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TGM2 promotes formation of soluble and insoluble high molecular weight aggregates by catalyzing a covalent linkage between peptide\u2010bound Q residues in polyQ proteins and a peptide\u2010bound Lys residue. Therapeutic approaches to modulate the activity of TGM2 are needed to proceed with studies to test the efficacy of TGM2 inhibition in disease processes. We investigated whether acetylation of Lys\u2010residues by sulfosuccinimidyl acetate (SNA) or aspirin (ASA) would alter the crosslinking activity of TGM2. Acetylation by either SNA and\/or ASA resulted in a loss of &gt;90% of crosslinking activity. The Lys residues that were critical for inhibition were identified by mass spectrometry as Lys<jats:sup>444<\/jats:sup>, Lys<jats:sup>468<\/jats:sup>, and Lys<jats:sup>663<\/jats:sup>. Hence, acetylation of Lys\u2010residues may modulate the enzymatic function of TGM2<jats:italic>in vivo<\/jats:italic>and offer a novel approach to treatment of TGM2 mediated disorders.<\/jats:p>","DOI":"10.1002\/pro.301","type":"journal-article","created":{"date-parts":[[2010,1,6]],"date-time":"2010-01-06T14:45:39Z","timestamp":1262789139000},"page":"229-235","source":"Crossref","is-referenced-by-count":19,"title":["Human tissue transglutaminase is inhibited by pharmacologic and chemical acetylation"],"prefix":"10.1002","volume":"19","author":[{"given":"Thung S.","family":"Lai","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher","family":"Davies","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles 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