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High-molecular-weight human epidermal transglutaminase.
The Journal of Investigative Dermatology
|July 1, 1985
Summary
This study identifies two forms of epidermal transglutaminase (ETG) in human stratum corneum, a 50kDa and a 72kDa protein. These distinct ETG forms may regulate enzyme activity.
Area of Science:
- Biochemistry
- Dermatology
- Enzymology
Background:
- Epidermal transglutaminase (ETG) plays a crucial role in skin structure and function.
- Understanding the different forms and regulation of ETG is essential for skin biology research.
Purpose of the Study:
- To investigate the presence and characteristics of epidermal transglutaminase (ETG) in human stratum corneum.
- To determine if different molecular weight forms of ETG exist and how they are regulated.
Main Methods:
- Human stratum corneum proteins were extracted and separated using SDS-PAGE.
- Proteins were transferred to nitrocellulose and detected using rabbit anti-human ETG antibody.
- Enzyme activity assays were performed after various treatments (heat, trypsin, solvents).
Main Results:
- Two distinct protein bands, 50kDa and 72kDa, were recognized by anti-ETG antibody.
- Treatment with trypsin or solvents altered the 72kDa band but not the 50kDa band.
- Partially purified 72kDa ETG activity increased after heating or trypsin treatment, suggesting activation.
Conclusions:
- The results suggest the existence of two forms of epidermal transglutaminase (ETG) in human stratum corneum.
- These different ETG forms may have distinct roles in regulating enzyme activity and skin barrier function.