Role of Lipid Polymorphism in Pulmonary Surfactant

Perkins, Walter R.; Dause, Richard B.; Parente, Roberta A.; Minchey, Sharma R.; Neuman, Keir C.; Grüner, Sol M.; Taraschi, Theodore F.; Janoff, Andrew S.

doi:10.1126/science.273.5273.330

Cited by 75 publications

(50 citation statements)

References 27 publications

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“…It has been proposed, for example, that the inverted H II phase promotes interfacial surfactant adsorption (49) and that hydrophobic surfactant proteins favor highly curved lipid organizations, such as cubic and H II phases (50,51). Moreover, certain lipid systems enriched in phosphatidylethanolamine and cholesterol adopt non-lamellar phases under conditions of limited hydration (52).…”

Section: Discussionmentioning

confidence: 99%

Transient Exposure of Pulmonary Surfactant to Hyaluronan Promotes Structural and Compositional Transformations into a Highly Active State

López-Rodríguez

Cruz

Richter

et al. 2013

Journal of Biological Chemistry

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Background: Pulmonary surfactant is inactivated under pathological conditions, making clinical surfactants fail in respiratory therapies. Results: Exposure to a hyaluronan meshwork modifies the structure and composition of surfactant. Conclusion: Transient exposure of surfactant to hyaluronan leads to a higher resistance to inactivation. Significance: Understanding the effects of polymers as additives in surfactant will allow the development of new therapeutic options.

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Section: Discussionmentioning

confidence: 99%

Transient Exposure of Pulmonary Surfactant to Hyaluronan Promotes Structural and Compositional Transformations into a Highly Active State

López-Rodríguez

Cruz

Richter

et al. 2013

Journal of Biological Chemistry

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“…The H II -prone phospholipid PE has been shown to accumulate at the cleavage furrow, during eukaryotic cell division (Emoto et al, 1996), and in Escherichia coli it exhibits a chaperone-like activity (Bogdanov et al, 1996). Indeed, PE is required for the membrane packaging of integral proteins (de Kruijff, 1997), and it has also been used for biomedical and biotechnological purposes (Landau and Rosenbusch, 1996;Perkins et al, 1996;Zelphati and Szoka, 1996). The high proportion of this phospholipid in membranes and the precise regulation of its levels indicate that the hexagonal phase propensity is of great functional importance (Wieslander et al, 1986;Goldfine et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Influence of the Membrane Lipid Structure on Signal Processing via G Protein-Coupled Receptors

Yang¹,

Alemany²,

Casas³

et al. 2005

Molecular Pharmacology

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We have recently reported that lipid structure regulates the interaction with membranes, recruitment to membranes, and distribution to membrane domains of heterotrimeric G␣␤␥ proteins, G␣ subunits, and G␤␥ dimers (J Biol Chem 279: 36540 -36545, 2004). Here, we demonstrate that modulation of the membrane structure not only determines G protein localization but also regulates the function of G proteins and related signaling proteins. In this context, the antitumor drug daunorubicin (daunomycin) and oleic acid changed the membrane structure and inhibited G protein activity in biological membranes. They also induced marked changes in the activity of the ␣ 2A/Dadrenergic receptor and adenylyl cyclase. In contrast, elaidic and stearic acid did not change the activity of the abovementioned proteins. These fatty acids are chemical but not structural analogs of oleic acid, supporting the structural basis of the modulation of membrane lipid organization and subsequent regulation of G protein-coupled receptor signaling. In addition, oleic acid (and also daunorubicin) did not alter G protein activity in a membrane-free system, further demonstrating the involvement of membrane structure in this signal modulation. The present work also unravels in part the molecular bases involved in the antihypertensive (Hypertension 43: 249 -254, 2004) and anticancer (Mol Pharmacol 67:531-540, 2005) activities of synthetic oleic acid derivatives (e.g., 2-hydroxyoleic acid) as well as the molecular bases of the effects of diet fats on human health.

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“…This effect is due either to the coexistence of lamellar and nonlamellar structures (18) or to the increased H II propensity. When the same PE species were mixed with egg PC, instead of DPPC, a similar enhancement of G␣i binding was observed (data not shown).…”

Section: Effect Of Pe On the Binding Of G␣i To Model Membranesmentioning

confidence: 99%

Role of lipid polymorphism in G protein-membrane interactions: Nonlamellar-prone phospholipids and peripheral protein binding to membranes

Escribá

Ozaita

Ribas

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

106

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Heterotrimeric G proteins (peripheral proteins) conduct signals from membrane receptors (integral proteins) to regulatory proteins localized to various cellular compartments. They are in excess over any G protein-coupled receptor type on the cell membrane, which is necessary for signal amplification. These facts account for the large number of G protein molecules bound to membrane lipids. Thus, the protein-lipid interactions are crucial for their cellular localization, and consequently for signal transduction. In this work, the binding of G protein subunits to model membranes (liposomes), formed with defined membrane lipids, has been studied. It is shown that although G protein ␣-subunits were able to bind to lipid bilayers, the presence of nonlamellarprone phospholipids (phosphatidylethanolamines) enhanced their binding to model membranes. This mechanism also appears to be used by other (structurally and functionally unrelated) peripheral proteins, such as protein kinase C and the insect protein apolipophorin III, indicating that it could constitute a general mode of protein-lipid interactions, relevant in the activity and translocation of some peripheral (amphitropic) proteins from soluble to particulate compartments. Other factors, such as the presence of cholesterol or the vesicle surface charge, also modulated the binding of the G protein subunits to lipid bilayers. Conversely, the binding of G protein-coupled receptor kinase 2 and the G protein ␤-subunit to liposomes was not increased by hexagonally prone lipids. Their distinct interactions with membrane lipids may, in part, explain the different cellular localizations of all of these proteins during the signaling process.

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Role of Lipid Polymorphism in Pulmonary Surfactant

Cited by 75 publications

References 27 publications

Transient Exposure of Pulmonary Surfactant to Hyaluronan Promotes Structural and Compositional Transformations into a Highly Active State

Transient Exposure of Pulmonary Surfactant to Hyaluronan Promotes Structural and Compositional Transformations into a Highly Active State

Influence of the Membrane Lipid Structure on Signal Processing via G Protein-Coupled Receptors

Role of lipid polymorphism in G protein-membrane interactions: Nonlamellar-prone phospholipids and peripheral protein binding to membranes

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