Publication Date:
1995-08-04
Description:
An immunoglobulin E (IgE)-dependent histamine-releasing factor (HRF) produced by lymphocytes of atopic children and present in biological fluids of allergic patients has been identified and purified. Amino-terminal sequencing revealed extensive homology to a mouse protein, p21, and its human homolog, p23. Both recombinant proteins caused histamine release from the human basophils of a subpopulation of donors, and this release was dependent on IgE. Polyclonal antibodies recognized and removed the biological activity of recombinant and native HRF. HRF identifies a heterogeneity of IgE and is believed to play a prominent role in chronic allergic disease processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacDonald, S M -- Rafnar, T -- Langdon, J -- Lichtenstein, L M -- AI 07290/AI/NIAID NIH HHS/ -- AI 32651/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):688-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Johns Hopkins Asthma and Allergy Center, Baltimore, MD 21224, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542803" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Antibodies/immunology
;
Base Sequence
;
Basophils/immunology
;
*Biomarkers, Tumor
;
Cell Line
;
Cloning, Molecular
;
*Histamine Release
;
Humans
;
Immunoglobulin E/*immunology
;
Kinetics
;
Lymphokines/*chemistry/immunology/isolation & purification/pharmacology
;
Macrophages/metabolism
;
Mice
;
Molecular Sequence Data
;
Recombinant Fusion Proteins/pharmacology
;
Sequence Homology, Amino Acid
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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