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PMID: 1281979 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Formyl peptides and ATP stimulate Ca2+ and Na+ inward currents through non-selective cation channels via G-proteins in dibutyryl cyclic AMP-differentiated HL-60 cells. Involvement of Ca2+ and Na+ in the activation of beta-glucuronidase release and superoxide production.

The Biochemical journal ·Vol. 288 ( Pt 3) ·1992-12-15 ·Pages 1025-35

Krautwurst D, Seifert R, Hescheler J, Schultz G

Abstract

In human neutrophils, the chemotactic peptide N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP) induces increases in the intracellular free Ca2+ concentration ([Ca2+]i) with subsequent activation of beta-glucuronidase release and superoxide (O2-) production. Results from several laboratories suggest that the increase in [Ca2+]i is due to activation of non-selective cation (NSC) channels. We studied the biophysical characteristics, pharmacological modulation and functional role of NSC channels in dibutyryl cyclic AMP (Bt2cAMP)-differentiated HL-60 cells. fMLP increased [Ca2+]i by release of Ca2+ from intracellular stores and influx of Ca2+ from the extracellular space. fMLP also induced Mn2+ influx. Ca2+ and Mn2+ influxes were inhibited by 1-(beta-[3-(4-methoxyphenyl)propoxy]-4-methoxyphenethyl)-1H-imidazole hydrochloride (SK&F 96365). Under whole-cell voltage-clamp conditions, fMLP and ATP (a purinoceptor agonist) activated inward currents characterized by a linear current-voltage relationship and a reversal potential near 0 mV. NSC channels were substantially more permeable to Na+ than to Ca2+. SK&F 96365 inhibited fMLP- and ATP-stimulated currents with a half-maximal effect at about 3 microM. Pertussis toxin prevented stimulation by fMLP of NSC currents and reduced ATP-stimulated currents by about 80%. Intracellular application of the stable GDP analogue, guanosine 5'-O-[2-thio]diphosphate, completely blocked stimulation by agonists of NSC currents. In excised inside-out patches, single channel openings with an amplitude of 0.24 pA were observed in the presence of fMLP and the GTP analogue, guanosine 5'-O-[3-thio]triphosphate. The bath solution contained neither Ca2+ nor ATP. The current/voltage relationship was linear with a conductance of 4-5 pS and reversed at about 0 mV. fMLP-induced beta-glucuronidase release and O2- production were substantially reduced by replacement of extracellular CaCl2 or NaCl by ethylenebis(oxyethylenenitrilo)tetra-acetic acid and choline chloride respectively. In the absence of Ca2+ and Na+, fMLP was ineffective. SK&F 96365 inhibited fMLP-induced beta-glucuronidase release and O2- production in the presence of both Ca2+ and Na+, and in the presence of Ca2+ or Na+ alone. NaCl (25-50 mM) enhanced the basal and absolute extent of fMLP-stimulated GTP hydrolysis of heterotrimeric regulatory G-proteins in HL-60 membranes. The order of effectiveness of salts in enhancing GTP hydrolysis was LiCl > KCl > NaCl > choline chloride.(ABSTRACT TRUNCATED AT 400 WORDS)

MeSH Terms
Adenosine Triphosphate/pharmacology Bucladesine/pharmacology Calcium/metabolism,physiology Calcium Channels/drug effects,physiology Cell Differentiation/drug effects Enzyme Activation Fluorescence Fura-2 GTP-Binding Proteins/physiology Glucuronidase/metabolism Humans Intracellular Fluid/metabolism Ion Channels/drug effects,physiology Leukemia, Myeloid/enzymology,metabolism,pathology Manganese/metabolism Membrane Potentials/drug effects,physiology N-Formylmethionine Leucyl-Phenylalanine/pharmacology Sodium/metabolism,physiology Sodium Channels/drug effects,physiology Stimulation, Chemical Superoxides/metabolism Tumor Cells, Cultured
Chemicals
Calcium Channels Ion Channels Sodium Channels Superoxides Manganese N-Formylmethionine Leucyl-Phenylalanine Bucladesine Adenosine Triphosphate Sodium Glucuronidase GTP-Binding Proteins Calcium Fura-2
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Krautwurst D
Institut für Pharmakologie, Freie Universität Berlin, Federal Republic of Germany.
Seifert R
Hescheler J
Schultz G
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2881025
Published
1992-12-15
Pages
1025-35
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1131990
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2881025 PMC Full Text View journal details
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