dipropyl disulfide/発がん過程

The mechanism of differential efficacies of diallyl sulfide (DAS), diallyl disulfide (DADS), diallyl trisulfide (DATS), dipropyl sulfide (DPS) and dipropyl disulfide (DPDS) in preventing benzo(a)pyrene (BP)-induced cancer in mice has been investigated by determining their effects on the enzymes of

Natural compounds which elevate detoxification enzymes and/or reduce activating enzymes could be considered as good candidates to protect against cancer. In this work, we studied the modulation of hepatic drug-metabolizing enzymes in rats treated with dimethyl sulfide (DMS), dimethyl disulfide

We have shown previously that the chemoprotective activity of diallyl disulfide (DADS), a naturally occurring anticancer agent in garlic, against benzo[a]pyrene (BP)-induced forestomach carcinogenesis in mice correlates strongly with its inductive effects on the expression of Pi class glutathione

There is a growing need for short-term and cost-effective bioassay to assess the efficacy of potential chemo-preventive agents. We report that the induction of glutathione (GSH) S-transferase pi (mGSTP1-1) by a chemo-preventive agent can be used as a reliable marker to assess its efficacy in

Organosulfur compounds (OSCs) derived from garlic have been studied for the ability to inhibit experimental cancer in various animal models, primarily through modification of carcinogen detoxification enzymes, such as cytochrome P450 (CYP) enzymes. OSCs vary in structural and physical properties,

Water extracts of garlic, deodorized garlic powder, and onions, but not leeks, were found to significantly (p < 0.05) reduce the in vitro formation of N-nitrosomorpholine (NMOR), a known liver carcinogen. Addition of increasing quantities (20, 40, and 80 mM) of S-allyl cysteine (SAC), a

In a previous study, we showed that naturally occurring organosulfur compounds (OSCs) from garlic and onion modulated the activation of carcinogen via the alteration of cytochromes P450. The present study was undertaken to determine the incidence of the in vivo induction of phase II enzymes by