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Chemotaxis of Rat Mast Cells Toward Adenine Nucleotides¹

Department of Zoology and Genetics, Iowa State University, Ames, IA 50011

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 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.

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