Relevant bibliographies by topics / Protein-Surfactant /Lipid Bioconjugate Formation

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Academic literature on the topic 'Protein-Surfactant /Lipid Bioconjugate Formation'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Protein-Surfactant /Lipid Bioconjugate Formation"

1

Creuwels, Lambert A. J. M., Lambert M. G. van Golde, and Henk P. Haagsman. "Surfactant protein B: effects on lipid domain formation and intermembrane lipid flow." Biochimica et Biophysica Acta (BBA) - Biomembranes 1285, no. 1 (November 1996): 1–8. http://dx.doi.org/10.1016/s0005-2736(96)00131-9.

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2

Qanbar, R., S. Cheng, F. Possmayer, and S. Schurch. "Role of the palmitoylation of surfactant-associated protein C in surfactant film formation and stability." American Journal of Physiology-Lung Cellular and Molecular Physiology 271, no. 4 (October 1, 1996): L572—L580. http://dx.doi.org/10.1152/ajplung.1996.271.4.l572.

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The effect of palmitoylation of pulmonary surfactant-associated protein C (SP-C) on the surface activity of phospholipid mixtures of dipalmitoylphosphatidylcholine and phosphatidylglycerol was studied. Phospholipids reconstituted with palmitoylated or depalmitoylated bovine SP-C were examined at neutral and acidic pH using a captive bubble surfactometer. At low pH, effective lipid adsorption and near zero surface tensions upon compression were obtained even with protein-free samples. At physiological pH, only SP-C-containing samples achieved such properties. Lipid adsorption was decreased by prior SP-C depalmitoylation. Bubbles with palmitoylated SP-C were more mechanically stable and required less compression to reach low surface tensions. Subphase depletion experiments showed that dynamically cycled surface layers containing palmitoylated SP-C maintained their surface activity after subphase lipid depletion. In contrast, surface activity was rapidly lost where depalmitoylated SP-C or SP-B was included. Our results indicate that although SP-C palmitoylation has little effect on its ability to enhance lipid adsorption and surface tension reduction, it greatly enhances lipid respreading and film stability and is therefore important for surfactant function.
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3

Palaniyar, Nades, Ross A. Ridsdale, Stephen A. Hearn, Fred Possmayer, and George Harauz. "Formation of membrane lattice structures and their specific interactions with surfactant protein A." American Journal of Physiology-Lung Cellular and Molecular Physiology 276, no. 4 (April 1, 1999): L642—L649. http://dx.doi.org/10.1152/ajplung.1999.276.4.l642.

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Biological membranes exist in many forms, one of which is known as tubular myelin (TM). This pulmonary surfactant membranous structure contains elongated tubes that form square lattices. To understand the interaction of surfactant protein (SP) A and various lipids commonly found in TM, we undertook a series of transmission-electron-microscopic studies using purified SP-A and lipid vesicles made in vitro and also native surfactant from bovine lung. Specimens from in vitro experiments were negatively stained with 2% uranyl acetate, whereas fixed native surfactant was delipidated, embedded, and sectioned. We found that dipalmitoylphosphatidylcholine-egg phosphatidylcholine (1:1 wt/wt) bilayers formed corrugations, folds, and predominantly 47-nm-square latticelike structures. SP-A specifically interacted with these lipid bilayers and folds. We visualized other proteolipid structures that could act as intermediates for reorganizing lipids and SP-As. Such a reorganization could lead to the localization of SP-A in the lattice corners and could explain, in part, the formation of TM-like structures in vivo.
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4

Johansson, J. "Membrane properties and amyloid fibril formation of lung surfactant protein C." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 601–6. http://dx.doi.org/10.1042/bst0290601.

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Pulmonary surfactant is essential for respiration and lung host defence and is composed of 80–90% lipids, mainly dipalmitoylphosphatidylcholine (DPPC). Surfactant protein C (SP-C) constitutes 1–2 % of the surfactant mass, and is one of the most hydrophobic peptides yet isolated. SP-C residues 9–34 form an α-helix with a central poly-valine segment, which perfectly matches the thickness of a fluid DPPC bilayer. The palmitoyl groups linked to Cys-5 and Cys-6 of SP-C increase the capacity of the peptide to promote lipid adsorption at an air/liquid interface, and augment the mechanical stability of SP-C/lipid mixtures. SP-C undergoes α-helix → β-sheet transition and forms amyloid fibrils. NMR and MS studies show that the poly-valine helix is kinetically stabilized, and that once it unfolds, formation of β-sheet aggregates is significantly faster than refolding. α-Helix unfolding is accelerated after removal of the palmitoyl groups. Secondary structure prediction of SP-C yields β-strand conformation of the poly-valine part. A database search revealed similar discordance between experimentally determined helices and predicted β-strands for other amyloid-forming proteins, including the prion protein associated with spongiform encephalopathies, and the amyloid-β (Aβ) peptide associated with Alzheimer's disease. For Aβ and SP-C, removal of the helix/strand discordance by residue replacements abrogates fibril formation in vitro.
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5

Krol, Silke, Michaela Ross, Manfred Sieber, Stephanie Künneke, Hans-Joachim Galla, and Andreas Janshoff. "Formation of Three-Dimensional Protein-Lipid Aggregates in Monolayer Films Induced by Surfactant Protein B." Biophysical Journal 79, no. 2 (August 2000): 904–18. http://dx.doi.org/10.1016/s0006-3495(00)76346-6.

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6

Pérez-Gil, Jesus, Jacqueline Tucker, Gary Simatos, and Kevin M. W. Keough. "Interfacial adsorption of simple lipid mixtures combined with hydrophobic surfactant protein from pig lung." Biochemistry and Cell Biology 70, no. 5 (May 1, 1992): 332–38. http://dx.doi.org/10.1139/o92-051.

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Hydrophobic pulmonary surfactant protein enriched in SP-C has been mixed in amounts up to 10% by weight with various phospholipids. The lipids used were dipalmitoyl phosphatidylcholine (DPPC), or DPPC plus unsaturated phosphatidylglycerol (PG), or phosphatidylinositol (PI) in molar ratios of 9:1 and 7:3. The protein enhanced the rate and extent of adsorption of each lipid preparation into the air–water interface, and its respreading after compression on a surface balance. Maximum surface pressures attained on compression of monolayers of mixtures of lipids were slightly higher in the presence of protein. The effects on rate and extent of adsorption were proportional to the amount of protein present. Mixtures containing 30 mol% PG or PI adsorbed more readily into the interface than those containing 10% acidic lipid or DPPC alone. Mixtures containing 30% PI were slightly more rapidly adsorbed than those containing 30% PG. The results suggest that mixtures of DPPC with either acidic lipid in the presence of surfactant protein could be effective in artificial surfactants.Key words: pulmonary surfactant, monolayer formation, adsorption, synthetic surfactant, proteolipids.
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7

Bates, Sandra R., Jian-Qin Tao, Kathleen Notarfrancesco, Kristine DeBolt, Henry Shuman, and Aron B. Fisher. "Effect of surfactant protein A on granular pneumocyte surfactant secretion in vitro." American Journal of Physiology-Lung Cellular and Molecular Physiology 285, no. 5 (November 2003): L1055—L1065. http://dx.doi.org/10.1152/ajplung.00271.2002.

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Surfactant secretion by lung type II cells occurs when lamellar bodies (LBs) fuse with the plasma membrane and surfactant is released into the alveolar lumen. Surfactant protein A (SP-A) blocks secretagogue-stimulated phospholipid (PL) release, even in the presence of surfactant-like lipid. The mechanism of action is not clear. We have shown previously that an antibody to LB membranes (MAb 3C9) can be used to measure LB membrane trafficking. Although the ATP-stimulated secretion of PL was blocked by SP-A, the cell association of iodinated MAb 3C9 was not altered, indicating no effect on LB movement. FM1-43 is a hydrophobic dye used to monitor the formation of fusion pores. After secretagogue exposure, the threefold enhancement of the number of FM1-43 fluorescent LBs (per 100 cells) was not altered by the presence of SP-A. Finally, there was no evidence of a large PL pool retained on the cell surface through interaction with SP-A. Thus SP-A exposure does not affect these stages in the surfactant secretory pathway of type II cells.
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8

Palaniyar, Nades, Ross A. Ridsdale, Stephen A. Hearn, Yew Meng Heng, F. Peter Ottensmeyer, Fred Possmayer, and George Harauz. "Filaments of surfactant protein A specifically interact with corrugated surfaces of phospholipid membranes." American Journal of Physiology-Lung Cellular and Molecular Physiology 276, no. 4 (April 1, 1999): L631—L641. http://dx.doi.org/10.1152/ajplung.1999.276.4.l631.

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Pulmonary surfactant, a mixture of lipids and surfactant proteins (SPs), plays an important role in respiration and gas exchange. SP-A, the major SP, exists as an octadecamer that can self-associate to form elongated protein filaments in vitro. We have studied here the association of purified bovine SP-A with lipid vesicle bilayers in vitro with negative staining with uranyl acetate and transmission electron microscopy. Native bovine surfactant was also examined by transmission electron microscopy of thinly sectioned embedded material. Lipid vesicles made from dipalmitoylphosphatidylcholine and egg phosphatidylcholine (1:1 wt/wt) generally showed a smooth surface morphology, but some large vesicles showed a corrugated one. On the smooth-surfaced vesicles, SP-As primarily interacted in the form of separate octadecamers or as multidirectional protein networks. On the surfaces of the striated vesicles, SP-As primarily formed regularly spaced unidirectional filaments. The mean spacing between adjacent striations and between adjacent filaments was 49 nm. The striated surfaces were not essential for the formation of filaments but appeared to stabilize them. In native surfactant preparations, SP-A was detected in the dense layers. This latter arrangement of the lipid bilayer-associated SP-As supported the potential relevance of the in vitro structures to the in vivo situation.
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9

Frey, Shelli L., Luka Pocivavsek, Alan J. Waring, Frans J. Walther, Jose M. Hernandez-Juviel, Piotr Ruchala, and Ka Yee C. Lee. "Functional importance of the NH2-terminal insertion sequence of lung surfactant protein B." American Journal of Physiology-Lung Cellular and Molecular Physiology 298, no. 3 (March 2010): L335—L347. http://dx.doi.org/10.1152/ajplung.00190.2009.

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Lung surfactant protein B (SP-B) is required for proper surface activity of pulmonary surfactant. In model lung surfactant lipid systems composed of saturated and unsaturated lipids, the unsaturated lipids are removed from the film at high compression. It is thought that SP-B helps anchor these lipids closely to the monolayer in three-dimensional cylindrical structures termed “nanosilos” seen by atomic force microscopy imaging of deposited monolayers at high surface pressures. Here we explore the role of the SP-B NH2 terminus in the formation and stability of these cylindrical structures, specifically the distribution of lipid stack height, width, and density with four SP-B truncation peptides: SP-B 1–25, SP-B 9–25, SP-B 11–25, and SP-B 1–25Nflex (prolines 2 and 4 substituted with alanine). The first nine amino acids, termed the insertion sequence and the interface seeking tryptophan residue 9, are shown to stabilize the formation of nanosilos while an increase in the insertion sequence flexibility (SP-B 1–25Nflex) may improve peptide functionality. This provides a functional understanding of the insertion sequence beyond anchoring the protein to the two-dimensional membrane lining the lung, as it also stabilizes formation of nanosilos, creating reversible repositories for fluid lipids at high compression. In lavaged, surfactant-deficient rats, instillation of a mixture of SP-B 1–25 (as a monomer or dimer) and synthetic lung lavage lipids quickly improved oxygenation and dynamic compliance, whereas SP-B 11–25 surfactants showed oxygenation and dynamic compliance values similar to that of lipids alone, demonstrating a positive correlation between formation of stable, but reversible, nanosilos and in vivo efficacy.
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10

Miles, P. R., L. Bowman, K. M. K. Rao, J. E. Baatz, and L. Huffman. "Pulmonary surfactant inhibits LPS-induced nitric oxide production by alveolar macrophages." American Journal of Physiology-Lung Cellular and Molecular Physiology 276, no. 1 (January 1, 1999): L186—L196. http://dx.doi.org/10.1152/ajplung.1999.276.1.l186.

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The objectives of this investigation were 1) to report that pulmonary surfactant inhibits lipopolysaccharide (LPS)-induced nitric oxide (⋅ NO) production by rat alveolar macrophages, 2) to study possible mechanisms for this effect, and 3) to determine which surfactant component(s) is responsible. ⋅ NO produced by the cells in response to LPS is due to an inducible ⋅ NO synthase (iNOS). Surfactant inhibits LPS-induced ⋅ NO formation in a concentration-dependent manner; ⋅ NO production is inhibited by ∼50 and ∼75% at surfactant levels of 100 and 200 μg phospholipid/ml, respectively. The inhibition is not due to surfactant interference with the interaction of LPS with the cells or to disruption of the formation of iNOS mRNA. Also, surfactant does not seem to reduce ⋅ NO formation by directly affecting iNOS activity or by acting as an antioxidant or radical scavenger. However, in the presence of surfactant, there is an ∼80% reduction in the amount of LPS-induced iNOS protein in the cells. LPS-induced ⋅ NO production is inhibited by Survanta, a surfactant preparation used in replacement therapy, as well as by natural surfactant. ⋅ NO formation is not affected by the major lipid components of surfactant or by two surfactant-associated proteins, surfactant protein (SP) A or SP-C. However, the hydrophobic SP-B inhibits ⋅ NO formation in a concentration-dependent manner; ⋅ NO production is inhibited by ∼50 and ∼90% at SP-B levels of 1–2 and 10 μg/ml, respectively. These results show that lung surfactant inhibits LPS-induced ⋅ NO production by alveolar macrophages, that the effect is due to a reduction in iNOS protein levels, and that the surfactant component responsible for the reduction is SP-B.
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