PMID- 10051594
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 5
DP  - 1999 Mar 2
TI  - Mouse trp2, the homologue of the human trpc2 pseudogene, encodes mTrp2, a store
      depletion-activated capacitative Ca2+ entry channel.
PG  - 2060-4
AB  - Capacitative Ca2+ entry (CCE) is Ca2+ entering after stimulation of inositol
      1,4,5-trisphosphate (IP3) formation and initiation of Ca2+ store depletion. One
      hallmark of CCE is that it can also be triggered merely by store depletion, as
      occurs after inhibition of internal Ca2+ pumps with thapsigargin. Evidence has
      accumulated in support of a role of transient receptor potential (Trp) proteins
      as structural subunits of a class of Ca2+-permeable cation channels activated by 
      agonists that stimulate IP3 formation-very likely through a direct interaction
      between the IP3 receptor and a Trp subunit of the Ca2+ entry channel. The role of
      Trp's in Ca2+ entry triggered by store depletion alone is less clear. Only a few 
      of the cloned Trp's appear to enhance this type of Ca2+ entry, and when they do, 
      the effect requires special conditions to be observed, which native CCE does not.
      Here we report the full-length cDNA of mouse trp2, the homologue of the human
      trp2 pseudogene. Mouse Trp2 is shown to be readily activated not only after
      stimulation with an agonist but also by store depletion in the absence of an
      agonist. In contrast to other Trp proteins, Trp2-mediated Ca2+ entry activated by
      store depletion is seen under the same conditions that reveal endogenous store
      depletion-activated Ca2+ entry, i.e., classical CCE. The findings support the
      general hypothesis that Trp proteins are subunits of store- and receptor-operated
      Ca2+ channels.
FAU - Vannier, B
AU  - Vannier B
AD  - Department of Anesthesiology, University of California, Los Angeles, CA 90095,
      USA.
FAU - Peyton, M
AU  - Peyton M
FAU - Boulay, G
AU  - Boulay G
FAU - Brown, D
AU  - Brown D
FAU - Qin, N
AU  - Qin N
FAU - Jiang, M
AU  - Jiang M
FAU - Zhu, X
AU  - Zhu X
FAU - Birnbaumer, L
AU  - Birnbaumer L
LA  - eng
SI  - GENBANK/AF111107
SI  - GENBANK/AF111108
GR  - GM-54235/GM/NIGMS NIH HHS/United States
GR  - HL45198/HL/NHLBI 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 (Calcium Channels)
RN  - 0 (Ion Channels)
RN  - 0 (Membrane Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (TRPC Cation Channels)
RN  - 0 (TRPC2 protein, human)
RN  - 0 (TRPM Cation Channels)
RN  - 0 (TRPM2 protein, human)
RN  - 0 (Trp2 protein, vertebrate)
RN  - 0 (Trpc2 protein, mouse)
RN  - 67526-95-8 (Thapsigargin)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells
MH  - Calcium/metabolism
MH  - Calcium Channels/*genetics/physiology
MH  - Gene Expression Regulation/drug effects
MH  - Humans
MH  - Ion Channels/*genetics
MH  - Male
MH  - Membrane Potentials
MH  - Membrane Proteins/chemistry/*genetics/physiology
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Biosynthesis
MH  - Protein Structure, Secondary
MH  - *Pseudogenes
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - TRPC Cation Channels
MH  - TRPM Cation Channels
MH  - Testis/metabolism
MH  - Thapsigargin/pharmacology
MH  - Transfection
PMC - PMC26736
EDAT- 1999/03/03 00:00
MHDA- 1999/03/03 00:01
CRDT- 1999/03/03 00:00
PHST- 1999/03/03 00:00 [pubmed]
PHST- 1999/03/03 00:01 [medline]
PHST- 1999/03/03 00:00 [entrez]
AID - 10.1073/pnas.96.5.2060 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2060-4. doi: 10.1073/pnas.96.5.2060.