PMID- 10488066
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 39
DP  - 1999 Sep 24
TI  - Molecular and functional characterization of a novel mouse transient receptor
      potential protein homologue TRP7. Ca(2+)-permeable cation channel that is
      constitutively activated and enhanced by stimulation of G protein-coupled
      receptor.
PG  - 27359-70
AB  - Characterization of mammalian homologues of Drosophila transient receptor
      potential protein (TRP) is an important clue to understand molecular mechanisms
      underlying Ca(2+) influx activated in response to stimulation of G(q)
      protein-coupled receptors in vertebrate cells. Here we have isolated cDNA
      encoding a novel seventh mammalian TRP homologue, TRP7, from mouse brain. TRP7
      showed abundant RNA expression in the heart, lung, and eye and moderate
      expression in the brain, spleen, and testis. TRP7 recombinantly expressed in
      human embryonic kidney cells exhibited distinctive functional features, compared 
      with other TRP homologues. Basal influx activity accompanied by reduction in
      Ca(2+) release from internal stores was characteristic of TRP7-expressing cells
      but was by far less significant in cells expressing TRP3, which is structurally
      the closest to TRP7 in the TRP family. TRP7 induced Ca(2+) influx in response to 
      ATP receptor stimulation at ATP concentrations lower than those necessary for
      activation of TRP3 and for Ca(2+) release from the intracellular store, which
      suggests that the TRP7 channel is activated independently of Ca(2+) release. In
      fact, TRP7 expression did not affect capacitative Ca(2+) entry induced by
      thapsigargin, whereas TRP7 greatly potentiated Mn(2+) influx induced by
      diacylglycerols without involvement of protein kinase C. Nystatin-perforated and 
      conventional whole-cell patch clamp recordings from TRP7-expressing cells
      demonstrated the constitutively activated and ATP-enhanced inward cation
      currents, both of which were initially blocked and then subsequently facilitated 
      by extracellular Ca(2+) at a physiological concentration. Impairment of TRP7
      currents by internal perfusion of the Ca(2+) chelator
      1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid revealed an essential
      role of intracellular Ca(2+) in activation of TRP7, and their potent activation
      by the diacylglycerol analogue suggests that the TRP7 channel is a new member of 
      diacylglycerol-activated cation channels. Relative permeabilities indicate that
      TRP7 is slightly selective to divalent cations. Thus, our findings reveal an
      interesting correspondence of TRP7 to the background and receptor
      stimulation-induced cation currents in various native systems.
FAU - Okada, T
AU  - Okada T
AD  - Laboratory of Humoral Information, Department of Information Physiology, National
      Institute for Physiological Sciences, Okazaki 444-8585, Japan.
FAU - Inoue, R
AU  - Inoue R
FAU - Yamazaki, K
AU  - Yamazaki K
FAU - Maeda, A
AU  - Maeda A
FAU - Kurosaki, T
AU  - Kurosaki T
FAU - Yamakuni, T
AU  - Yamakuni T
FAU - Tanaka, I
AU  - Tanaka I
FAU - Shimizu, S
AU  - Shimizu S
FAU - Ikenaka, K
AU  - Ikenaka K
FAU - Imoto, K
AU  - Imoto K
FAU - Mori, Y
AU  - Mori Y
LA  - eng
SI  - GENBANK/AF139923
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Calcium Channels)
RN  - 0 (DNA, Complementary)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Estrenes)
RN  - 0 (Insect Proteins)
RN  - 0 (Ion Channels)
RN  - 0 (Membrane Proteins)
RN  - 0 (Phosphodiesterase Inhibitors)
RN  - 0 (Pyrrolidinones)
RN  - 0 (Recombinant Proteins)
RN  - 0 (TRPC Cation Channels)
RN  - 0 (TRPM Cation Channels)
RN  - 0 (TRPM2 protein, human)
RN  - 0 (Transient Receptor Potential Channels)
RN  - 0 (Trpc7 protein, mouse)
RN  - 0 (trp protein, Drosophila)
RN  - 112648-68-7
      (1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione)
RN  - 142878-12-4 (U 73343)
RN  - 42Z2K6ZL8P (Manganese)
RN  - 526U7A2651 (Egtazic Acid)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/*metabolism
MH  - Calcium/*metabolism
MH  - Calcium Channels/metabolism
MH  - Cell Line
MH  - DNA, Complementary
MH  - Drosophila/physiology
MH  - *Drosophila Proteins
MH  - Egtazic Acid/pharmacology
MH  - Estrenes/pharmacology
MH  - Gene Expression Regulation
MH  - Humans
MH  - Insect Proteins/metabolism
MH  - Ion Channels/chemistry/*genetics/*physiology
MH  - Male
MH  - Manganese/metabolism
MH  - Membrane Potentials/drug effects/physiology
MH  - *Membrane Proteins
MH  - Mice
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Phosphodiesterase Inhibitors/pharmacology
MH  - Phylogeny
MH  - Pyrrolidinones/pharmacology
MH  - Recombinant Proteins/metabolism
MH  - Sequence Alignment
MH  - TRPC Cation Channels
MH  - TRPM Cation Channels
MH  - Transcription, Genetic
MH  - Transfection
MH  - Transient Receptor Potential Channels
EDAT- 1999/09/17 00:00
MHDA- 1999/09/17 00:01
CRDT- 1999/09/17 00:00
PHST- 1999/09/17 00:00 [pubmed]
PHST- 1999/09/17 00:01 [medline]
PHST- 1999/09/17 00:00 [entrez]
AID - 10.1074/jbc.274.39.27359 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 24;274(39):27359-70. doi: 10.1074/jbc.274.39.27359.