title: In situ hybridization evidence for the coexistence of ASIC and TRPV1 within rat single sensory neurons.
abstract: The activation of nociceptors by protons plays a crucial role in the initiation and maintenance of acidosis-linked pain. Acid-sensing ion channel (ASIC) and transient receptor potential/vanilloid receptor subtype-1 (TRPV1) encode proton-activated cation channels expressed by nociceptors and the opening of these channels results in nociceptor excitation. Histological relations among ASIC clones and the colocalization of each ASIC subunit and TRPV1 within single sensory neurons were examined on serial sections of rat dorsal root ganglia (DRG) using in situ hybridization histochemistry. ASIC1a transcripts were expressed in 20-25% of the DRG neurons, and most of the neurons had small (<30 microm)-diameter cell bodies. ASIC1b transcripts and ASIC3 transcripts were expressed in approximately 10% and 30-35% of the DRG neurons, respectively, and the greater part of each population was located in small-to-medium (30-50 microm)-diameter cells. The ASIC1a transcripts and ASIC1b transcripts were basically localized in the distinct populations of the DRG neurons, while approximately 20% of the ASIC1a-positive neurons and approximately 10% of the ASIC1b-positive neurons expressed ASIC3 transcripts. TRPV1 transcripts were expressed in 35-40% of the DRG neurons, and most of the TRPV1-positive neurons had small-diameter cell bodies. Intense expression signals for ASIC1a transcripts were detected in 40-45% of the TRPV1-positive neurons. Neurons expressing both ASIC1b and TRPV1 transcripts were barely detected in the DRG. Approximately 30% of the TRPV1-positive neurons expressed ASIC3 transcripts, and the double-labeled neurons were comprised of both small-diameter and medium-diameter cells. Approximately 13% of the TRPV1-positive neurons expressed both ASIC1a and ASIC3 transcripts.
authors.affiliation: Department of Molecular Morphology, Graduate School of Medical Sciences, Nagoya City University, 1 Kawasumi, Mizuho-cho, Mizuho-ku, Nagoya 467-8601, Japan. ugawa@med.nagoya-cu.ac.jp
authors.forename: Shinya
authors.initials: S
authors.lastname: Ugawa
authors.forename: Takashi
authors.initials: T
authors.lastname: Ueda
authors.forename: Hisao
authors.initials: H
authors.lastname: Yamamura
authors.forename: Shoichi
authors.initials: S
authors.lastname: Shimada
mesh_terms: D062565:Acid Sensing Ion Channels; D000818:Animals; D002452:Cell Count / Q000379:methods; D005123:Eye / Q000378:metabolism; D005727:Ganglia, Spinal / Q000166:cytology*; D017403:In Situ Hybridization / Q000379:methods; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D009475:Neurons, Afferent / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D020133:Reverse Transcriptase Polymerase Chain Reaction / Q000379:methods; D015222:Sodium Channels / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D050916:TRPV Cation Channels
chemical_list: C568269:ASIC3 protein, rat; D062565:Acid Sensing Ion Channels; D007473:Ion Channels; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D015222:Sodium Channels; D050916:TRPV Cation Channels; C493922:Trpv1 protein, rat