PLA2 promotes fusion between PMN-specific granules and complex liposomes

Blackwood, R. Alexander; Transue, Amy T.; Harsh, Donna M.; Brower, R. C.; Zacharek, Sima J.; Smolen, James E.; Hessler, Ronald J.

doi:10.1002/jlb.59.5.663

Cited by 29 publications

(23 citation statements)

References 7 publications

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“…Nagao et al (1995) reported that the fusion of parotid SGs with PMs, as measured by a fluorescence-dequenching assay with octadecyl rhodamine B, was induced when the PM fraction was pre-treated with PLA2. Similar results were reported in neutrophils and chromaffin cells (Creutz, 1981;Karli et al, 1990;Blackwood et al, 1996). PLA2 was also shown to increase ZG and chromaffin granule lysis (Izumi et al, 1986;Gasser and Holda, 1994).…”

Section: The Role Of Lipids/fusinogens In Membranesupporting

confidence: 83%

“…However, unlike AA, lysolipids appear to inhibit rather than promote fusion reactions (Chernomordik et al, 1993); these opposing effects have been shown to occur in the same cell type (Blackwood et al 1996). Because of these opposing effects, fusion mediated by lipid degradation products appears to be controversial in a physiologic context.…”

Section: The Role Of Lipids/fusinogens In Membranementioning

confidence: 99%

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GTP-Binding Proteins and Regulated Exocytosis

Watson

1999

Critical Reviews in Oral Biology & Medicine

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Regulated exocytosis, which occurs in response to stimuli, is a two-step process involving the docking of secretory granules (SGs) at specific sites on the plasma membrane (PM), with subsequent fusion and release of granule contents. This process plays a crucial role in a number of tissues, including exocrine glands, chromaffin cells, platelets, and mast cells. Over the years, our understanding of the proteins involved in vesicular trafficking has increased dramatically. Evidence from genetic, biochemical, immunological, and functional assays supports a role for ras-like monomeric GTP-binding proteins (smgs) as well as heterotrimeric GTP-binding protein (G-protein) subunits in various steps of the vesicular trafficking pathway, including the transport of secretory vesicles to the PM. Data suggest that the function of GTP-binding proteins is likely related to their localization to specific cellular compartments. The presence of both G-proteins and smgs on secretory vesicles/granules implicates a role for these proteins in the final stages of exocytosis. Molecular mechanisms of exocytosis have been postulated, with the identification of a number of proteins that modify, regulate, and interact with GTP-binding proteins, and with the advent of approaches that assess the functional importance of GTP-binding proteins in downstream, exocytotic events. Further, insight into vesicle targeting and fusion has come from the characterization of a SNAP receptor (SNARE) complex composed of vesicle, PM, and soluble membrane trafficking components, and identification of a functional linkage between GTP-binding and SNARES.

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Section: The Role Of Lipids/fusinogens In Membranesupporting

confidence: 83%

Section: The Role Of Lipids/fusinogens In Membranementioning

confidence: 99%

GTP-Binding Proteins and Regulated Exocytosis

Watson

1999

Critical Reviews in Oral Biology & Medicine

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“…Another prominent aspect of PLA 1 reactions is that their products, lysophospholipids, generally have an inverted cone shape with a bulky polar head and a smaller fatty acid moiety and, therefore, generate positive membrane curvature (55,56). A number of studies have suggested that phospholipid hydrolysis induces morphological changes of membranes in vitro including fusion (57)(58)(59). However, it remains to be determined whether lipidmetabolizing enzymes have such roles in vivo.…”

Section: Discussionmentioning

confidence: 99%

Intracellular Phospholipase A1γ (iPLA1γ) Is a Novel Factor Involved in Coat Protein Complex I- and Rab6-independent Retrograde Transport between the Endoplasmic Reticulum and the Golgi Complex

Morikawa

Aoki

Kano

et al. 2009

Journal of Biological Chemistry

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The mammalian intracellular phospholipase A 1 (iPLA 1 ) family consists of three members, iPLA 1 ␣/PA-PLA 1 , iPLA 1 ␤/p125, and iPLA 1 ␥/KIAA0725p. Although iPLA 1 ␤ has been implicated in organization of the ER-Golgi compartments, little is known about the physiological role of its closest paralog, iPLA 1 ␥. Here we show that iPLA 1 ␥ mediates a specific retrograde membrane transport pathway between the endoplasmic reticulum (ER) and the Golgi complex. iPLA 1 ␥ appeared to be localized to the cytosol, the cis-Golgi, and the ER-Golgi intermediate compartment (ERGIC). Time-lapse microscopy revealed that a population of GFP-iPLA 1 ␥ was associated with transport carriers moving out from the Golgi complex. Knockdown of iPLA 1 ␥ expression by RNAi did not affect the anterograde transport of VSVGts045 but dramatically delayed two types of Golgi-to-ER retrograde membrane transport; that is, transfer of the Golgi membrane into the ER in the presence of brefeldin A and delivery of cholera toxin B subunit from the Golgi complex to the ER. Notably, knockdown of iPLA 1 ␥ did not impair COPI-and Rab6-dependent retrograde transports represented by ERGIC-53 recycling and ER delivery of Shiga toxin, respectively. Thus, iPLA 1 ␥ is a novel membrane transport factor that contributes to a specific Golgi-to-ER retrograde pathway distinct from presently characterized COPI-and Rab6-dependent pathways.

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“…The potential role of phosphatidic acid (40) and arachidonic acid (41) formation on membrane fusion events has been previously examined using exogenous phospholipases. The augmentation of phospholipid vesicle fusion by ceramide-1-phosphate was verified by the conversion of sphingomyelin to ceramide-1-phosphate with sphingomyelinase D. This augmentation was observed when as little as 0.5% (1% of the outer membrane leaflet) was ceramide-1-phosphate, suggesting that ceramide-1-phosphate formation potentially may play a positive regulatory role in PMN granuleplasma membrane fusion.…”

Section: Figmentioning

confidence: 99%

The Formation of Ceramide-1-phosphate during Neutrophil Phagocytosis and Its Role in Liposome Fusion

Hinkovska‐Galcheva¹,

Boxer²,

Mansfield³

et al. 1998

Journal of Biological Chemistry

123

108

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Ceramide, a product of agonist-stimulated sphingomyelinase activation, is known to be generated during the phagocytosis of antibody-coated erythrocytes by polymorphonuclear leukocytes. Agonist-stimulated formation of ceramide-1-phosphate is now shown to occur in 32 PO 4 -labeled neutrophils. Ceramide-1-phosphate is formed by a calcium-dependent ceramide kinase, found predominately in the neutrophil plasma membrane. The neutrophil kinase is specific for ceramide because, in contrast to the bacterial diglyceride kinase, ceramide is not phosphorylated under conditions specific for diglyceride phosphorylation. Conversely, 1,2-diacylglycerol does not serve as substrate for the neutrophil ceramide kinase. Ceramide kinase activation occurs in a time-dependent fashion, reaching peak activity 10 min after formyl peptide stimulation and challenge with antibody-coated erythrocytes. The lipid kinase activity is optimal at pH 6.8. Because the formation of the phagolysosome is a critical event in phagocytosis, the effect of ceramide-1-phosphate in promoting the fusion of liposomes was determined. Both the addition of increasing concentrations of sphingomyelinase D and ceramide-1-phosphate promoted liposomal fusion. In summary, ceramide-1-phosphate is formed during phagocytosis through activation of ceramide kinase. Ceramide-1-phosphate may promote phagolysosome formation.

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PLA2 promotes fusion between PMN-specific granules and complex liposomes

Cited by 29 publications

References 7 publications

GTP-Binding Proteins and Regulated Exocytosis

GTP-Binding Proteins and Regulated Exocytosis

Intracellular Phospholipase A1γ (iPLA1γ) Is a Novel Factor Involved in Coat Protein Complex I- and Rab6-independent Retrograde Transport between the Endoplasmic Reticulum and the Golgi Complex

The Formation of Ceramide-1-phosphate during Neutrophil Phagocytosis and Its Role in Liposome Fusion

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