PMID- 10318963
OWN - NLM
STAT- MEDLINE
DCOM- 19990617
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 10
DP  - 1999 May 11
TI  - TRP2: a candidate transduction channel for mammalian pheromone sensory signaling.
PG  - 5791-6
AB  - The vomeronasal organ (VNO) of terrestrial vertebrates plays a key role in the
      detection of pheromones, chemicals released by animals that elicit stereotyped
      sexual and aggressive behaviors among conspecifics. Sensory transduction in the
      VNO appears unrelated to that in the vertebrate olfactory and visual systems: the
      putative pheromone receptors of the VNO are evolutionarily independent from the
      odorant receptors and, in contrast to vertebrate visual and olfactory
      transduction, vomeronasal transduction is unlikely to be mediated by
      cyclic-nucleotide-gated channels. We hypothesized that sensory transduction in
      the VNO might instead involve an ion channel of the transient receptor potential 
      (TRP) family, members of which mediate cyclic-nucleotide-independent sensory
      responses in Drosophila melanogaster and Caenorhabditis elegans and play unknown 
      functions in mammals. We have isolated a cDNA (rTRP2) from rat VNO encoding a
      protein of 885 amino acids that is equally distant from vertebrate and
      invertebrate TRP channels (10-30% amino acid identity). rTRP2 mRNA is exclusively
      expressed in VNO neurons, and the protein is highly localized to VNO sensory
      microvilli, the proposed site of pheromone sensory transduction. The absence of
      Ca2+ stores in sensory microvilli suggests that, in contrast to a proposed
      mechanism of activation of mammalian TRP channels, but in accord with analysis of
      TRP function in Drosophila phototransduction, the gating of TRP2 is independent
      from the depletion of internal Ca2+ stores. Thus, TRP2 is likely to participate
      in vomeronasal sensory transduction, which may share additional similarities with
      light-induced signaling in the Drosophila eye.
FAU - Liman, E R
AU  - Liman ER
AD  - Howard Hughes Medical Institute, Neurobiology Department, Massachusetts General
      Hospital, Boston, MA 02114, USA. liman@helix.mgh.harvard.edu
FAU - Corey, D P
AU  - Corey DP
FAU - Dulac, C
AU  - Dulac C
LA  - eng
SI  - GENBANK/AF136401
GR  - R01 DC003903/DC/NIDCD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Ion Channels)
RN  - 0 (Membrane Proteins)
RN  - 0 (Pheromones)
RN  - 0 (RNA, Messenger)
RN  - 0 (TRPC Cation Channels)
RN  - 0 (Trp2 protein, vertebrate)
RN  - 0 (Trpc2 protein, rat)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Behavior, Animal/drug effects
MH  - Calcium/metabolism
MH  - Cloning, Molecular
MH  - Drosophila/metabolism
MH  - Immunohistochemistry
MH  - In Situ Hybridization
MH  - Ion Channel Gating
MH  - Ion Channels/*metabolism
MH  - Membrane Proteins/*chemistry
MH  - Molecular Sequence Data
MH  - Neurons, Afferent/metabolism
MH  - Pheromones/*metabolism
MH  - Phylogeny
MH  - RNA, Messenger/metabolism
MH  - Rats
MH  - Signal Transduction/*drug effects
MH  - TRPC Cation Channels
MH  - Vomeronasal Organ/*metabolism
PMC - PMC21939
EDAT- 1999/05/13 00:00
MHDA- 1999/05/13 00:01
CRDT- 1999/05/13 00:00
PHST- 1999/05/13 00:00 [pubmed]
PHST- 1999/05/13 00:01 [medline]
PHST- 1999/05/13 00:00 [entrez]
AID - 10.1073/pnas.96.10.5791 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 May 11;96(10):5791-6. doi:
      10.1073/pnas.96.10.5791.