Abstract
Purinergic P2X receptors are a family of ligand-gated cationic channels activated by extracellular ATP. P2X subunit protein sequences are highly conserved between vertebrate species. However, they can generate a great diversity of coding splicing variants to fulfill several roles in mammalian physiology. Despite intensive research in P2X expression in both central and peripheral nervous system, there is little information about their homology, genomic structure and other key features that can help to develop selective drugs or regulatory strategies of pharmacological value which are lacking today. In order to obtain clues on mammalian P2X diversity, we have performed a bioinformatics analysis of the coding regions and introns of the seven P2X subunits present in human, simian, dog, mouse, rat and zebrafish. Here we report the arrangements of exon and intron sequences, considering its number, size, phase and placement; proposing some ideas about the gain and loss of exons and retention of introns. Taken together, these evidences show traits that can be used to gain insight into the evolutionary history of vertebrate P2X receptors and better understand the diversity of subunits coding the purinergic signaling in mammals.
Highlights
Purinergic P2X receptors are a family of ligand-gated cationic channels activated by extracellular ATP [1]. *Corresponding author.How to cite this paper: Loera-Valencia, R., Jaramillo-Polanco, J.O., Linan-Rico, A., Pescador, M.G.N., Bremont, J.F.J. and Barajas-López, C. (2015) Genomic Organization of Purinergic P2X Receptors
Size of the seven subunits from the species analyzed in this work has an average of 1.3 Kb without untranslated sequences—P2X4 has the smallest transcript with 1.16 Kb and P2X7 possess the longest transcript of 1.78 Kb, their aminoacid sequences are 388 and 595 residues respectively
We have suggested that genomic organization of P2X2 in mammals is composed of 12 exons and 11 introns, such as it’s been displayed in Ensembl and fast DB databases
Summary
Purinergic P2X receptors are a family of ligand-gated cationic channels activated by extracellular ATP [1]. *Corresponding author.How to cite this paper: Loera-Valencia, R., Jaramillo-Polanco, J.O., Linan-Rico, A., Pescador, M.G.N., Bremont, J.F.J. and Barajas-López, C. (2015) Genomic Organization of Purinergic P2X Receptors. Purinergic P2X receptors are a family of ligand-gated cationic channels activated by extracellular ATP [1]. (2015) Genomic Organization of Purinergic P2X Receptors. To form a functional channel, P2X subunits assemble as homo or heteromeric trimers [6]. The pharmacological properties of the assembled P2X receptor vary in function to subunit composition [7] [8]. The subunit stoichiometry has a different arrangement among tissue in a given organism, and different composition among species, for example, the enteric nervous system of the rat, mouse and guinea pig expresses P2X2/P2X3 heteromeric receptors [6] [9] while sensory ganglia and heart of rodents and humans express homomeric P2X3 receptors [10]
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