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| Methionine (MET) restriction (MR) has been shown to arrest cancer growth and sensitizes tumors to chemotherapy. -Many cancer cells rely heavily on exogenous methionine to sustain rapid growth and proliferation because they often have impaired methionine salvage pathways. -Methionine contributes to the synthesis of glutathione, a key antioxidant. (Methionine is a precursor of glutathione, a tripeptide that reduces reactive oxygen species.) -MR diets might influence the redox state of cancer cells, increasing oxidative stress and thereby leading to cell death in metabolically compromised tumor cells. -Proliferation and growth of several types of cancer cells are inhibited by MR, while normal cells are unaffected by limiting methionine as long as homocysteine is present. -Methionine restriction is effective when the non-essential amino acid, cysteine, is absent from the diet or media. methionine is the precursor for cysteine which is essential for the formation of GSH. -Malignant cells lack the enzyme required to recycle homocysteine therefore giving methionine restriction the capacity to alter cancer cells while maintaining normal, healthy cells. While vegan diets are typically low in methionine, some nuts and legumes (such as Brazil nuts and kidney beans) are rich in methionine. Foods to avoid for MR diet: Animal Proteins: -Red Meat (Beef, Pork, Lamb): -Poultry (Chicken, Turkey): -Fish and Seafood: -Eggs: Both the egg whites and yolks are protein rich. -Dairy Products: Milk, cheese, and yogurt Certain Plant Proteins: -Soy Products: -Legumes: Protein Supplements: Foods Lower in Methionine (Often Favorable on an MR Diet) Fruits & Vegetables: leafy greens, berries, apples, and citrus fruits. Grains & Cereals: rice, oats, and barley Nuts and Seeds: can vary in methionine content. Alternative Protein Sources: emphasize protein sources with a lower methionine-to-cysteine ratio.
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| Glutathione S-transferases (GSTs) are a family of phase II detoxification enzymes that play key roles in catalyzing the conjugation of glutathione (GSH) to a wide range of electrophilic compounds. This family includes multiple isoenzymes (e.g., GST-α, GST-μ, GST-π) with tissue-specific expression patterns and overlapping as well as distinct substrate specificities. -GSTs are important for detoxifying potentially harmful compounds, including products of oxidative stress, environmental toxins, and chemotherapeutic agents. -They contribute to the cellular defense mechanism against oxidative damage and help maintain cellular redox balance. -Beyond detoxification, GSTs can modulate cell signaling pathways, potentially affecting cell proliferation, apoptosis, and drug resistance. -GST-π is commonly upregulated in several cancers such as breast, lung, colorectal, and hematologic malignancies. -Elevated expression of specific GST isoenzymes—most notably GST-π—has been associated with a poorer prognosis in several cancer types. This is often linked to resistance to chemo- or radiotherapy, as higher GST activity can lead to more efficient detoxification of these agents, reducing their cytotoxic effects. -In contrast, reduced GST expression in some contexts might indicate a less robust detoxification system, which can correlate with increased sensitivity to oxidative stress and possibly a less aggressive tumor phenotype. |
| 2272- | dietMet, | Methionine restriction - Association with redox homeostasis and implications on aging and diseases |
| - | Review, | Nor, | NA |
Query results interpretion may depend on "conditions" listed in the research papers. Such Conditions may include : -low or high Dose -format for product, such as nano of lipid formations -different cell line effects -synergies with other products -if effect was for normal or cancerous cells
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