AbstractObjective: Gαh (tissue transglutaminase; TGII), known as the αMethods: We examined not only the cross-linking ability of TGII for tau, but also the expression level of tau as well as αResults: When the tau protein was assayed as a transglutaminase substrate of TGII, tau proteins formed cross-linked products. However, phospholipase C-δ1 inhibited transglutaminase activity in TGII to cross-link with tau in vitro. The amount of expressed mRNA in AD brain tissue was elevated 2~10 fold for tau and 3~20 fold for TGII. Consistent with these observations, the densities of expressed proteins in AD brain tissue also increased 9 fold for tau and 15 fold for TGII. Moreover, phospholipase C-δ1, which is a negative regulator for transglutaminase activity of TGII, also increased 2~25 fold for mRNA as well as 8 fold for protein in AD brain tissue. In contrast, expressed mRNA and protein activity for αConclusion: These results suggest that the α