Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10747891 | Biochemical and Biophysical Research Communications | 2016 | 6 Pages |
Abstract
Transglutaminase (TGase) catalyzes protein cross-linking reactions essential for several biological processes. In differentiating keratinocytes, TG1 (keratinocyte-type) is crucial for the cross-linking of substrate proteins required for the complete formation of the cornified envelop, a proteinaceous supermolecule located in the outermost layer of the epidermis. TG1 expressions and its substrate were induced in cultured keratinocytes at differentiation-stage specific manner. In the cultured keratinocytes, we used the TG1-specific substrate peptide, which enables the specific detection of enzymatic activity to investigate its induction patterns. As a further application of the substrate peptide, several substrate candidates of TG1 that may be essential for cornified envelope formation were identified and characterized.
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Authors
Miki Yamane, Kayoko Sugimura, Hiroko Kawasaki, Hideki Tatsukawa, Kiyotaka Hitomi,