Multiple P2 receptor-mediated mechanisms exist by which ATP can alter nociceptive sensitivity following tissue injury. Evidence from a variety of experimental strategies, including genetic disruption studies and the development of selective antagonists, has indicated that the activation of P2X receptor subtypes, including P2X3, P2X2/3, P2X4 and P2X7, and P2Y (e.g., P2Y2) receptors, can modulate...

Extracellular nucleotides interact with purinergic receptors, which regulate ion transport in a variety of epithelia. With the use of two different human epithelial carcinoma cell lines (HCT8 and Caco-2), we have shown by RT-PCR that the cells express mRNA for P2X1, P2X3, P2X4, P2X5, P2X6, P2X7, P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, and P2Y12 receptors. Protein expression for P2Y1 and P2Y2 receptors w...

Purinergic1 receptors were initially conceived to describe the likely existence of membrane receptors responding to adenosine triphosphate (ATP) (P2 receptors) or its breakdown product adenosine (P1 receptors) in causing nonadrenergic, noncholinergic relaxation of gut smooth muscle.1 Cloning of these receptors has yielded insights into their properties and signaling mechanisms, allowing classif...

Purinergic1 receptors were initially conceived to describe the likely existence of membrane receptors responding to adenosine triphosphate (ATP) (P2 receptors) or its breakdown product adenosine (P1 receptors) in causing nonadrenergic, noncholinergic relaxation of gut smooth muscle.1 Cloning of these receptors has yielded insights into their properties and signaling mechanisms, allowing classif...

Optimization of membrane protein stability under different solution conditions is essential for obtaining crystals that diffract to high resolution. Traditional methods that evaluate protein stability require large amounts of material and are, therefore, ill suited for medium- to high-throughput screening of membrane proteins. Here we present a rapid and efficient fluorescence-detection size-ex...