| http://purl.uniprot.org/citations/16489761 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16489761 | http://www.w3.org/2000/01/rdf-schema#comment | "We have reported that Gram-negative organisms decorated with rough lipopolysaccharide (LPS) are particularly susceptible to the direct antimicrobial actions of the pulmonary collectins, surfactant proteins A (SP-A) and D (SP-D). In this study, we examined the lipid and LPS components required for the permeabilizing effects of the collectins on model bacterial membranes. Liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE), with or without rough Escherichia coli LPS (J5), smooth E. coli LPS (B5), or cholesterol, were loaded with self-quenching probes and exposed to native or oxidatively modified SP-A. Fluorescence that resulted from permeabilization of liposomes and diffusion of dyes was assessed by microscopy or fluorimetry. Human SP-A and melittin increased the permeability of J5 LPS/POPE liposomes, but not B5 LPS/POPE liposomes or control (POPE only) liposomes. At a human SP-A concentration of 100 microg/mL, the permeability of the J5 LPS/POPE membranes increased 4.4-fold (p < 0.02) compared to the control with no added SP-A. Rat SP-A and SP-D also permeabilized the J5-containing liposomes. Incorporation of cholesterol into J5 LPS/POPE liposomes at a POPE:cholesterol molar ratio of 1:0.15 blocked human SP-A or melittin-induced permeability (p < 0.05) compared to cholesterol-free liposomes. Exposure of human SP-A to surfactant lipid peroxidation blocked the permeabilizing activity of the protein. We conclude that SP-A permeabilizes phospholipid membranes in an LPS-dependent and rough LPS-specific manner, that the effect is neither SP-A-nor species-specific, and that oxidative damage to SP-A abolishes its membrane destabilizing properties. Incorporation of cholesterol into the membrane enhances resistance to permeabilization by SP-A, most likely by increasing the packing density and membrane rigidity."xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0522652"xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/author | "Wu H."xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/author | "McCormack F.X."xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/author | "Kuzmenko A.I."xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/pages | "2679-2685"xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/title | "Pulmonary collectins selectively permeabilize model bacterial membranes containing rough lipopolysaccharide."xsd:string |
| http://purl.uniprot.org/citations/16489761 | http://purl.uniprot.org/core/volume | "45"xsd:string |
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