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Related Experiment Videos

Histamine-releasing factors.

A P Kaplan1, M Baeza, S Reddigari

  • 1Department of Medicine, SUNY, Stony Brook.

International Archives of Allergy and Applied Immunology
|January 1, 1991
PubMed
Summary
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Histamine-releasing factors (HRF) were purified from human cells, revealing distinct molecular forms. These HRF, including variants of connective-tissue activating peptide III, activate basophils and mast cells.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Histamine-releasing factors (HRF) are crucial mediators of allergic responses.
  • HRF are released from various immune cells, including basophils and mast cells.
  • Understanding HRF composition is key to deciphering allergic inflammation mechanisms.

Purpose of the Study:

  • To isolate and characterize histamine-releasing factors (HRF) from human mononuclear cells and platelets.
  • To identify the molecular species and potential identities of these HRF.
  • To investigate the functional activity of purified HRF on histamine release.

Main Methods:

  • Isolation and purification of HRF from human mononuclear cells and platelets.
  • Characterization of HRF molecular weights using gel electrophoresis (8-10, 15-17, 35-41 kDa).

Related Experiment Videos

  • Monoclonal antibody preparation for HRF, affinity chromatography, and amino acid sequencing.

    • Main Results:

    • Three distinct HRF molecular species were purified.
    • The 8-10 kDa HRF showed homology to connective-tissue activating peptide III (CTAP III) and neutrophil-activating peptide 2.
    • HRF demonstrated dose-dependent activation of basophils, distinct from IL-3 and GM-CSF.

    Conclusions:

    • Purified HRF, particularly CTAP III variants, are potent activators of basophils.
    • The 15-17 kDa and 40-41 kDa HRF moieties represent unique gene products.
    • These findings advance the understanding of allergic inflammation pathways and HRF function.