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Related Experiment Videos

Oriented structure in human stratum corneum revealed by X-ray diffraction.

J C Garson1, J Doucet, J L Lévêque

  • 1Laboratoires de Recherche de l'Oreal, Aulnay-Sous-Bois, France.

The Journal of Investigative Dermatology
|January 1, 1991
PubMed
Summary
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Synchrotron X-rays reveal distinct supramolecular structures in human stratum corneum. Keratin in normal skin is beta form, while callus keratin is alpha form, indicating keratinization influences organization.

Area of Science:

  • Biophysics
  • Materials Science
  • Dermatology

Background:

  • The stratum corneum is the outermost layer of the skin, crucial for barrier function.
  • Its supramolecular organization of proteins and lipids is key to its properties.
  • Understanding this organization can inform treatments for skin conditions.

Purpose of the Study:

  • To investigate the supramolecular organization of human stratum corneum using synchrotron X-rays.
  • To differentiate the roles of proteins and lipids in stratum corneum structure.
  • To explore differences in keratin structure between normal skin and callus.

Main Methods:

  • Exposure of human stratum corneum (sheets and callus) to high-flux synchrotron X-rays.
  • Analysis of resulting diffraction patterns in parallel and perpendicular geometries.

Related Experiment Videos

  • Comparative study of normal, delipidized, and membrane couplet stratum corneum samples.

    • Main Results:

    • Obtained clear diffraction patterns revealing supramolecular organization of stratum corneum proteins and lipids.
    • Identified two distinct distances for lipid bilayers in the 3-7 nm range.
    • Showed keratin in normal stratum corneum is primarily in the beta form, while callus keratin is in the alpha form.
    • Confirmed the presence of an unknown beta-form protein component.

    Conclusions:

    • Lipid and protein organization in the stratum corneum are distinct and influenced by the keratinization process.
    • Keratin's supramolecular form (alpha vs. beta) is dependent on the keratinization state.
    • An unidentified beta-form protein component exists within corneocytes or intercellular spaces.