The effect of taurine on angiotensin II-induced hypertrophy of cultured neonatal rat heart cells (myocytes and nonmyocytes) was examined. Angiotensin II (1-100 nM) alone caused an increase in the rate of protein synthesis of myocytes without changing the rate of DNA synthesis and cell number. It mediated increases in DNA synthesis and cell number in nonmyocytes. Furthermore, at the lower concentration of 1 nM, it induced c-fos and c-jun expression in both cultured myocytes and nonmyocytes. Exposure of the cells to taurine (20 mM) in the absence of angiotensin II had no effect on either hyperplastic growth or immediate early response gene expression by the two types of cultured cardiac cells. However, myocytes pretreated for 24 h with 20 mM taurine exhibited reduced responsiveness to angiotensin II (1 nM), resulting in lower levels of angiotensin II-mediated stimulation in protein synthesis, and immediate early response gene expression was attenuated. Similarly, taurine treatment of nonmyocytes reduced the degree of hyperplastic growth (DNA synthesis and cell number) and immediate early response gene expression stimulated by angiotensin II. Finally, taurine partially prevented the increase in intracellular free calcium [Ca2+]i mediated by angiotensin II in cardiac cells. Our results indicate that taurine is an effective inhibitor of angiotensin II action.
N ε-(Carboxymethyl)lysine (CML), which is formed by the glycation of collagen, is a skin-accumulating advanced glycation end product and has been shown to be deeply involved in diabetic osteopenia and skin aging. In this study, we prepared the phlorotannins of marine algal polyphenols from Japanese Lessoniaceae ( Ecklonia cava, Ecklonia kurome, cultured E. kurome, Ecklonia stolonifera, Eisenia nipponica, and Eisenia bicyclis) and evaluated their inhibitory activities against CML formation in a collagen-glyoxal environment. The level of CML formed from the glycation of collagen by glyoxal was detected using an enzyme-linked immunosorbent assay. Except for E. stolonifera, the level of CML formation in the treatment with crude phlorotannins at 0.16 µg/mL was found to be comparable to that in the treatment with 0.40 mM aminoguanidine hydrochloride (AG) which is a typical antiglycation agent. In the test using phloroglucinol and isolated eckols (eckol, fucofuroeckol A, phlorofucofuroeckol A, dieckol, and 8,8’-bieckol) at a concentration of 0.80 µg/mL, the level of CML formed was lower for each compound, except for phlorofucofuroeckol A, than the data obtained with the addition of 2.0 mM AG. The mass concentration of 0.80 µg/mL was converted to 6.3 µM for phloroglucinol, 2.2 µM for eckol, 1.7 µM for fucofuroeckol A, 1.3 µM for phlorofucofuroeckol A, and 1.1 µM for dieckol and 8,8’-bieckol. From a comparison of the molar concentrations, it was found that phloroglucinol and the eckols inhibited the formation of CML resulting from glycation of collagen by glyoxal at concentrations of approximately 317 to 1818 times lower than AG.
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