@article{oai:nagoya.repo.nii.ac.jp:00022974,
 author = {Yamane, Miki and Sugimura, Kayoko and Kawasaki, Hiroko and Tatsukawa, Hideki and Hitomi, Kiyotaka},
 issue = {1},
 journal = {Biochemical and Biophysical Research Communications},
 month = {Sep},
 note = {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.},
 pages = {343--348},
 title = {Analysis on transglutaminase 1 and its substrates using specific substrate peptide in cultured keratinocytes},
 volume = {478},
 year = {2016}
}