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Related Experiment Videos

Endogenous lectin from terminally differentiated epidermal cells.

M M Brysk, S Rajaraman, P Penn

    Differentiation; Research in Biological Diversity
    |January 1, 1986
    PubMed
    Summary

    Researchers identified a novel histidine-rich glycoprotein in the human stratum corneum. This endogenous lectin acts as a cell-surface molecule, potentially crucial for corneocyte adhesion and skin barrier function.

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    Area of Science:

    • Biochemistry
    • Dermatology
    • Cell Biology

    Background:

    • The stratum corneum forms the outermost skin barrier.
    • Understanding its structural components is key to skin health.

    Purpose of the Study:

    • To isolate and characterize a novel concanavalin A (Con-A)-binding glycoprotein from the human stratum corneum.
    • To elucidate its function in skin structure and adhesion.

    Main Methods:

    • Nonionic detergent extraction
    • Lectin affinity chromatography
    • Preparative gel electrophoresis
    • Isoelectric focusing
    • Monospecific polyclonal antibody production
    • Ultrastructural cytoimmunolocalization
    • Hemagglutination assays

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    Main Results:

    • A 40-kilodalton histidine-rich glycoprotein was isolated.
    • This glycoprotein localizes to stratum corneum membranes.
    • It functions as an endogenous lectin, exhibiting hemagglutination activity inhibited by amino sugars.
    • It is distinct from other known histidine-rich proteins.

    Conclusions:

    • The isolated glycoprotein is a major carbohydrate-binding, cross-linking molecule in the stratum corneum.
    • It likely plays a significant role in corneocyte adhesion and desquamation.
    • This endogenous lectin represents a novel component of the skin barrier.