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Shibuya-ku, Japan

A Tie2 activator containing, as an active ingredient, a hawthorn extract, a starfruit extract, a shellflower extract, a lotus extract, a rooibos extract, an Indian date extract, a Chinese quince extract, a Psidium guava extract, a long pepper extract, a Quillaja extract, a Kouki extract, a ginkgo extract, an oyster extract, a turmeric extract, a chrysanthemum extract, a jujube extract, a Chinese wolfberry extract, a chamomile extract, or a Butchers Broom extract, or any combination thereof.

Usuki H.,Research Institute for Biological science RIBS | Usuki H.,Japan Society for the Promotion of Science | Yamamoto Y.,Research Institute for Biological science RIBS | Arima J.,Tottori University | And 4 more authors.
Organic and Biomolecular Chemistry

A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach. © 2011 The Royal Society of Chemistry. Source

Mizushina Y.,Kobe Gakuin University | Kuriyama I.,Kobe Gakuin University | Nakahara T.,Maruzen Pharmaceuticals Co. | Kawashima Y.,Maruzen Pharmaceuticals Co. | Yoshida H.,Kobe Gakuin University
Food and Chemical Toxicology

We found that the ethanol extract of mangosteen (Garcinia mangostana L.) fruit rind had a strong inhibitory effect on mammalian DNA polymerase (pol) activity and isolated α-mangostin as a potent pol inhibitor from the extract. In this study, the inhibitory activities against mammalian pols by α-mangostin and its related five compounds, 3-isomangostin, xanthone, 9,10-anthraquinone, 9-anthracenecarboxylic acid, and anthracene, were investigated. α-Mangostin was the most potent inhibitor of the mammalian pol species among the tested compounds, with IC50 values of 14.8-25.6μM. This compound also inhibited human DNA topoisomerases (topos) I and II activities with IC50 values of 15.0 and 7.5μM, respectively, but did not inhibit the activities of other DNA metabolic enzymes tested. α-Mangostin also did not directly bind to double-stranded DNA as determined by thermal transition analysis. α-Mangostin was found to suppress human colon HCT116 carcinoma cell proliferation with an LC50 of 18.5μM, inhibit the activity of cellular topos, halt cell cycle in the G2/M phase, and induce apoptosis. These results suggest that decreased proliferation by α-mangostin may be a result of the inhibition of cellular topos rather than pols, and α-mangostin might be an anticancer chemotherapeutic agent. © 2013 Elsevier Ltd. Source

Miyake Y.,Maruzen Pharmaceuticals Co. | Aoyama N.,Maruzen Pharmaceuticals Co. | Matsuyama A.,Takeyama Medical Clinic
Japanese Pharmacology and Therapeutics

Objectives To investigate the dermatological effects of an Alpinia zerumbet leaves extract (ALE) on the skin of Japanese females. Methods A randomized, placebo-controlled, double-blind, parallel-group comparative study was conducted on 20 healthy females who provided informed consent. Subjects took either a beverage containing ALE or a placebo beverage once daily for eight consecutive weeks, and skin moisture content, transepidermal water loss, and skin elasticity were determined, in addition to skin texture replica analysis. Results A non-significant increase in skin moisture content was observed in the placebo group, while a significant increase in skin moisture content and a significant decrease in trans- epidermal water loss were observed in the ALE group. A significant increase in skin elasticity was also observed in the ALE group, whereas the skin replica analysis showed significant increases in the number of skin textures in both groups. No clinically relevant adverse events were observed throughout the study. Conclusion These findings suggested that the ALE may prevent skin dryness, moisturize the skin, and enhance skin elasticity. It was also suggested that the ALE is safe for consumption as a useful functional food. Source

Maruzen Pharmaceuticals Co. | Date: 2009-09-29

Flavor enhancers used in food and beverage products; food additives including licorice root extract for non-nutritional purposes for use as a flavoring; sugar substitute.

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