Evidence map›Paper›PMID 2018484›Full record

ArticleThe Biochemical journal1991

Band 3 protein degradation by calpain is enhanced in erythrocytes of old people.

N Schwarz-Ben Meir, T Glaser, N S Kosower

Open access · bronzeAbstract readComparative Study
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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. How Do Red Blood Cells Die?Frontiers in physiology · 2021
    Review
  6. Manipulating Eryptosis of Human Red Blood Cells: A Novel Antimalarial Strategy?Frontiers in cellular and infection microbiology · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Calpain (Ca(2+)-dependent thiol protease) in erythrocytes of young and old individuals.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  12. Article
  13. Article
  14. 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

3 authors at 1 institution in 1 country.

N Schwarz-Ben MeirDepartment of Human Genetics, Sackler School of Medicine, Tel-Aviv University, Israel.
T Glaser
N S Kosower
Tel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Band 3 protein is a major erythrocyte transmembrane glycoprotein. We compared the degradation of band 3 protein by calpain I (a cytoplasmic, micromolar-Ca2(+)-requiring thiol proteinase) in the cells from old individuals (greater than 70 years old) to that in the cells from young ones (20-30 years old). In the young, little degradation of band 3 protein occurred in calpain-treated erythrocyte ghosts. In the old, significant band 3 protein degradation was found in erythrocyte ghosts treated similarly. The difference between young and old in the susceptibility of band 3 protein to calpain was retained in membrane vesicles (membranes stripped of peripheral proteins by NaOH) and in chymotrypsin-generated 60 kDa fragment (CH-60). The isolated N-terminal cytoplasmic 43 kDa fragment was degraded by calpain to a similar extent in old and in young. The separated 17 kDa membrane domain of the CH-60 and the trypsin-generated C-terminal 55 kDa membrane-spanning fragment were not degraded by calpain I in the young, nor in the old. Thus the N-terminal cytoplasmic domain is the domain degraded by calpain I. Enhanced sensitivity in the old is observed in intact band 3 protein and in CH-60, the isolated cytoplasmic domain being equally susceptible in young and old. The observed age-related enhanced sensitivity to calpain is consistent with the presence of modifications in band 3 protein and alterations in the association with the calpain-calpastatin system. Band 3 protein has several important functions, with modifications in the protein having implications for altered cell behaviour in the old individual.

Indexed as

AdultAgedAged, 80 and overAgingAnion Exchange Protein 1, ErythrocyteCalpainChymotrypsinErythrocyte MembraneHumansImmunoblottingMembrane ProteinsMolecular WeightPeptide FragmentsAnion Exchange Protein 1, ErythrocyteCalpainChymotrypsinMembrane ProteinsPeptide Fragments

Identifiers

PMID2018484
PMCPMC1150011
OpenAlexW1937918917

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.