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Seifert, Roland ; Serke, S. ; Huhn, D. ; Bessler, W. G. ; Hauschildt, S. ; Metzger, J. ; Wismüller, K. H. ; Jung, G.

Incomplete functional differentiation of HL-60 leukemic cells by synthetic lipopeptides. Partial inhibition by pertussis toxin of enhanced superoxide formation

Seifert, Roland, Serke, S., Huhn, D., Bessler, W. G., Hauschildt, S., Metzger, J., Wismüller, K. H. und Jung, G. (1992) Incomplete functional differentiation of HL-60 leukemic cells by synthetic lipopeptides. Partial inhibition by pertussis toxin of enhanced superoxide formation. European journal of biochemistry / FEBS 203 (1-2), S. 143-151.

Veröffentlichungsdatum dieses Volltextes: 24 Jan 2012 08:12
Artikel
DOI zum Zitieren dieses Dokuments: 10.5283/epub.23223


Zusammenfassung

In human neutrophils, the synthetic lipopeptide, N-palmitoyl-S-[2,3- bis(palmitoyloxy-(2RS)-propyl]-(R)-cysteinyl-(S)-seryl-(S)-lysyl-( S)-lysyl-(S) -lysyl-(S)-lysine [Pam3CysSer(Lys)4], activates NADPH-oxidase catalyzed superoxide (O2-) formation through pertussis-toxin-sensitive and pertussis-toxin-insensitive mechanisms (Seifert, R., Schultz, G., Richter-Freund, M., Metzger, J., Wiesmüller, ...

In human neutrophils, the synthetic lipopeptide, N-palmitoyl-S-[2,3- bis(palmitoyloxy-(2RS)-propyl]-(R)-cysteinyl-(S)-seryl-(S)-lysyl-( S)-lysyl-(S) -lysyl-(S)-lysine [Pam3CysSer(Lys)4], activates NADPH-oxidase catalyzed superoxide (O2-) formation through pertussis-toxin-sensitive and pertussis-toxin-insensitive mechanisms (Seifert, R., Schultz, G., Richter-Freund, M., Metzger, J., Wiesmüller, K.-H., Jung, G., Bessler, W. G. & Hauschildt, S. (1990) Biochem. J. 267, 795-802). We studied the effects of lipopeptides on differentiation of HL-60 leukemic cells. Pam3CysSer(Lys)4 enhanced phorbol-12-myristate-13-acetate-induced O2- formation (presumably through the expression of components of NADPH oxidase) in a concentration-dependent manner with a half-maximal effect at 100 ng/ml and a maximum at 1 microgram/ml. The effect of the lipopeptide was evident after 24 h and reached a plateau after 48 h. (2S,6S)-2-Palmitoylamino-6,7- bis(palmitoyloxy)heptanoyl-(S)-seryl-(S)-lysyl-(S)-lysyl-(S) -lysyl-(S)-lysine enhanced O2- formation as well. The effects of Pam3CysSer(Lys)4 were potentiated by dibutyryl cAMP, dimethyl sulfoxide, retinoic acid, 1,25-dihydroxyvitamin D3, interferon-gamma and tumor-necrosis-factor-alpha. Pertussis toxin, but not its B-oligomer, partially inhibited enhanced O2- formation induced by Pam3CysSer(Lys)4. O2- formation induced by arachidonic acid and gamma-hexachlorocyclohexane were more sensitive to inhibition by pertussis toxin than O2- formation induced by phorbol 12-myristate 13-acetate. Enhanced O2- formation induced by dibutyryl cAMP was not affected by pertussis toxin. Unlike ATP, histamine, prostaglandin E1 and the beta-adrenergic agonist, isoproterenol, Pam3CysSer(Lys)4 did not increase cytosolic Ca2+ [( Ca2+]i) in undifferentiated HL-60 cells. Histamine but not lipopeptides stimulated high-affinity GTPase of guanine-nucleotide-binding proteins in membranes of undifferentiated HL-60 cells. In Pam3CysSer(Lys)4-differentiated HL-60 cells, the responsiveness to the [Ca2+]i-increasing agonists, N-formyl-L-methionyl-L-leucyl-L-phenylalanine, C5a and leukotriene B4, was increased, whilst the responsiveness to prostaglandin E1 and isoproterenol was decreased. Pam3CysSer(Lys)4 did not inhibit proliferation of HL-60 cells but decreased transferrin receptor expression and increased C3bi receptor expression. Pertussis toxin did not affect proliferation and expression of transferrin and C3bi receptors. Dibutyryl cAMP was considerably more effective than Pam3CysSer(Lys)4 at inducing alterations in the above parameters. Our results suggest that (a) Pam3CysSer(Lys)4 induces incomplete functional differentiation of HL-60 cells through a mechanism which does not depend on a rise in [Ca2+]i and is different from that of other differentiation-inducing substances and (b) the mechanism by which Pam3CysSer(Lys)4 induces differentiation involves pertussis-toxin-sensitive and pertussis-toxin-insensitive mechanisms.



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Details

DokumentenartArtikel
Titel eines Journals oder einer ZeitschriftEuropean journal of biochemistry / FEBS
Verlag:Wiley-Blackwell
Band:203
Nummer des Zeitschriftenheftes oder des Kapitels:1-2
Seitenbereich:S. 143-151
Datum1992
InstitutionenChemie und Pharmazie > Institut für Pharmazie > Lehrstuhl Pharmakologie und Toxikologie (Prof. Schlossmann, ehemals Prof. Seifert)
Identifikationsnummer
WertTyp
1309696PubMed-ID
Klassifikation
NotationArt
Bucladesine/pharmacologyMESH
Calcitriol/pharmacologyMESH
Cell DifferentiationMESH
Dimethyl Sulfoxide/pharmacologyMESH
Flow CytometryMESH
GTP Phosphohydrolases/metabolismMESH
HumansMESH
Interferon-gamma/pharmacologyMESH
Leukemia/pathologyMESH
Lipoproteins/pharmacologyMESH
Pertussis ToxinMESH
Superoxides/metabolismMESH
Transferrin/metabolismMESH
Tretinoin/pharmacologyMESH
Tumor Cells, CulturedMESH
Tumor Necrosis Factor-alpha/pharmacologyMESH
Virulence Factors, Bordetella/pharmacologyMESH
Dewey-Dezimal-Klassifikation600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin
600 Technik, Medizin, angewandte Wissenschaften > 615 Pharmazie
StatusVeröffentlicht
BegutachtetJa, diese Version wurde begutachtet
An der Universität Regensburg entstandenUnbekannt / Keine Angabe
URN der UB Regensburgurn:nbn:de:bvb:355-epub-232235
Dokumenten-ID23223

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