Immunohistochemical localization of type 2 inositol 1,4,5-trisphosphate receptor to the nucleus of different mammalian cells

2002 ◽  
Vol 85 (1) ◽  
pp. 219-228 ◽  
Author(s):  
Karina Laflamme ◽  
Olivier Domingue ◽  
Benoit I. Guillemette ◽  
Gaétan Guillemette
Keyword(s):  
Mammalian Cells ◽  
Immunohistochemical Localization ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

Transcription initiation sites and promoter structure of the mouse type 2 inositol 1,4,5-trisphosphate receptor gene

Gene ◽  
1997 ◽  
Vol 196 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Kiyoshi Morikawa ◽  
Tetsuya Ohbayashi ◽  
Midori Nakagawa ◽  
Yoshiyuki Konishi ◽  
Yasutaka Makino ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
Receptor Gene ◽  
Promoter Structure ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

Type 2 inositol 1,4,5-trisphosphate receptor is predominantly involved in agonist-induced Ca2+ signaling in Bergmann glia

2012 ◽  
Vol 74 (1) ◽  
pp. 32-41 ◽  
Author(s):  
Sayako Tamamushi ◽  
Takeshi Nakamura ◽  
Takafumi Inoue ◽  
Etsuko Ebisui ◽  
Kotomi Sugiura ◽  
...  
Keyword(s):  
Bergmann Glia ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

scholarly journals Location of the Permeation Pathway in the Recombinant Type 1 Inositol 1,4,5-Trisphosphate Receptor

1999 ◽  
Vol 114 (2) ◽  
pp. 243-250 ◽  
Author(s):  
Josefina Ramos-Franco ◽  
Daniel Galvan ◽  
Gregory A. Mignery ◽  
Michael Fill
Keyword(s):  
Lipid Bilayers ◽  
Mammalian Cells ◽  
Single Channel ◽  
Site Directed Mutagenesis ◽  
Recombinant Type ◽  
Mutation Strategy ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Permeation Properties

The inositol 1,4,5-trisphosphate receptor (InsP3R) forms ligand-regulated intracellular Ca2+ release channels in the endoplasmic reticulum of all mammalian cells. The InsP3R has been suggested to have six transmembrane regions (TMRs) near its carboxyl terminus. A TMR-deletion mutation strategy was applied to define the location of the InsP3R pore. Mutant InsP3Rs were expressed in COS-1 cells and single channel function was defined in planar lipid bilayers. Mutants having the fifth and sixth TMR (and the interceding lumenal loop), but missing all other TMRs, formed channels with permeation properties similar to wild-type channels (gCs = 284; gCa = 60 pS; PCa/PCs = 6.3). These mutant channels bound InsP3, but ligand occupancy did not regulate the constitutively open pore (Po > 0.80). We propose that a region of 191 amino acids (including the fifth and sixth TMR, residues 2398–2589) near the COOH terminus of the protein forms the InsP3R pore. Further, we have produced a constitutively open InsP3R pore mutant that is ideal for future site-directed mutagenesis studies of the structure–function relationships that define Ca2+ permeation through the InsP3R channel.

DNA sequences of RAPD fragments in artiodactyls

Genome ◽  
1996 ◽  
Vol 39 (2) ◽  
pp. 456-458 ◽  
Author(s):  
Silja Kostia ◽  
Jukka Palo ◽  
Sirkka-Liisa Varvio
Keyword(s):  
Dna Sequences ◽  
Sequence Similarity ◽  
Receptor Gene ◽  
Chromosome 2 ◽  
High Sequence Similarity ◽  
Microsatellite Repeats ◽  
Rapd Profile ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

A bovine RAPD profile, generated by a 10-mer primer, was analysed by sequencing the major fragments. Three of four different fragments showed homologies to previously characterized mammalian sequences. One was 61–66% identical to LINE sequences and another was 78.5% identical to a human chromosome 2 sequence tagged site. The third fragment was 93.1% identical to the human type 2 inositol 1,4,5-trisphosphate receptor gene. This fragment had counterparts in white-tailed deer and reindeer; fragments of slightly different size in these species showed high sequence similarity and the size differences were due to varying numbers of dinucleotide microsatellite repeats inside the fragment. Key words : RAPD, artiodactyls, sequence similarity, microsatellites, type 2 inositol 1,4,5-trisphosphate receptor.

scholarly journals Type 2 inositol 1,4,5-trisphosphate receptor modulates bile salt export pump activity in rat hepatocytes

Hepatology ◽  
2011 ◽  
Vol 54 (5) ◽  
pp. 1790-1799 ◽  
Author(s):  
Emma A. Kruglov ◽  
Samir Gautam ◽  
Mateus T. Guerra ◽  
Michael H. Nathanson
Keyword(s):  
Bile Salt ◽  
Rat Hepatocytes ◽  
Bile Salt Export Pump ◽  
Inositol 1,4,5 Trisphosphate ◽  
Pump Activity ◽  
Trisphosphate Receptor
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