Tokuya Takahashi

Expression of mRNA for matrix metalloproteinases and tissue inhibitors of metalloproteinases in periodontitis-affected human gingival tissue

It is known that the host responds to an increased concentration of collagenase [or matrix metalloproteinase (MMP)-1] by preferentially expressing mRNA for the tissue inhibitor of metalloproteinase-1 (TIMP-1) in order to overcome tissue destruction due to periodontitis. To further elucidate the relation between MMPs and TIMPs in periodontitis-affected tissues, the expression of mRNA for MMP-1, -3 and -8, and TIMP-1 and -2, in 10 gingival samples from patients and five from healthy individuals was assessed by reverse transcription-polymerase chain reaction. The diseased group showed significantly higher levels of MMP-1, -3, -8 and TIMP-1 mRNA relative to beta-actin than the control group (mean +/- SE: diseased vs healthy (%): 0.26 +/- 0.05 vs 0.018 +/- 0.0040 for MMP-1; 0.09 +/- 0.16 vs 0.063 +/- 0.016 for MMP-3; 0.068 +/- 0.017 vs 0.006 +/- 0.0010 for MMP-8; 12.66 +/- 2.90 vs 2.71 +/- 0.54 for TIMP-1; p < 0.01). TIMP-2 did not significantly differ between the two groups (1.79 +/- 0.33 vs 1.42 +/- 0.53; p > 0.05). The preferential increase in the level of MMP-3 mRNA relative to that of MMP-1 and -8 in inflamed gingiva would be relevant to tissue destruction because MMP-3 is a broad-spectrum MMP and a pivotal activator of latent MMP-1 and -8. Therefore, the overall increase in MMP-1, -3 and -8 mRNA in periodontitis-affected gingiva might account for a concerted action of MMPs during connective tissue destruction in periodontitis.

Enzymatic Acetylation of histones and some chemical characters of their acetyl groups

Abstract The enzymatic acetylation of histones by pigeon liver fractions and the chemical properties of acetyl groups accepted by histones were studied. The results are summarized as follows. 1. 1. Two pigeon liver fractions, which act as acetate activating and transferring enzyme respectively, catalyze the incorporation of [14C]acetate into histones in the presence of ATP, Mg2+ and CoA. 2. 2. Although all of histone fractions were labelled with [14C]acetate by the system, arginine-rich histone was found to be the most rapidly labelled fraction. 3. 3. The presence of both labile and stable acetyl groups for NH2OH treatment was observed in the labelled arginine-rich and slightly lysine-rich histone, whereas only the stable one was seen in the labelled lysine-rich histone.