Evidence map›Paper›PMID 11106940›Full record

ArticleImmunology2000

Natural autoantibodies against heat-shock proteins hsp70 and gp96: implications for immunotherapy using heat-shock proteins.

A Ménoret, R Y Chandawarkar, P K Srivastava

Open access · bronzeAbstract read
In one paragraph

Article in Immunology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Microorganisms · 2021
    Review
  3. Review
  4. Review
  5. Review
  6. Biological autoimmunity screening in hepatitis C patients by anti-HepG2 lysate and anti-heat shock protein 70.1 autoantibodies.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2009
    Article
  7. Article
  8. Therapeutic cancer vaccines: using unique antigens.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Review
  9. Article
  10. 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 2 institutions in 1 country.

A MénoretCenter for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, CT 06030, USA.
R Y Chandawarkar
P K Srivastava
University of Connecticut · USAkron General Medical Center · US

Funding

HEAT SHOCK PROTEINS AS TUMOR ANTIGENSR01CA044786 · NCI · FORDHAM UNIVERSITY · PI SRIVASTAVA, PRAMOD K. · 1993 to 1995
–
HSP70 PEPTIDE COMPLEXES IN SPECIFIC IMMUNOTHERAPYR01CA064394 · NCI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SRIVASTAVA, PRAMOD K. · 1994 to 1997
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GENETIC DETERMINANTS OF POLYMORPHIC SARCOMA ANTIGENSR29CA044786 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SRIVASTAVA, PRAMOD K. · 1987 to 1991
–
NCI NIH HHS CA44786NCI NIH HHS CA64394
6 · The paper itself

Abstract

Immunization of mice with cognate cancer-derived heat-shock protein (hsp) preparations leads to protection from cancer growth. As hsp used for vaccination or therapy are derived from autologous cancers, questions of pathological autoimmunity are of immense significance for the ongoing translation of this approach to therapy of human cancer. Employing the sera of normal adult mice as the first antibody, highly sensitive immunoblotting revealed the presence of anti-hsp natural autoantibodies in healthy animals. Natural autoantibodies of the immunoglobulin D (IgD) isotype bind to gp96, whereas hsp70 was recognized by IgD and IgM autoantibodies. Neither hsp was recognized by the IgA, IgE or IgG immunoglobulins contained in the serum. The antigen-antibody recognition was titratable and dependent on the integrity of the IgD molecule. Sera from only a subset of the animals tested were found to be positive for autoantibodies against gp96 and hsp70, and individual and strain-specific variations were detected. Injection of gp96 into healthy mice did not show sustained or consistent anti-gp96 IgD antibody response, class switching, toxicity or pathological autoimmunity. IgD autoantibodies against gp96 and hsp70 were also not detected in the autoimmune lpr mice. These observations show the existence of a measured and tightly regulated natural immune response to hsp.

Indexed as

AnimalsAntigens, NeoplasmAutoantibodiesAutoimmunityDiabetes Mellitus, ExperimentalDiabetes Mellitus, Type 1HSP70 Heat-Shock ProteinsImmunoglobulin DImmunoglobulin MImmunotherapy, ActiveMiceMice, Inbred NODMice, Inbred StrainsSpecies SpecificityAntigens, NeoplasmAutoantibodiesHSP70 Heat-Shock ProteinsImmunoglobulin DImmunoglobulin Msarcoma glycoprotein gp96 rejection antigens

Identifiers

PMID11106940
PMCPMC2327096
OpenAlexW2022014402

What OpenQuestion holds

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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.