Evidence map›Paper›PMID 1849402›Full record

ArticleThe Biochemical journal1991

Subcellular distribution of the calcium-storing inositol 1,4,5-trisphosphate-sensitive organelle in rat liver. Possible linkage to the plasma membrane through the actin microfilaments.

M F Rossier, G S Bird, J W Putney

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
8.9field-weighted citation impact, top 1% 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

35 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Article
  3. Ca(2+) channels on the move.Biochemistry · 2009
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Capacitative calcium entry.The Biochemical journal · 1995
    Review
  18. Article
  19. Article
  20. Inositol phosphates in the heart: controversy and consensus.Journal of molecular medicine (Berlin, Germany) · 1995
    Review
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

3 authors at 1 institution in 1 country.

M F RossierLaboratory of Cellular and Molecular Pharmacology, NIEHS/NIH, Research Triangle Park, NC 27709.
G S Bird
J W Putney
Research Triangle Park Foundation · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of Ins(1,4,5)P3 in the mobilization of Ca2+ from intracellular stores of non-muscle cells has been extensively demonstrated; however, the nature of the organelle releasing the Ca2+ is still poorly understood. The distributions of the Ins(1,4,5)P3-binding sites and of the Ins(1,4,5)P3-sensitive Ca2+ pool were investigated in subcellular fractions obtained from rat liver and compared with those of other markers. The Ins(1,4,5)P3-binding vesicles appeared to be completely distinct from the endoplasmic-reticulum-derived microsomes and were enriched in the same fractions which were enriched in alkaline phosphodiesterase I activity. This co-purification of the plasma-membrane marker with the Ins(1,4,5)P3-binding sites was dramatically altered after freezing or after treatment of the homogenate with the microfilament-disruptive drug cytochalasin B, suggesting that the Ins(1,4,5)P3-sensitive organelle may be linked to the plasma membrane through the actin microfilaments. No correlation was observed between the Ins(1,4,5)P3-binding capacity and the portion of the Ca2+ pool that was released by Ins(1,4,5)P3. This may result from the disruption of the native organelle during homogenization, leading to the formation of vesicles containing the Ins(1,4,5)P3 receptor, but lacking the Ca2+ pump. These results are consistent with the idea of a specialized Ins(1,4,5)P3-regulated organelle distinct from the endoplasmic reticulum, and we propose a model of the structural organization of this organelle, in which the anchorage to the cytoskeleton as well as the spatial separation of the Ca2+ pump from the Ins(1,4,5)P3 receptor have important functional significance.

Indexed as

Calcium ChannelsReceptors, Cytoplasmic and NuclearAnimalsCalciumCell FractionationCytochalasin BEndoplasmic ReticulumInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsLiverMaleOrganellesRatsRats, Inbred StrainsReceptors, Cell SurfaceCalciumCalcium ChannelsCytochalasin BInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsReceptors, Cell SurfaceReceptors, Cytoplasmic and Nuclear

Identifiers

PMID1849402
PMCPMC1149960
OpenAlexW2345003741

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.