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Galactoside-binding lectin in human tissues.

H J Allen1, C Karakousis, M S Piver

  • 1Department of Surgical Oncology, Roswell Park Memorial Institute, Buffalo, N.Y.

Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine
|January 1, 1987
PubMed
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Researchers detected lactose-inhibitable lectin activity in various human tissues, including cancerous and non-cancerous samples. This lectin, found to be endogenously synthesized, binds to human cell receptors.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • Lectins are carbohydrate-binding proteins with diverse biological roles.
  • Lectin activity has been observed in various tissues, but its presence and function in human cancers require further investigation.
  • Understanding lectin expression in different tissues can provide insights into cellular interactions and disease processes.

Purpose of the Study:

  • To analyze lactose-inhibitable lectin activity in human tissues and cells.
  • To characterize the lectin's physical properties and tissue distribution.
  • To investigate the origin and binding capabilities of the lectin.

Main Methods:

  • Hemagglutination assay to detect lectin activity.
  • Affinity chromatography for lectin isolation.

Related Experiment Videos

  • Immunohistochemical assay and Ouchterlony immunodiffusion for lectin localization and presence confirmation.
  • In vitro metabolic radiolabelling to determine synthesis versus absorption.
  • Binding assays with human buffy coat cells.

    • Main Results:

    • Lectin activity was detected in surgically removed malignant tissues (melanoma, sarcoma, colon, breast carcinoma) and adjacent non-malignant tissues, as well as autopsy samples and malignant effusions.
    • Malignant tissues generally showed higher hemagglutinating titers than non-malignant tissues, with significant inter-individual variability.
    • The isolated lung lectin had a native molecular mass of 31,000 Da and a subunit mass of 14,000 Da.
    • Immunohistochemistry revealed lectin distributed in the cytoplasm of lung epithelial cells.
    • Ouchterlony analysis confirmed lectin presence in various tissues and some body fluids.
    • Radiolabelling indicated endogenous synthesis of the lectin.
    • Isolated lectin bound to human buffy coat cell receptors.

    Conclusions:

    • Lactose-inhibitable lectin is present in a wide range of human tissues, including malignant and non-malignant types.
    • The lectin is likely endogenously synthesized and exhibits binding activity towards human blood cells.
    • Further research into this lectin's role in cellular interactions and potential involvement in disease is warranted.