Chemotaxis of Rat Mast Cells Toward Adenine Nucleotides

Rat mucosal mast cells express P2 purinoceptors, occupation of which mobilizes cytosolic Ca2+ and activates a potassium conductance. The primary function of this P2 system in mast cell biology remains unknown. Here, we show that extracellular ADP causes morphological changes in rat bone marrow-cultu...

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Bibliographic Details
Published in:The Journal of immunology (1950) 1999-07, Vol.163 (2), p.970-977
Main Authors: McCloskey, Michael A, Fan, Yihong, Luther, Stacie
Format: Article
Language:English
Subjects:
Adenine Nucleotides - pharmacology
Adenine Nucleotides - physiology
Animals
Bone Marrow Cells - cytology
Bone Marrow Cells - drug effects
Calcium - metabolism
Calcium - physiology
Cell Migration Inhibition
Cell Movement - drug effects
Cell Movement - physiology
Cell Size - drug effects
Chemotaxis - drug effects
Complement C5a - physiology
Extracellular Space - physiology
GTP-Binding Proteins - physiology
Intracellular Fluid - metabolism
Kinetics
Mast Cells - cytology
Mast Cells - drug effects
Mast Cells - physiology
Membrane Potentials - physiology
Mice
Rats
Rats, Inbred F344
Receptors, Purinergic P2 - physiology
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Summary:Rat mucosal mast cells express P2 purinoceptors, occupation of which mobilizes cytosolic Ca2+ and activates a potassium conductance. The primary function of this P2 system in mast cell biology remains unknown. Here, we show that extracellular ADP causes morphological changes in rat bone marrow-cultured mast cells (BMMC) typical of those occurring in cells stimulated by chemotaxins, and that the nucleotides ADP, ATP, and UTP are effective chemoattractants for rat BMMC. ADP was also a chemotaxin for murine J774 monocytes. The nucleotide selectivity and pertussis toxin sensitivity of the rat BMMC migratory response suggest the involvement of P2U receptors. Poorly hydrolyzable derivatives of ADP and ATP were effective chemotaxins, obviating a role for adenosine receptors. Buffering of external Ca2+ at 100 nM or reduction of the electrical gradient driving Ca2+ entry (by elevating external K+) blocked ADP-driven chemotaxis, suggesting a role for Ca2+ influx in this process. Anaphylatoxin C5a was a potent chemotaxin (EC50 approximately 0.5 nM) for J774 monocytes, but it was inactive on rat BMMC in the presence or absence of laminin. Ca2+ removal or elevated [K+] had modest effects on C5a-driven chemotaxis of J774 cells, implicating markedly different requirements for Ca2+ signaling in C5a- vs ADP-mediated chemotaxis. This is supported by the observation that depletion of Ca2+ stores with thapsigargin completely blocked migration induced by ADP but not C5a. These findings suggest that adenine nucleotides liberated from parasite-infested tissue could participate in the recruitment of mast cells by intestinal mucosa.
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.163.2.970