Lung annexin II promotes fusion of isolated lamellar bodies with liposomes

Liu, Lin; Fisher, Aron B.; Zimmerman, Un‐Jin P.

doi:10.1016/0005-2760(95)00159-a

Cited by 32 publications

(43 citation statements)

References 37 publications

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“…1A). Annexin II exists in alveolar type II cells and is involved in lung surfactant secretion (13,33). To test directly whether annexin II is the protein responsible for the type II cell cytosol-mediated fusion, we removed annexin II from type II cell cytosol by immunoprecipitation using affinitypurified anti-annexin II antibodies.…”

Section: Resultsmentioning

confidence: 99%

“…Our plasma membrane preparation used for the fusion assay contained 1.6 g of lipid/g of proteins as determined by the method of Stewart (39). The lipid/protein ratio of lamellar body limiting membrane is 1.5 (w/w) (13). Interestingly, a robust increase was observed in the absence of AIIt when AA-LB and AA-PM were used for membrane fusion assay.…”

Section: Table I Effect Of Different Inhibitors On Aiit-mediated Membmentioning

confidence: 99%

“…It has been implicated in Ca 2ϩ -dependent membrane fusion during exocytosis in a variety of cells including chromaffin cells and alveolar type II cells (12)(13)(14). Annexin II binds to negatively charged phospholipids and mediates the aggregation and fusion of liposomes in the presence of Ca 2ϩ (13,15). Annexin II exists as a monomer (AIIm, 1 36-kDa) or heterotetramer (AIIt, two AIIm plus two 11-kDa subunits) (10).…”

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confidence: 99%

“…Cholesterol also alters the subcellular localization of AIIt at low Ca 2ϩ concentrations (25,26). Arachidonic acid enhances AIIt-mediated fusion in model membranes (13). The mechanisms are not clear, but arachidonic acid itself acts as a fusogen (27)(28)(29).…”

mentioning

confidence: 99%

“…‡ To whom correspondence should be addressed: We have shown previously that AIIt can promote the fusion of lamellar bodies with liposomes, and this fusion is dependent on the composition of liposomes (13). Other groups also used liposomes to mimic granule membrane or plasma membrane (10,15,16,21,22,25).…”

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Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Chattopadhyay

Sun

Wang

et al. 2003

Journal of Biological Chemistry

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Annexin II has been implicated in membrane fusion during the exocytosis of lamellar bodies from alveolar epithelial type II cells. Most previous studies were based on the fusion assays by using model membranes. In the present study, we investigated annexin II-mediated membrane fusion by using isolated lamellar bodies and plasma membrane as determined by the relief of octadecyl rhodamine B (R18) self-quenching. Immunodepletion of annexin II from type II cell cytosol reduced its fusion activity. Purified annexin II tetramer (AIIt) induced the fusion of lamellar bodies with the plasma membrane in a dose-dependent manner. This fusion is Ca 2؉ -dependent and is highly specific to AIIt because other annexins (I and II monomer, III, IV, V, and VI) were unable to induce the fusion. Modification of the different functional residues of AIIt by N-ethylmaleimide, nitric oxide, or peroxynitrite abolished AIIt-mediated fusion. Arachidonic acid enhanced AIIt-mediated fusion and reduced its Ca 2؉ requirement to an intracellularly achievable level. This effect is due to membranebound arachidonic acid, not free arachidonic acid. Other fatty acids including linolenic acid, palmitoleic acid, myristoleic acid, stearic acid, palmitic acid, and myristic acid had little effect. AIIt-mediated fusion was suppressed by the removal of arachidonic acid from lamellar body and plasma membrane using bovine serum albumin. The addition of arachidonic acid back to the arachidonic acid-depleted membranes restored its fusion activity. Our results suggest that the fusion between lamellar bodies with the plasma membrane is driven by the synergistic action of AIIt and arachidonic acid.Lung surfactant is a surface active material synthesized and secreted by cuboidal alveolar type II cells (1-3). It is composed of phospholipids, mainly dipalmitoylphosphatidylcholine, and surfactant proteins A-D. It minimizes the surface tension at the air-liquid interface by inserting phospholipids between water molecules. As a result, surfactant disrupts the cohesive hydrogen bonds and prevents them from exerting high molecular forces at the alveolar surface. Deficiency of dipalmitoylphosphatidylcholine in the alveolar surface has been associated with infant respiratory distress syndrome.The secretion of surfactant by type II cells involves the translocation, docking, and fusion of lamellar bodies to the plasma membrane. For the lamellar body content to reach its extracellular destination, a continuity of the vesicular lumen and extracellular fluid must be established. This continuity is maintained through the formation of a narrow pore similar to membrane channels (4 -6). The formation of this pore is a complex event involving physical and chemical factors and is regulated by intracellular Ca 2ϩ and proteins (7). Studies on mast cells and chromaffin cells revealed that the opening of fusion pore and extrusion of granule content is influenced by an osmotic force depending upon the osmolarity of the surrounding solution (8).Annexin II plays multidimensional roles in dif...

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Section: Resultsmentioning

confidence: 99%

Section: Table I Effect Of Different Inhibitors On Aiit-mediated Membmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Chattopadhyay

Sun

Wang

et al. 2003

Journal of Biological Chemistry

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Regulation of lung surfactant secretion by phospholipase A2

Liu

1999

J. Cell. Biochem.

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Arachidonic acid has been shown to stimulate lung surfactant secretion from alveolar epithelial type II cells. To identify the (phospho)lipases responsible for generating arachidonic acid during lung surfactant secretion, the effects of various (phospho)lipase inhibitors on phosphatidylcholine (PC) secretion from rat alveolar type II cells were investigated. N-(p-amylcinnamoyl)anthranilic acid (ACA), a general inhibitor of phsopholipase A2 (PLA2), inhibited ATP-stimulated PC secretion in a dose-dependent manner. ACA also blocked PC secretion from type II cells stimulated by other secretagogues including phorbol 12-myristate 13-acetate, Ca2+ ionophore A23187 and terbutaline, indicating that PLA2 acts at a late step distal to the generation of second messengers. To determine which PLA2 isoform(s) is involved in lung surfactant secretion, selective inhibitors to different types of PLA2 were used to inhibit PLA2 activity in type II cells. The cytosolic PLA2 (cPLA2) inhibitor, arachidonyl trifluoromethyl ketone, was found to inhibit ATP-stimulated PC secretion, whereas the secretory PLA2 inhibitors, oleoyloxyethylphosphocholine, aristolochic acid, or p-bromophenacyl bromide, and the Ca2+-independent PLA2 inhibitors, palmitoyl trifluoromethyl ketone, or haloenol lactone suicide substrate, had no effect. In addition to PLA2, arachidonic acid is released from diacylglycerol (DAG) by DAG and monoacylglycerol lipases. The DAG lipase inhibitor, RHC-80267 also blocked ATP-stimulated PC secretion. The results suggest that both pathways for generating arachidonic acid via cPLA2 and DAG lipase may participate in lung surfactant secretion.

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Micro‐RNA‐375 inhibits lung surfactant secretion by altering cytoskeleton reorganization

et al. 2009

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SummaryLung surfactant is secreted via exocytosis of lamellar bodies from alveolar epithelial type II cells. Whether micro-RNAs regulate lung surfactant secretion is unknown. Micro-RNA-375 (miR-375) has been shown to be involved in insulin secretion. In this article, we report that the overexpression of miR-375 inhibited lung surfactant secretion. However, miR-125a, miR30a, miR-1, miR-382 and miR-101 did not influence lung surfactant secretion. miR-375 had no effects on surfactant synthesis or the formation of lamellar bodies. However, miR-375 did abolish the lung surfactant secretagogue-induced disassembly and reassembly of cytoskeleton. Our results suggest that miR-375 regulates surfactant secretion via the reorganization of cytoskeleton.2009 IUBMB IUBMB Life, 62(1): [78][79][80][81][82][83] 2010

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Lung annexin II promotes fusion of isolated lamellar bodies with liposomes

Cited by 32 publications

References 37 publications

Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Regulation of lung surfactant secretion by phospholipase A2

Micro‐RNA‐375 inhibits lung surfactant secretion by altering cytoskeleton reorganization

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