Nisoldepine inhibits formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) receptor-coupled calcium transport in human neutrophils

K. C. Williamson; A. I. Tauber; J. Navarro

doi:10.1002/jlb.42.3.239

Nisoldepine inhibits formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) receptor-coupled calcium transport in human neutrophils

K. C. Williamson, A. I. Tauber, J. Navarro

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

The formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) dependent Ca²⁺ uptake by human neutrophils consists of at least two components, one of which is sensitive to dihydropyridine derivatives. Inhibition by dihydropyridine derivatives showed the rank order of nisoldepine > nitrendipine > nimodepine > /Bay K 8644. The nisoldepine-sensitive calcium uptake exhibited an ID₅₀ of 1.5 μM and maximal inhibition were observed at 5 μM. Neither calcium efflux or [³H]fMet-Leu-Phe binding was affected by nisoldepine up to 10 μM. The inhibition by nisoldepine was inversely proportional to the extracellular calcium concentration. Unlabeled nisoldepine and other dihydropyridine derivatives displaced the specific binding of [³H]PN 200-110 to human neutrophils. Our data suggest a relationship between dihydropyridine binding and the inhibition of fMet-Leu-Phe-dependent Ca²⁺ uptake.

Original language	English (US)
Pages (from-to)	239-244
Number of pages	6
Journal	Journal of Leukocyte Biology
Volume	42
Issue number	3
DOIs	https://doi.org/10.1002/jlb.42.3.239
State	Published - 1987
Externally published	Yes

ASJC Scopus subject areas

Immunology and Allergy
Immunology
Cell Biology

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title = "Nisoldepine inhibits formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) receptor-coupled calcium transport in human neutrophils",

abstract = "The formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) dependent Ca2+ uptake by human neutrophils consists of at least two components, one of which is sensitive to dihydropyridine derivatives. Inhibition by dihydropyridine derivatives showed the rank order of nisoldepine > nitrendipine > nimodepine > /Bay K 8644. The nisoldepine-sensitive calcium uptake exhibited an ID50 of 1.5 μM and maximal inhibition were observed at 5 μM. Neither calcium efflux or [3H]fMet-Leu-Phe binding was affected by nisoldepine up to 10 μM. The inhibition by nisoldepine was inversely proportional to the extracellular calcium concentration. Unlabeled nisoldepine and other dihydropyridine derivatives displaced the specific binding of [3H]PN 200-110 to human neutrophils. Our data suggest a relationship between dihydropyridine binding and the inhibition of fMet-Leu-Phe-dependent Ca2+ uptake.",

author = "Williamson, {K. C.} and Tauber, {A. I.} and J. Navarro",

year = "1987",

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AU - Williamson, K. C.

AU - Tauber, A. I.

AU - Navarro, J.

PY - 1987

Y1 - 1987

N2 - The formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) dependent Ca2+ uptake by human neutrophils consists of at least two components, one of which is sensitive to dihydropyridine derivatives. Inhibition by dihydropyridine derivatives showed the rank order of nisoldepine > nitrendipine > nimodepine > /Bay K 8644. The nisoldepine-sensitive calcium uptake exhibited an ID50 of 1.5 μM and maximal inhibition were observed at 5 μM. Neither calcium efflux or [3H]fMet-Leu-Phe binding was affected by nisoldepine up to 10 μM. The inhibition by nisoldepine was inversely proportional to the extracellular calcium concentration. Unlabeled nisoldepine and other dihydropyridine derivatives displaced the specific binding of [3H]PN 200-110 to human neutrophils. Our data suggest a relationship between dihydropyridine binding and the inhibition of fMet-Leu-Phe-dependent Ca2+ uptake.

AB - The formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) dependent Ca2+ uptake by human neutrophils consists of at least two components, one of which is sensitive to dihydropyridine derivatives. Inhibition by dihydropyridine derivatives showed the rank order of nisoldepine > nitrendipine > nimodepine > /Bay K 8644. The nisoldepine-sensitive calcium uptake exhibited an ID50 of 1.5 μM and maximal inhibition were observed at 5 μM. Neither calcium efflux or [3H]fMet-Leu-Phe binding was affected by nisoldepine up to 10 μM. The inhibition by nisoldepine was inversely proportional to the extracellular calcium concentration. Unlabeled nisoldepine and other dihydropyridine derivatives displaced the specific binding of [3H]PN 200-110 to human neutrophils. Our data suggest a relationship between dihydropyridine binding and the inhibition of fMet-Leu-Phe-dependent Ca2+ uptake.

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Nisoldepine inhibits formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) receptor-coupled calcium transport in human neutrophils

Abstract

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