ArticleThe American journal of pathology2010
Transglutaminase1 preferred substrate peptide K5 is an efficient tool in diagnosis of lamellar ichthyosis.
Article in The American journal of pathology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Human Transglutaminases: Updated Insights into Activation Mechanisms, Allosteric Regulation and Disease.International journal of molecular sciences · 2026Review
- Transglutaminase 6 Is Colocalized and Interacts with Mutant Huntingtin in Huntington Disease Rodent Animal Models.International journal of molecular sciences · 2021Article
- Ichthyosis molecular fingerprinting shows profound TThe Journal of allergy and clinical immunology · 2019Article
- Variations in both TG1 and TG2 isozyme-specific in situ activities and protein expressions during mouse embryonic development.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2013Article
- In situ detection of active transglutaminases for keratinocyte type (TGase 1) and tissue type (TGase 2) using fluorescence-labeled highly reactive substrate peptides.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
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Abstract
Lamellar ichthyosis (LI) is a genetically heterogeneous, severe genodermatosis showing widespread hyperkeratosis of the skin. Transglutaminase 1 (TGase1) deficiency by TGase1 gene (TGM1) mutations is the most prevalent cause of LI. Screening of TGase1 deficiency in skin is essential to facilitate the molecular diagnosis of LI. However, cadaverine, the most widely used substrate for TGase activity assay, is not isozyme specific. Recently, a human TGase1-specific highly preferred substrate peptide K5 (pepK5) was generated. To evaluate its potential as a diagnostic tool for LI, we performed pepK5 labeling of TGase1 activity in normal human and LI skin. Ca(2+)-dependent labeling of FITC-pepK5 was clearly seen in the upper spinous and granular layers of normal human skin where it precisely overlapped with TGase1 immunostaining. Both specificity and sensitivity of FITC-pepK5 labeling for TGase1 activity were higher than those of FITC-cadaverine labeling. FITC-pepK5 labeling colocalized with involucrin and loricrin immunostaining at cornified cell envelope forming sites. FITC-pepK5 labeling was negative in LI patients carrying TGM1 truncation mutations and partially abolished in the other LI patients harboring missense mutations. The present results clearly indicate that pepK5 is a powerful tool for screening LI patient TGase1 deficiency when we make molecular diagnosis of LI.
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