Activation of superoxide formation and lysozyme release in human neutrophils by the synthetic lipopeptide Pam3Cys-Ser-(Lys)4. Involvement of guanine-nucleotide-binding proteins and synergism with chemotactic peptides

URN zum Zitieren dieses Dokuments:

urn:nbn:de:bvb:355-epub-232448 Copy

DOI zum Zitieren dieses Dokuments:

10.5283/epub.23244 Copy

Seifert, Roland ; Schultz, Günter ; Richter-Freund, M. ; Metzger, J. ; Wiesmüller, K. H. ; Jung, G. ; Bessler, W. G. ; Hauschildt, S.

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Veröffentlichungsdatum dieses Volltextes: 24 Jan 2012 13:38

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Alternative Links zum Volltext:Pubmed

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Details

Dokumentenart:	Artikel
Titel eines Journals oder einer Zeitschrift:	The Biochemical journal
Verlag:	Portland Pr.
Band:	267
Nummer des Zeitschriftenheftes oder des Kapitels:	3
Seitenbereich:	S. 795-802
Datum:	1990
Institutionen:	Chemie und Pharmazie > Institut für Pharmazie > Lehrstuhl Pharmakologie und Toxikologie (Prof. Schlossmann, ehemals Prof. Seifert)
Identifikationsnummer:	Wert Typ 2160237 PubMed-ID
Klassifikation:	Notation Art Dose-Response Relationship, Drug MESH Drug Synergism MESH Exocytosis/drug effects MESH GTP-Binding Proteins/physiology MESH Humans MESH Lipoproteins/pharmacology MESH Muramidase/secretion MESH N-Formylmethionine Leucyl-Phenylalanine/pharmacology MESH Neutrophils/metabolism MESH Oligopeptides/pharmacology MESH Platelet Activating Factor/pharmacology MESH Structure-Activity Relationship MESH Superoxides/metabolism MESH Tumor Necrosis Factor-alpha/pharmacology MESH
Dewey-Dezimal-Klassifikation:	600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin 600 Technik, Medizin, angewandte Wissenschaften > 615 Pharmazie
Status:	Veröffentlicht
Begutachtet:	Ja, diese Version wurde begutachtet
An der Universität Regensburg entstanden:	Unbekannt / Keine Angabe
Dokumenten-ID:	23244

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Zusammenfassung

Upon exposure to the bacterial chemotactic peptide fMet-Leu-Phe, human neutrophils release lysozyme and generate superoxide anions (O2.-). The synthetic lipoamino acid N-palmitoyl-S-[2,3-bis(palmitoyloxy)-(2RS)-propyl]-(R)-cysteine (Pam3Cys), which is derived from the N-terminus of bacterial lipoprotein, when attached to Ser-(Lys)4 [giving Pam3Cys-Ser-(Lys)4], activated O2.- formation and ...

Zusammenfassung

Upon exposure to the bacterial chemotactic peptide fMet-Leu-Phe, human neutrophils release lysozyme and generate superoxide anions (O2.-). The synthetic lipoamino acid N-palmitoyl-S-[2,3-bis(palmitoyloxy)-(2RS)-propyl]-(R)-cysteine (Pam3Cys), which is derived from the N-terminus of bacterial lipoprotein, when attached to Ser-(Lys)4 [giving Pam3Cys-Ser-(Lys)4], activated O2.- formation and lysozyme release in human neutrophils with an effectiveness amounting to about 15% of that of fMet-Leu-Phe. Palmitic acid, muramyl dipeptide, lipopolysaccharide and the lipopeptides Pam3Cys-Ala-Gly, Pam3Cys-Ser-Gly, Pam3Cys-Ser, Pam3Cys-OMe and Pam3Cys-OH did not activate O2.- formation. Pertussis toxin, which ADP-ribosylates guanine-nucleotide-binding proteins (G-proteins) and functionally uncouples formyl peptide receptors from G-proteins, prevented activation of O2.- formation by fMet-Leu-Phe and inhibited Pam3Cys-Ser-(Lys)4-induced O2.- formation by 85%. Lipopeptide-induced exocytosis was pertussis-toxin-insensitive. O2.- formation induced by Pam3Cys-Ser-(Lys)4 and fMet-Leu-Phe was enhanced by cytochalasin B, by a phorbol ester and by a diacylglycerol kinase inhibitor. Addition of activators of adenylate cyclase and removal of extracellular Ca2+ inhibited O2.- formation by fMet-Leu-Phe and Pam3Cys-Ser-(Lys)4 to different extents. Pam3Cys-Ser-(Lys)4 synergistically enhanced fMet-Leu-Phe-induced O2.- formation and primed neutrophils to respond to the chemotactic peptide at non-stimulatory concentrations. Our data suggest the following. (1) Pam3Cys-Ser-(Lys)4 activates neutrophils through G-proteins, involving pertussis-toxin-sensitive and -insensitive processes. (2) The signal transduction pathways activated by fMet-Leu-Phe and Pam3Cys-Ser-(Lys)4 are similar but not identical. (3) In inflammatory processes, bacterial lipoproteins and chemotactic peptides may interact synergistically to activate O2.- formation, leading to enhanced bactericidal activity.

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