Interfacial activation, lysophospholipase and transacylase activity of Group VI Ca2+-independent phospholipase A2

Lio, Yi-Ching; Dennis, Edward A.

doi:10.1016/s0005-2760(98)00049-6

Cited by 93 publications

(90 citation statements)

References 51 publications

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“…Indeed, our studies demonstrated that 1 mM ATP or 1 mM ADP increases the subunit stoichiometry of IPLA-1 complexes, although the larger homo-oligomers remain labile and appear to disassemble during the course of glycerol gradient sedimentation experiments, which require 8 h of centrifugation time. Previous work suggested that ATP may not directly activate iPLA 2 isoforms but instead may limit its denaturation during an enzymatic assay (48). Our data are consistent with this idea but further argue that ATP and ADP promote iPLA 2 self-association.…”

Section: Discussionsupporting

confidence: 91%

Roles of Acidic Phospholipids and Nucleotides in Regulating Membrane Binding and Activity of a Calcium-independent Phospholipase A2 Isoform

Morrison

Witte

Mayers

et al. 2012

Journal of Biological Chemistry

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Background: Ca 2ϩ -independent phospholipase A 2 (iPLA 2 ) isoforms mediate the deacylation of phospholipids. Results: Acidic phospholipids and nucleotides associate with the C. elegans iPLA 2 isoform IPLA-1 and modulate its activity. Conclusion: Acidic phospholipids and nucleotides play important roles in regulating iPLA 2 function by enhancing membrane recruitment and promoting enzyme oligomerization. Significance: These findings highlight new regulatory mechanisms that control iPLA 2 function.

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Section: Discussionsupporting

confidence: 91%

Roles of Acidic Phospholipids and Nucleotides in Regulating Membrane Binding and Activity of a Calcium-independent Phospholipase A2 Isoform

Morrison

Witte

Mayers

et al. 2012

Journal of Biological Chemistry

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“…Saturated or monounsaturated fatty acids at the sn-2 position of PE may be preferentially hydrolyzed by the PLA 2 activity of cPLA 2 ␥, and the derived lysoPE may be reacylated with PUFA by other enzymes with acyltransferase activities. Alternatively, cPLA 2 ␥ may have transacylase or acyltransferase activity in itself, as in the case of other PLA 2 s (28,29). Lysophospholipase activity of cPLA 2 ␥ (21) may also contribute to the remodeling of the phospholipids.…”

Section: Discussionmentioning

confidence: 99%

Human Group IVC Phospholipase A2(cPLA2γ)

Asai

Hirabayashi

Houjou

et al. 2003

Journal of Biological Chemistry

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To create the unique properties of a certain cellular membrane, both the composition and the metabolism of membrane phospholipids are key factors. Phospholipase A 2 (PLA 2 ), with hydrolytic enzyme activities at the sn-2 position in glycerophospholipids, plays critical roles in maintaining the phospholipid composition as well as producing bioactive lipid mediators. In this study we examined the contribution of a Ca 2؉ -independent group IVC PLA 2 isozyme (cPLA 2 ␥), a paralogue of cytosolic PLA 2 ␣ (cPLA 2 ␣), to phospholipid remodeling. The enzyme was localized in the endoplasmic reticulum and Golgi apparatus, as seen using green fluorescence fusion proteins. Electrospray ionization mass spectrometric analysis of membrane extracts revealed that overexpression of cPLA 2 ␥ increased the proportion of polyunsaturated fatty acids in phosphatidylethanolamine, suggesting that the enzyme modulates the phospholipid composition. We also found that H 2 O 2 and other hydroperoxides induced arachidonic acid release in cPLA 2 ␥-transfected human embryonic kidney 293 cells, possibly through the tyrosine phosphorylation pathway. Thus, we propose that cPLA 2 ␥ is constitutively expressed in the endoplasmic reticulum and plays important roles in remodeling and maintaining membrane phospholipids under various conditions, including oxidative stress.

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“…Unlike cPLA 2 , which exhibits preference for hydrolysis of AA from the sn -2 position ( 89 ), the iPLA 2 s demonstrate no substrate specifi city and manifest PLA 2 /PLA 1 , lysophospholipase ( 90,91 ), transacylase ( 27,91 ), and thioesterase ( 92,93 ) activities. The extensively studied iPLA 2 ␤ was PUFAs from the sn -2 position, as refl ected by generation of 2-arachidonoyl LPC at a 10-fold faster rate than 1-palmitoyl LPC ( 69 ).…”

mentioning

confidence: 99%

“…The iPLA 2 ␤ protein contains a consensus nucleotide-binding motif (GGGVKG) that is homologous to those of protein kinases ( 61,116 ). This feature mediates regulation and stabilization of iPLA 2 ␤ activity by ATP ( 6, 91,117,118 ), which is independent of enzyme phosphorylation ( 6, 117, 118 ). Also contained in iPLA 2 ␤ are a C-terminal 1-9-14 calmodulin-binding motif (IRKGQGNKVKK LSI) and a calmodulin-binding peptide (AWSEMVGIQYFR) ( 106,116,119 ).…”

mentioning

confidence: 99%

Calcium-independent phospholipases A2 and their roles in biological processes and diseases

Ramanadham

Ali

Ashley

et al. 2015

Journal of Lipid Research

167

190

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The Ca 2+ -independent phospholipases A 2 (iPLA 2 s) are part of a diverse family of PLA 2 s that hydrolyze the sn -2 substituent from membrane phospholipids to release a free fatty acid and a lysolipid ( 1, 2 ). These enzymes are ubiquitously expressed, and in contrast to secretory PLA 2 s (sPLA 2 s) and cytosolic PLA 2 s (cPLA 2 s), do not require Ca 2+ for either translocation or activity. Some of the fi rst descriptions of iPLA 2 activity were in the mid-to late-1980s with the identifi cation of a plasmalogen-selective PLA 2 in Abstract Among the family of phospholipases A 2 (PLA 2 s) are the Ca 2+ -independent PLA 2 s (iPLA 2 s) and they are designated group VI iPLA 2 s. In relation to secretory and cytosolic PLA 2 s, the iPLA 2 s are more recently described and details of their expression and roles in biological functions are rapidly emerging. The iPLA 2 s or patatin-like phospholipases (PNPLAs) are intracellular enzymes that do not require Ca 2+ for activity, and contain lipase (GXSXG) and nucleotide-binding (GXGXXG) consensus sequences. Though nine PNPLAs have been recognized, PNPLA8 (membraneassociated iPLA 2 ␥ ) and PNPLA9 (cytosol-associated iPLA 2 ␤ ) are the most widely studied and understood. The iPLA 2 s manifest a variety of activities in addition to phospholipase, are ubiquitously expressed, and participate in a multitude of biological processes, including fat catabolism, cell differentiation, maintenance of mitochondrial integrity, phospholipid remodeling, cell proliferation, signal transduction, and cell death. As might be expected, increased or decreased expression of iPLA 2 s can have profound effects on the metabolic state, CNS function, cardiovascular performance, and cell survival; therefore, dysregulation of iPLA 2 s can be a critical factor in the development of many diseases. This review is aimed at providing a general framework of the current understanding of the iPLA 2 s and discussion of the potential mechanisms of action of the iPLA 2 s and related involved lipid mediators. -Ramanadham, S

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Interfacial activation, lysophospholipase and transacylase activity of Group VI Ca2+-independent phospholipase A2

Cited by 93 publications

References 51 publications

Roles of Acidic Phospholipids and Nucleotides in Regulating Membrane Binding and Activity of a Calcium-independent Phospholipase A2 Isoform

Roles of Acidic Phospholipids and Nucleotides in Regulating Membrane Binding and Activity of a Calcium-independent Phospholipase A2 Isoform

Human Group IVC Phospholipase A2(cPLA2γ)

Calcium-independent phospholipases A2 and their roles in biological processes and diseases

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