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Ultrastructural study of the specific granule of the human eosinophil

Journal of Submicroscopic Cytology
|July 1, 1981
PubMed

Insights

Human eosinophils release peroxidase when exposed to immunocomplexes. A tubular structure within granules appears to contain and excrete this enzyme, crucial for allergic responses.

Area of Science:

  • Immunology
  • Cell Biology
  • Allergy Research

Background:

  • Human eosinophils contain specific granules rich in peroxidase.
  • Incubation with homologous immunocomplexes causes eosinophil granule lysis and peroxidase release.

Purpose of the Study:

  • To elucidate the role of the granule matrix in eosinophil peroxidase release.
  • To investigate the nature and function of structures within the eosinophil granule matrix.

Main Methods:

  • Incubation of human eosinophils with homologous immunocomplexes.
  • Microscopic examination of specific granules and allergic nasal tissue.

Main Results:

  • A membranous tubular structure was identified within the eosinophil granule matrix.
  • Peroxidase content decreased as this tubular structure emerged, suggesting it contains the enzyme.
  • The tubular structure was observed both in stimulated eosinophils and in allergic nasal membranes.

Conclusions:

  • The membranous tubular structure acts as a container for eosinophil peroxidase.
  • This structure facilitates the excretion of peroxidase from the granule matrix and potentially outside the cell.
  • Understanding this mechanism offers insights into eosinophil function in allergic inflammation.

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