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¹ Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Caixa Postal 26077, CEP 05513-970, São Paulo, Brazil

Adenosine triphosphate acts as a fast excitatory neurotransmitter by binding to and activating seven structurally related subtypes of purinergic P2X receptors, which act as ligand-gated ion channels. Besides its role in neurotransmission, ATP also has trophic functions during development of the neuronal system. P2X receptor expression, mainly of P2X₄ and P2X₆ subtypes, has been detected in adult brain and also during neuronal development. We have used the mouse teratocarcinoma P19 cell line as an in vitro model to study P2X₆ receptor expression during early neuronal differentiation. We have detected a full-length and an alternatively spliced form of the mouse P2X₆ receptor gene in P19 cells using reverse transcriptase-polymerase chain reaction. The alternatively spliced form was already present at the stage of pluripotent undifferentiated P19 cells, and was predominant compared to the full-length form during the whole course of neuronal differentiation of P19 cells. Alternative splicing of P2X₆ receptor subunits was also confirmed during postnatal development of mouse brain. During postnatal development, however, the full-length form was predominant compared to the spliced form. Alternative splicing is suggested to regulate P2X₆ receptor function during neuronal differentiation.

(Received 2 March 2006; accepted after revision 1 September 2006; first published online 7 September 2006)
Corresponding author H. Ulrich: Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Caixa Postal 26077, CEP 05513-970, São Paulo, Brazil. Email: henning{at}iq.usp.br