Differential Effect of Brefeldin A on the Palmitoylation of Surfactant Protein C Proprotein Mutants

Brinke, Anja ten; Batenburg, Joseph J.; Haagsman, Henk P.; Golde, L.M.G. Van; Vaandrager, Arie B.

doi:10.1006/bbrc.2001.6223

Cited by 9 publications

(3 citation statements)

References 24 publications

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“…Immunoblotting of the membrane fraction of transfected cells with anti-GFP or anti-DsRed demonstrated processing of wild-type SP-C as shown by bands ( Fig. 6 , second panel, lanes b, d, e) corresponding to the predicted Mr of the primary translation product of the fusion protein (48,000) and a smaller intermediate cleaved product (arrow) as previously reported ( 23,(37)(38)(39). In contrast, neither DsRed/ABCA3-Chimera nor EGFP/ SP-C SPPDY → LLLWKN was suffi ciently processed with disproportionate expression of their respective primary translation products ( Fig.…”

Section: Post-golgi-targeted Abca3 N-terminal Motif Proteins Do Not Psupporting

confidence: 80%

“…When A549 cells are used as a surrogate for alveolar type II cells, in addition to their colocalization with CD63, a biochemical signature for traffi cking to post-Golgi distal vesicles is their partial cleavage to a lower molecular weight intermediate ( 23,(37)(38)(39). Immunoblotting of the membrane fraction of transfected cells with anti-GFP or anti-DsRed demonstrated processing of wild-type SP-C as shown by bands ( Fig.…”

Section: Post-golgi-targeted Abca3 N-terminal Motif Proteins Do Not Pmentioning

confidence: 97%

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A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments

Beers

Hawkins

Shuman

et al. 2011

Journal of Lipid Research

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Section: Post-golgi-targeted Abca3 N-terminal Motif Proteins Do Not Psupporting

confidence: 80%

Section: Post-golgi-targeted Abca3 N-terminal Motif Proteins Do Not Pmentioning

confidence: 97%

A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments

Beers

Hawkins

Shuman

et al. 2011

Journal of Lipid Research

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“…Lung surfactant protein C (SP-C) is initially synthesized as a precursor protein, proSP-C. Palmitoylation of proSP-C occurs at two internal cysteine residues with high efficiency , under enzymatic control, occurring between the ER and the cis -Golgi. , After processing to SP-C, the protein is incorporated into lamellar bodies (multilamellar vesicles) and transported to the plasma membrane, where fusion of the lamellar bodies releases SP-C into the liquid layer lining the airway epithelium. Examination of SP-C obtained from bronchoalveolar lavage has identified a third SP-C lipidation site.…”

Section: Aminolysis and Transesterificationmentioning

confidence: 99%

The Chemical Reactivity of Membrane Lipids

Duché,

Sanderson

2024

Chem. Rev.

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It is well-known that aqueous dispersions of phospholipids spontaneously assemble into bilayer structures. These structures have numerous applications across chemistry and materials science and form the fundamental structural unit of the biological membrane. The particular environment of the lipid bilayer, with a water-poor low dielectric core surrounded by a more polar and better hydrated interfacial region, gives the membrane particular biophysical and physicochemical properties and presents a unique environment for chemical reactions to occur. Many different types of molecule spanning a range of sizes, from dissolved gases through small organics to proteins, are able to interact with membranes and promote chemical changes to lipids that subsequently affect the physicochemical properties of the bilayer. This Review describes the chemical reactivity exhibited by lipids in their membrane form, with an emphasis on conditions where the lipids are well hydrated in the form of bilayers. Key topics include the following: lytic reactions of glyceryl esters, including hydrolysis, aminolysis, and transesterification; oxidation reactions of alkenes in unsaturated fatty acids and sterols, including autoxidation and oxidation by singlet oxygen; reactivity of headgroups, particularly with reactive carbonyl species; and E/Z isomerization of alkenes. The consequences of reactivity for biological activity and biophysical properties are also discussed. CONTENTS

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Structure and Function of Pulmonary Surfactant Proteins

García‐Álvarez

Alonso

Pérez‐Gil

2019

Encyclopedia of Life Sciences

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Pulmonary surfactant is a lipid/protein complex essential to keep the airspaces of mammalian lungs open. It forms surface‐active films at the respiratory air–liquid interface, reducing surface tension to a minimum and thus minimising the work of breathing. At the same time, surfactant establishes the first barrier against the entry of potential pathogens through the large surface that lungs expose to environment. Both the interfacial and the innate defence activities depend critically on the presence of highly specialised evolutionarily conserved surfactant‐associated proteins. The structure and molecular mechanisms of these proteins have been extensively characterised in the last decades, in studies that constitute the basis for current models on surfactant mechanisms at the alveolar spaces, in health and disease. This article summarises the current knowledge on the structure–function relationships defining the molecular action of pulmonary surfactant proteins and how they are being key actors to maintain operative breathing in the lungs. Key Concepts The presence of specific proteins is essential for pulmonary surfactant to play its crucial role in stabilising the respiratory air–liquid interface. Collectin proteins SP‐A and SP‐D oligomerise to form trimers and supratrimeric oligomers with multivalent binding capacities to sugars and lipids and participate in innate defence mechanisms, binding to the surface of pathogens and allergens to facilitate their clearance. Surfactant protein SP‐B is essential for life; its absence is associated with an irreversible respiratory failure at birth. SP‐B belongs to the saposin protein family and assembles as ring‐shaped oligomers that enclose hydrophobic channels competent to transfer phospholipids between membranes and between membranes and the interface, avoiding its exposure to aqueous environments. Some synthetic peptides designed to mimic key SP‐B motifs are being used to produce alternative surfactant preparations for therapeutic applications. Protein SP‐C is a very hydrophobic helical protein whose expression is linked to the differentiation of lung tissue. Its oligomerisation is associated with surfactant membrane fragmentation and their interconversions at the alveolar spaces.

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Differential Effect of Brefeldin A on the Palmitoylation of Surfactant Protein C Proprotein Mutants

Cited by 9 publications

References 24 publications

A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments

A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments

The Chemical Reactivity of Membrane Lipids

Structure and Function of Pulmonary Surfactant Proteins

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