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Titolo:
Interaction between lipopolysaccharide (LPS), LPS-binding protein (LBP), and planar membranes
Autore:
Gutsmann, T; Haberer, N; Carroll, SF; Seydel, U; Wiese, A;
Indirizzi:
Res Ctr Borstel, Ctr Med & Biosci, Div Biophys, D-23845 Borstel, Germany Res Ctr Borstel Borstel Germany D-23845 iophys, D-23845 Borstel, Germany Xoma Corp US LLC, Berkeley, CA 94710 USA Xoma Corp US LLC Berkeley CA USA94710 orp US LLC, Berkeley, CA 94710 USA
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 3, volume: 382, anno: 2001,
pagine: 425 - 434
SICI:
1431-6730(200103)382:3<425:IBL(LP>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GRAM-NEGATIVE BACTERIA; BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN; LIPID BILAYER-MEMBRANES; ACUTE PHASE REACTANT; (LPS)-BINDING PROTEIN; MOLECULAR MECHANISMS; OUTER MEMBRANES; SEPTIC SHOCK; A BINDING; ACTIVATION;
Keywords:
capacitance; cell activation; innermembrane potential; lipopolysaccharide-binding protein; membrane interaction; signaling;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Wiese, A Res Ctr Borstel, Ctr Med & Biosci, Div Biophys, D-23845 Borstel, Germany Res Ctr Borstel Borstel Germany D-23845 -23845 Borstel, Germany
Citazione:
T. Gutsmann et al., "Interaction between lipopolysaccharide (LPS), LPS-binding protein (LBP), and planar membranes", BIOL CHEM, 382(3), 2001, pp. 425-434

Abstract

The mechanism of interaction of the lipopolysaccharide (LPS)-binding protein, LBP, with differently composed symmetric and asymmetric planar lipid bilayers was investigated in electrical measurements (membrane current, potential, capacitance). From a change of the inner membrane potential difference, binding of LBP to membranes was deduced. After addition of LBP to one side of the membrane, binding of anti-LBP antibodies and LPS to LBP on both sides of the bilayer was observed. Effects resulting from an interaction of anti-LBP antiserum with membrane-bound LBP depend on the side of addition of the antiserum, indicating a directed intercalation of LBP into the membrane. Addition of LPS to the same side as LBP may induce a change of the conformation of LBP or its orientation in the membrane. Based on these observations, we propose that LBP intercalates in a directed orientation into negatively-charged membranes and assumes a transmembrane configuration. Moreover, pre-incubated complexes of LPS and LBP do not interact with membranes. These experiments show that reconstituted planar membranes are a suitable tool for investigations of the interaction of non pore-forming proteins that are involved in signal transduction.

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Documento generato il 19/09/20 alle ore 21:30:10