Evidence map›Paper›PMID 1376109›Full record

ArticleThe Biochemical journal1992

Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement.

T R Hughes, S J Piddlesden, J D Williams, R A Harrison, B P Morgan

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. GluR3 autoantibodies destroy neural cells in a complement-dependent manner modulated by complement regulatory proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 1 country.

T R HughesDepartment of Medical Biochemistry, University of Wales College of Medicine, Heath Park, Cardiff, U.K.
S J Piddlesden
J D Williams
R A Harrison
B P Morgan
University of Wales · GBCardiff Royal Infirmary · GBMRC Laboratory of Molecular Biology · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated 'reactive' lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntigens, CDCD59 AntigensChromatographyComplement Membrane Attack ComplexErythrocyte MembraneGlycosylationGuinea PigsHumansMembrane GlycoproteinsMiceMolecular Sequence DataMolecular WeightPhosphatidylinositol Diacylglycerol-LyaseAntibodies, MonoclonalAntigens, CDCD59 AntigensComplement Membrane Attack ComplexMembrane GlycoproteinsPhosphatidylinositol Diacylglycerol-LyasePhosphoinositide Phospholipase CPhosphoric Diester Hydrolases

Identifiers

PMID1376109
PMCPMC1132712
OpenAlexW1922947289

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.