{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T20:40:08Z","timestamp":1791232808286,"version":"4.1.0"},"reference-count":46,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2011,10,18]],"date-time":"2011-10-18T00:00:00Z","timestamp":1318896000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"The Brain Foundation of The Netherlands","award":["2008(1).36"],"award-info":[{"award-number":["2008(1).36"]}]},{"name":"The Brain Foundation of The Netherlands","award":["F2010(1)-06 to MMMW"],"award-info":[{"award-number":["F2010(1)-06 to MMMW"]}]}],"content-domain":{"domain":["pathsocjournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Journal of Pathology"],"published-print":{"date-parts":[[2012,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Alzheimer's disease (AD), progressive supranuclear palsy (PSP), frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP\u201017), and Pick's disease (PiD) are commonly known as tauopathies. Neurodegeneration observed in these diseases is linked to neuronal fibrillary hyperphosphorylated tau protein inclusions. Transglutaminases (TGs) are inducible enzymes, capable of modifying conformational and\/or structural properties of proteins by inducing molecular cross\u2010links. Both transglutaminase 1 (TG1) and transglutaminase 2 (TG2) are abundantly expressed in the brain and are associated with fibrillary hyperphosphorylated tau protein inclusions in neurons of AD, so\u2010called neurofibrillary tangles (NFTs). However, other data obtained by our group suggested that tau pathology in the brain may be primarily related to TG1 and not to TG2 activity. To obtain more information on this issue, we set out to investigate the association of TG1, TG2, and TG\u2010catalysed cross\u2010links with fibrillary hyperphosphorylated tau inclusions in tauopathies other than AD, using immunohistochemistry. We found strong TG1 and TG\u2010catalysed cross\u2010link staining in neuronal tau inclusions characteristic of PSP, FTDP\u201017 with mutations in the tau gene (FTDP\u201017T), and PiD brain, whereas, in contrast to AD, TG2 was only rarely observed in these inclusions. Furthermore, using a biochemical approach, we demonstrated that tau is a substrate for TG1\u2010mediated cross\u2010linking. Interestingly, we found co\u2010localization of the TG1 activator, tazarotene\u2010induced gene 3 (TIG3), in the neuronal tau inclusions of PSP, FTDP\u201017T, and PiD, but not in NFTs of AD cases, indicating that these tau\u2010containing protein aggregates are not identical. We conclude that TG1\u2010catalysed cross\u2010linking, regulated by TIG3, might play an important role in the formation of neuronal tau inclusions in PSP, FTDP\u201017T, and PiD brain. Copyright \u00a9 2011 Pathological Society of Great Britain and Ireland. 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