ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2013
Variations in both TG1 and TG2 isozyme-specific in situ activities and protein expressions during mouse embryonic development.
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The role of transglutaminase 2 in stabilizing fibrin clots and supporting hemostasis.PloS one · 2026Article
- Transglutaminase 1: Emerging Functions beyond Skin.International journal of molecular sciences · 2024Review
- Development of peptide-based biosensors for detecting cross-linking and deamidation activities of transglutaminases.Amino acids · 2023Article
- Magnetic Resonance Imaging Reveals Distinct Roles for Tissue Transglutaminase and Factor XIII in Maternal Angiogenesis During Early Mouse Pregnancy.Arteriosclerosis, thrombosis, and vascular biology · 2019Article
- Isozyme-specific comprehensive characterization of transglutaminase-crosslinked substrates in kidney fibrosis.Scientific reports · 2018Article
- Global identification and analysis of isozyme-specific possible substrates crosslinked by transglutaminases using substrate peptides in mouse liver fibrosis.Scientific reports · 2017Article
- Transglutaminase 2 in cartilage homoeostasis: novel links with inflammatory osteoarthritis.Amino acids · 2017Review
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6 authors.
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Abstract
Transglutaminase (TG) is a family of enzymes that catalyzes cross-linking reactions among proteins. Using fluorescent-labeled highly reactive substrate peptides, we recently developed a system to visualize isozyme-specific in situ enzymatic activity. In the present study, we investigated the in situ activities of TG1 (skin-type) and TG2 (tissue-type) using whole mouse sections of various embryonic developmental stages and neonates. In each case, we also successfully used immunostaining of identical whole mouse sections for protein expression after detection of enzymatic activities. In general, the enzymatic activity was correlated with TG protein expression. However, in some tissues, TG protein expression patterns, which were inconsistent with the enzymatic activities, suggested that inactive TGs were produced possibly by self cross-linking or other modifications. Our method allowed us to simultaneously observe developmental variations in both TG isozyme-specific activities and protein levels in mouse embryonic and neonate tissues.
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