{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTransglutaminase 3 (TGM3) is a Ca²⁺‐dependent enzyme that plays a critical role in the differentiation and barrier function of stratified epithelia. In the skin, TGM3 participates in the cross‐linking of structural proteins during the formation of the cornified envelope, a process essential for maintaining an effective epidermal barrier. Beyond its structural role, TGM3 is also implicated as a key autoantigen in gluten‐related disorders; notably, patients with dermatitis herpetiformis develop high‐avidity IgA antibodies against TGM3, and immune deposits in the papillary dermis contain TGM3 rather than other transglutaminase isoforms. TGM3 expression is detected not only in the epidermis but also in other epithelial tissues such as the gingiva, and its deficiency or altered distribution (for example, in Netherton syndrome) is associated with impaired epithelial differentiation and barrier integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its established function in cornification, TGM3 is vital for hair follicle biology and hair shaft formation. Genetic studies have linked mutations in TGM3 to uncombable hair syndrome, illuminating its role in mediating posttranslational modifications of structural proteins that assemble into the hair fiber. Furthermore, investigations into the regulation of the TGM3 gene in keratinocytes have underscored the importance of precise transcriptional control in ensuring proper hair and epidermal differentiation, with alterations in TGM3 expression contributing to structural defects in the hair shaft."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, TGM3 activity is regulated through intricate biochemical mechanisms. Structural studies have revealed that TGM3 binds Ca²⁺ at distinct sites required for its activation, and it cooperates with nucleotide binding—specifically GTP/GDP interaction—to modulate access to its active site. The interplay among Ca²⁺, Mg²⁺, and guanine nucleotides defines a unique regulatory cycle for TGM3, and identification of precise substrate peptide sequences has further clarified its target specificity during the protein cross‐linking reaction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA growing body of evidence implicates TGM3 in tumorigenesis and its potential utility as a prognostic biomarker across several cancers. Down-regulation or epigenetic silencing of TGM3 has been observed in various squamous cell carcinomas of the esophagus, oral cavity, larynx, and cervix, with lower expression levels correlating with poorer patient survival, increased tumor proliferation, and resistance to chemo-radiotherapy. In contrast, restoration of TGM3 expression can suppress tumor cell growth and invasiveness, in part through modulation of the PI3K/Akt signaling pathway and by influencing extracellular protein networks that affect the tumor microenvironment. Moreover, aberrant TGM3 expression has also been linked to basal cell carcinoma susceptibility, reinforcing its role as a tumor suppressor in epithelial cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the realm of neuronal pathology, TGM3 has also been implicated in neurodegenerative processes. In models of Huntington disease, for example, TGM3 along with other transglutaminase family members contributes to the cross-linking and aggregation of mutant huntingtin protein, suggesting that TGM3 activity may influence the formation of intranuclear inclusions and thereby modulate disease progression. Additionally, receptor-stimulated transamidation events mediated by TGM3 have been observed in neuronal cells, where they impact small G protein signaling and dendritic spine morphology, linking TGM3 to aspects of synaptic plasticity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Miklós Sárdy, Sarolta Kárpáti, Barbara Merkl, et al. 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