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Concanavalin A binding glycoprotein in human stratum corneum
The Journal of Investigative Dermatology
|March 1, 1984
Summary
A novel mannose-containing glycoprotein was found in the human epidermis's outer layer. This membrane-bound protein becomes accessible to concanavalin A and trypsin only after detergent solubilization.
Area of Science:
- Biochemistry
- Dermatology
- Cell Biology
Background:
- The stratum corneum, the outermost layer of the epidermis, plays a crucial role in skin barrier function.
- Understanding the molecular composition of the stratum corneum is essential for elucidating skin physiology and pathology.
Purpose of the Study:
- To identify and characterize novel glycoproteins within the normal human epidermis.
- To investigate the localization and accessibility of a specific mannose-containing glycoprotein in the stratum corneum.
Main Methods:
- Isolation and biochemical analysis of proteins from human epidermis.
- Use of concanavalin A for glycoprotein labeling.
- Enzymatic digestion with trypsin to assess protein accessibility.
- Detergent solubilization techniques to alter protein accessibility.
Main Results:
- A 40K mannose-containing glycoprotein was identified in the stratum corneum.
- In intact epidermis, this glycoprotein is membrane-bound and inaccessible to concanavalin A and trypsin.
- Detergent solubilization renders the glycoprotein accessible to concanavalin A labeling and trypsin digestion.
- Minimal amounts of this glycoprotein were detected in viable epidermal cells.
Conclusions:
- A specific mannose-containing glycoprotein is present in the stratum corneum of normal human epidermis.
- Its membrane-bound nature and altered accessibility suggest a role in the specialized environment of the stratum corneum.
- Further research is warranted to determine the precise function of this glycoprotein in skin barrier homeostasis.