Histamine H1-receptors in HL-60 monocytes are coupled to Gi-proteins and pertussis toxin-insensitive G-proteins and mediate activation of Ca2+ influx without concomitant Ca2+ mobilization from intracellular stores

URN to cite this document:

urn:nbn:de:bvb:355-epub-233016 Copy

DOI to cite this document:

10.5283/epub.23301 Copy

Seifert, Roland ; Grünbaum, L. ; Schultz, Günter

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Date of publication of this fulltext: 26 Jan 2012 08:18

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Details

Item type:	Article
Journal or Publication Title:	Naunyn-Schmiedeberg's archives of pharmacology
Publisher:	Springer
Volume:	349
Number of Issue or Book Chapter:	4
Page Range:	pp. 355-361
Date:	1994
Institutions:	Chemistry and Pharmacy > Institute of Pharmacy > Pharmacology and Toxicology (Prof. Schlossmann, formerly Prof. Seifert)
Identification Number:	Value Type 8058107 PubMed ID
Classification:	Notation Type Adenosine Diphosphate Ribose/metabolism MESH Calcium/metabolism MESH Cell Line MESH GTP-Binding Proteins/metabolism MESH Histamine/pharmacology MESH Histamine Agonists/pharmacology MESH Humans MESH Imidazoles/pharmacology MESH Monocytes/metabolism MESH N-Formylmethionine Leucyl-Phenylalanine/pharmacology MESH Oxygen Consumption/drug effects MESH Pertussis Toxin MESH Platelet Aggregation Inhibitors/pharmacology MESH Receptors, Histamine H1/metabolism MESH Virulence Factors, Bordetella/pharmacology MESH
Dewey Decimal Classification:	600 Technology > 610 Medical sciences Medicine 600 Technology > 615 Pharmacy
Status:	Published
Refereed:	Yes, this version has been refereed
Created at the University of Regensburg:	Unknown
Item ID:	23301

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Abstract

The results of binding studies suggest the presence of histamine H1-receptors in human monocytes, but it is not known whether these receptors are functionally active. This prompted us to study the effects of histamine (HA) on cytosolic Ca2+ concentration ([Ca2+]i) and superoxide anion (O2-) formation in HL-60 cells differentiated towards monocytes with 1 alpha,25-dihydroxycholecalciferol. In ...

Abstract

The results of binding studies suggest the presence of histamine H1-receptors in human monocytes, but it is not known whether these receptors are functionally active. This prompted us to study the effects of histamine (HA) on cytosolic Ca2+ concentration ([Ca2+]i) and superoxide anion (O2-) formation in HL-60 cells differentiated towards monocytes with 1 alpha,25-dihydroxycholecalciferol. In HL-60 monocytes, HA increased [Ca2+]i with a half-maximal effect at 8 microM and a maximum at 30-100 microM. Pertussis toxin (PTX) partially inhibited the stimulatory effects of HA on [Ca2+]i. Betahistine, a weak partial H1-receptor agonist, also increased [Ca2+]i, whereas H2- and H3-receptor agonists were ineffective. H1- but not H2- and H3-receptor antagonists inhibited HA-induced rises in [Ca2+]i. HA-induced rises in [Ca2+]i were desensitized in a homologous manner and were also inhibited by the activator of protein kinase C, 4 beta-phorbol 12-myristate 13-acetate. Various protein kinase C inhibitors did not interfere with homologous desensitization. The stimulatory effects of HA on [Ca2+]i were completely dependent on the presence of extracellular Ca2+ and were inhibited by the blocker of non-selective cation (NSC) channels, 1-(beta-[3-(4-methoxyphenyl)propoxyl]-4-methoxyphenethyl)-1 H-imidazole hydrochloride (SK & F 96365). HA was much less effective than the chemotactic peptide, N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP), to induce rises in [Ca2+]i. Unlike fMLP, HA did not activate O2- formation.(ABSTRACT TRUNCATED AT 250 WORDS)

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