Evidence map›Paper›PMID 9355760›Full record

ArticleThe Biochemical journal1997

Differential expression and regulation of ryanodine receptor and myo-inositol 1,4,5-trisphosphate receptor Ca2+ release channels in mammalian tissues and cell lines.

J J Mackrill, R A Challiss, D A O'connell, F A Lai, S R Nahorski

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 65 citations in OpenAlex.

  1. IPAntioxidants (Basel, Switzerland) · 2024
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  7. Modulation of Gq-protein-coupled inositol trisphosphate and Ca2+ signaling by the membrane potential.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

J J MackrillDepartment of Cell Physiology and Pharmacology, University of Leicester, Medical Sciences Building, University Road, Leicester LE1 9HN, U.K.
R A Challiss
D A O'connell
F A Lai
S R Nahorski
University of Leicester · GBNational Institute for Medical Research · TZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ryanodine receptors (RyRs) and Ins(1,4,5)P3 receptors (Ins(1,4, 5)P3Rs) represent two multigene families of channel proteins that mediate the release of Ca2+ ions from intracellular stores. In the present study, the expression patterns of these channel proteins in mammalian cell lines and tissues were investigated by using isoform-specific antibodies. All cell lines examined expressed two or more Ins(1,4,5)P3R isoforms, with the type 1 Ins(1,4,5)P3R being ubiquitous. RyR isoforms were detected in only six out of eight cell lines studied. Similarly, of the nine rabbit tissues examined, RyR protein expression was detected only in brain, heart, skeletal muscle and uterus. Specific [3H]ryanodine binding was found in a number of rabbit tissues, although it was not detected in mammalian cell lines. Subcellular fractionation of SH-SY5Y human neuroblastomas revealed that the type 2 RyR and type 1 Ins(1,4,5)P3R co-localize among the fractions of a sucrose-cushion separation of crude microsomal membrane fractions. Manipulation of SH-SY5Y cells by chronic stimulation of muscarinic acetylcholine receptor (mAChR) results in a decrease in their type 1 Ins(1,4,5)P3R levels but not in the abundance of the type 2 RyR. Differentiation of these neuroblastomas by using retinoic acid did not detectably alter their expression of Ca2+-release channel proteins. Finally, differentiation of BC3H1 cells affects the expression of their Ca2+-release channel proteins in an isoform-specific manner. In summary, this study demonstrates that mammalian cell lines display distinct patterns of Ca2+-release channel protein expression. The abundance of these proteins is differentially regulated during phenotypic modifications of a cell, such as differentiation or chronic stimulation of mAChR.

Indexed as

Gene Expression RegulationAmino Acid SequenceAnimalsBlotting, WesternCalcium ChannelsCell DifferentiationHumansInositol 1,4,5-Trisphosphate ReceptorsMembrane ProteinsMethacholine ChlorideMicrosomesMolecular Sequence DataNeuronsProtein BindingRabbitsReceptors, Cytoplasmic and NuclearCalcium ChannelsInositol 1,4,5-Trisphosphate ReceptorsITPR1 protein, humanITPR2 protein, humanMembrane ProteinsMethacholine ChlorideReceptors, Cytoplasmic and NuclearReceptors, MuscarinicRyanodineRyanodine Receptor Calcium Release ChannelTretinoin

Identifiers

PMID9355760
PMCPMC1218788
OpenAlexW2148049759

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.