However, domain M alone was sufficient to promote translocation to the nuclear envelope and export of a nuclearlocalized GFP construct in FOH-or oleate-treated CHO58 cells. In the context of acute activation with lipid mediators, nuclear export of CCT-GFP mutants correlated with in vitro activity but not PtdCho synthesis. This study describes a nuclear export pathway that is dependent on membrane interaction of an amphipathic helix, thus linking lipiddependent activation to the nuclear/cytoplasmic distribution of CCTa.-Gehrig, K., C. C. Morton, and N. D. Ridgway. Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain. J. Lipid Res. 2009. 50: 966-976.

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“…Ang II also stimulates a cellular mitogenic response via the AT 1 receptor. A recent report suggests that the ang II mitogenic effects might be mediated via ERK1/2 (Kitos et al, 2006). Although AT 1 receptors predominate in most of the tissues, AT 2 receptors are widely expressed in fetal tissue, uterus, adrenal medullary tissue and localized in discrete parts of the brain of various species, including humans Chung et al, 1996).…”

Section: Introductionmentioning

confidence: 98%

An update on non-peptide angiotensin receptor antagonists and related RAAS modulators

2007

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Contribution of lipid mediators to the regulation of phosphatidylcholine synthesis by angiotensin

Cited by 11 publications

References 62 publications

CTP:phosphocholine cytidylyltransferase: Function, regulation, and structure of an amphitropic enzyme required for membrane biogenesis

CTP:phosphocholine cytidylyltransferase: Function, regulation, and structure of an amphitropic enzyme required for membrane biogenesis

Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain

An update on non-peptide angiotensin receptor antagonists and related RAAS modulators

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