Evidence map›Paper›PMID 1567352›Full record

ArticleBasic research in cardiology

Determination of alpha B crystallin aggregation: a new alternative method to assess ischemic damage of the heart.

M Chiesi, F Bennardini

Abstract read
PubMed Publisher
In one paragraph

Article in Basic research in cardiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. Article
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

2 authors at 1 institution in 1 country.

M ChiesiDepartment of Research, CIBA-GEIGY Ltd., Basel, Switzerland.
F Bennardini
Novartis (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

alpha B crystallin, a heat-shock-like protein, is a major component of the soluble protein fraction of the heart and is thought to play a protective role in stress situations. During an ischemic episode, the cytosol of cardiomyocytes acidifies, thus causing the aggregation of the protein with cytoskeletal elements. After homogenization of the tissue, alpha B crystallin can then be recovered with the insoluble cell components. This study investigated the change of the solubility properties of crystallin in the ischemic heart. The distribution of crystallin in the soluble and insoluble cellular fractions was determined by centrifugation of heart homogenates and immunoblot analysis with anti-alpha B crystallin antibodies. The proportion of aggregated alpha B-crystallin increased in hearts reperfused after total normothermic ischemia of increasing severity. alpha B crystallin aggregation was proportional to the amount of lactate dehydrogenase activity released by the hearts and was inversely correlated to the ability of the hearts to recover contractile activity after the ischemic episode. This study shows that the amount of aggregated crystallin can be used as a new marker for the ischemic damage of the heart. Biopsies of a few milligrams are sufficient for the analysis.

Indexed as

AnimalsCoronary DiseaseCrystallinsCulture MediaDensitometryGuinea PigsImmunoblottingL-Lactate DehydrogenaseMyocardiumTissue DistributionCrystallinsCulture MediaL-Lactate Dehydrogenase

Identifiers

PMID1567352
OpenAlexW1973107087

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.