PMID- 18249094
OWN - NLM
STAT- MEDLINE
DCOM- 20080508
LR  - 20191210
IS  - 0898-6568 (Print)
IS  - 0898-6568 (Linking)
VI  - 20
IP  - 4
DP  - 2008 Apr
TI  - Functional relevance of the de novo coupling between hTRPC1 and type II IP3 
      receptor in store-operated Ca2+ entry in human platelets.
PG  - 737-47
LID - 10.1016/j.cellsig.2007.12.010 [doi]
AB  - Store-operated Ca2+ entry (SOCE), a major mechanism for Ca2+ entry in 
      non-excitable cells, is regulated by the filling state of the intracellular Ca2+ 
      stores. We have previously reported that a de novo conformational coupling 
      between the type II IP3 receptor (IP3RII) and hTRPC1 channel occurs after 
      depletion of the intracellular Ca2+ stores in human platelets, which might be 
      involved in the activation of SOCE in these cells. Here we present for the first 
      time direct evidence for the functional relevance of the coupling between hTRPC1 
      and IP3RII in SOCE in human platelets. Our data suggest that at least two 
      pathways may contribute to SOCE in these cells. An early component, insensitive 
      to cytochalasin D (Cyt D), is followed by a late component which is sensitive to 
      Cyt D. Introduction of a peptide corresponding to IP3RII(317-334) 
      (IP3BD-peptide(317-334)) in the cells by electrotransjection impairs the coupling 
      between hTRPC1 and IP3RII but not the interaction between hTRPC1 and STIM1 
      induced by store depletion. Coimmunoprecipitation experiments indicated that 
      endogenously expressed hTRPC1 interacts with the IP3BD-peptide(317-334). 
      Electrotransjection of cells with IP3BD-peptide(317-334), significantly 
      attenuated the late stage of Ca2+ and Mn2+ entry induced by 10 nM thapsigargin 
      (TG) or 20 microM 2,5-di-(tert-butyl)-1,4-hydroquinone (TBHQ), providing evidence 
      for a functional role of the de novo coupling between hTRPC1 and IP3RII in the 
      activation of SOCE in human platelets.
FAU - Jardin, Isaac
AU  - Jardin I
AD  - Department of Physiology (Cellular Physiology Research Group), University of 
      Extremadura, 10071 Caceres, Spain.
FAU - Lopez, Jose J
AU  - Lopez JJ
FAU - Salido, Gines M
AU  - Salido GM
FAU - Rosado, Juan A
AU  - Rosado JA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20071223
PL  - England
TA  - Cell Signal
JT  - Cellular signalling
JID - 8904683
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Hydroquinones)
RN  - 0 (Inositol 1,4,5-Trisphosphate Receptors)
RN  - 0 (Peptide Fragments)
RN  - 0 (TRPC Cation Channels)
RN  - 0 (transient receptor potential cation channel, subfamily C, member 1)
RN  - 22144-77-0 (Cytochalasin D)
RN  - 26XK13B61B (2,5-di-tert-butylhydroquinone)
RN  - 42Z2K6ZL8P (Manganese)
RN  - 67526-95-8 (Thapsigargin)
RN  - EC 7.2.2.10 (Calcium-Transporting ATPases)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Blood Platelets/drug effects/*metabolism
MH  - Calcium/*metabolism
MH  - *Calcium Signaling/drug effects
MH  - Calcium-Transporting ATPases/antagonists & inhibitors/metabolism
MH  - Cytochalasin D/pharmacology
MH  - Electroporation
MH  - Enzyme Inhibitors/pharmacology
MH  - Humans
MH  - Hydroquinones/pharmacology
MH  - Inositol 1,4,5-Trisphosphate Receptors/*metabolism
MH  - Manganese/metabolism
MH  - Peptide Fragments/metabolism
MH  - Protein Binding
MH  - TRPC Cation Channels/*metabolism
MH  - Thapsigargin/pharmacology
MH  - Time Factors
EDAT- 2008/02/06 09:00
MHDA- 2008/05/09 09:00
CRDT- 2008/02/06 09:00
PHST- 2007/11/20 00:00 [received]
PHST- 2007/12/13 00:00 [revised]
PHST- 2007/12/13 00:00 [accepted]
PHST- 2008/02/06 09:00 [pubmed]
PHST- 2008/05/09 09:00 [medline]
PHST- 2008/02/06 09:00 [entrez]
AID - S0898-6568(07)00381-6 [pii]
AID - 10.1016/j.cellsig.2007.12.010 [doi]
PST - ppublish
SO  - Cell Signal. 2008 Apr;20(4):737-47. doi: 10.1016/j.cellsig.2007.12.010. Epub 2007 
      Dec 23.