Phospholipid transfer proteins in mammalian lung

Lumb, Roger H.

doi:10.1152/ajplung.1989.257.4.l190

Cited by 10 publications

(11 citation statements)

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“…Intermembrane transport of PC and PG is significantly elevated in type II epithelial cells relative to whole lung and transfer activity increases commensurate with surfactant synthesis before birth (38,63). Intracellular phospholipid transport activity was generally attributed to phospholipid transfer proteins and to PC-TP/StarD2 in particular.…”

Section: Intracellular Trafficking Of Surfactant Phospholipidsmentioning

confidence: 99%

Pulmonary Surfactant Pathophysiology: Current Models and Open Questions

2010

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Pulmonary surfactant is an essential lipid-protein complex that stabilizes the respiratory units (alveoli) involved in gas exchange. Quantitative or qualitative derangements in surfactant are associated with severe respiratory pathologies. The integrated regulation of surfactant synthesis, secretion, and metabolism is critical for air breathing and, ultimately, survival. The goal of this review is to summarize our current understanding and highlight important knowledge gaps in surfactant homeostatic mechanisms.

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Section: Intracellular Trafficking Of Surfactant Phospholipidsmentioning

confidence: 99%

Pulmonary Surfactant Pathophysiology: Current Models and Open Questions

2010

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“…It has been postulated that the movement of phospholipids between membranes may be facilitated by phospholipid transfer proteins, several of which have been localized to mammalian lung (5,6). However, the exact role of these transporters and their specificity for different phospholipids are unknown.…”

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confidence: 99%

“…Although there is evidence for the presence of phospholipid transfer proteins within the alveolar type-II cells (5,6), their exact role in the trafficking of phospholipids is unknown. The predicted structure of the ABCA3 protein is similar to that of other ABC proteins (7,23,24).…”

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Surfactant Composition and Function in Patients with ABCA3 Mutations

et al. 2006

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Mutations in the gene encoding the ATP binding cassette transporter member A3 (ABCA3) are associated with fatal surfactant deficiency. ABCA3 lines the limiting membrane of lamellar bodies within alveolar type-II cells, suggesting a role in surfactant metabolism. The objective of this study was to determine the surfactant phospholipid composition and function in patients with mutations in the ABCA3 gene. Bronchoalveolar lavage (BAL) fluid was analyzed from three groups of infants: 1) Infants with ABCA3 mutations, 2) infants with inherited surfactant protein-B deficiency (SP-B), and 3) patients without parenchymal lung disease (CON). Surfactant phospholipid profile was determined using twodimensional thin-layer chromatography, and surface tension was measured with a pulsating bubble surfactometer. Phosphatidylcholine comprised 41 Ϯ 19% of the total phospholipid in the BAL fluid of the ABCA3 group compared with 78 Ϯ 3% and 68 Ϯ 18%, p ϭ 0.008 and 0.05, of the CON and SP-B groups, respectively. Surface tension was 31.5 Ϯ 9.3 mN/m and was significantly greater than CON but no different from SP-B. We conclude that mutations in ABCA3 are associated with surfactant that is deficient in phosphatidylcholine and has decreased function, suggesting that ABCA3 plays an important role in pulmonary surfactant phospholipid homeostasis. (Pediatr Res 59: [801][802][803][804][805] 2006)

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“…These proteins are possibly present in soluble form although their association with membranes or specific organelles cannot be excluded. In type II cells also, several proteins have been postulated to mediate transfer of surfactant phospholipids, PC, DSPC, and PG, to lamellar bodies (7,36). Because methylamine decreased the packaging of all three phospholipids to a similar extent (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…One of these involves molecular transfer of phospholipids through phospholipid transfer proteins (5), which also are present in type II cells, where they are suggested to mediate transfer of PC, DSPC, and PG to lamellar bodies (reviewed in Ref. 7). Another mechanism for transfer of phospholipids (and proteins) may involve vesicle trafficking from the site of synthesis to the targeted membrane (8)(9)(10).…”

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Coordinate packaging of newly synthesized phosphatidylcholine and phosphatidylglycerol in lamellar bodies in alveolar type II cells

Chander

Sen

Wadsworth

et al. 2000

Lipids

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Methylamine, a weak base, inhibits packaging of newly synthesized phosphatidylcholine (PC) in lamellar bodies in 20-22 h cultured alveolar type II cells, suggesting a role for acidic pH of lamellar bodies. In this study, we tested if (i) the packaging of PC is similarly regulated in freshly isolated type II cells and (ii) methylamine also inhibits the packaging of other surfactant phospholipids, particularly, phosphatidylglycerol (PG). The latter would suggest coordinated packaging so as to maintain the phospholipid composition of lung surfactant. During the short-term metabolic labeling experiments in freshly isolated type II cells, methylamine treatment decreased the incorporation of radioactive precursors into PC, disaturated PC (DSPC), and PG of lamellar bodies but not of the microsomes, when compared with controls. The calculated packaging (the percentage of microsomal lipid packaged in lamellar bodies) of each phospholipid was similarly decreased (approximately 50%) in methylamine-treated cells, suggesting coordinated packaging of surfactant phospholipids in lamellar bodies. Equilibrium-labeling studies with freshly isolated type II cells (as is routinely done for studies on surfactant secretion) +/- methylamine showed that in methylamine-treated cells, the secretion of PC and PG was decreased (possibly due to decreased packaging), but the phospholipid composition of released surfactant (measured by radioactivity distribution) was unchanged; and the PC content (measured by mass or radioactivity) of lamellar bodies was lower, but the PC composition (as percentage of total phospholipids) was unchanged when compared with control cells. We speculate that the newly synthesized surfactant phospholipids, PC, DSPC, and PG, are coordinately transported into lamellar bodies by a mechanism requiring the acidic pH, presumably, of lamellar bodies.

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Phospholipid transfer proteins in mammalian lung

Cited by 10 publications

References 0 publications

Pulmonary Surfactant Pathophysiology: Current Models and Open Questions

Pulmonary Surfactant Pathophysiology: Current Models and Open Questions

Surfactant Composition and Function in Patients with ABCA3 Mutations

Coordinate packaging of newly synthesized phosphatidylcholine and phosphatidylglycerol in lamellar bodies in alveolar type II cells

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