MCT for Health

That sugar isn’t healthy is something almost everyone knows today, even if they don’t really care or restrict themselves. But that sugar could be harmful even without sugar in food? That sounds strange, doesn’t it? Do we have evidence, studies, results? Yes, I think we do. I found a nice PhD dissertation that tries to answer exactly this question. And the results are very interesting. I’ll try to summarize them briefly here. In discussions on X, I came across a great experimenter in the field of nutrition. He runs his blog at exfatloss.com . Recently, he raised an interesting point about the low-carb keto diet . For some people, it simply doesn’t work, and no one knows why. He observed this himself and shares his findings with others on his blog. The idea came to him while listening to lectures by Rick Johnson, M.D., on fructose research. Specifically, that the body produces fructose on its own, for example, with too much salty food and a lack of water, or when consuming food containin...

Let’s continue considering whether some level of protein restriction, even occasional, might lead to better metabolism and longer life. Although it may seem obvious that restricting food intake should prolong life, in the previous post this was not the case . The longest lifespan was observed in mice that consumed the most essential amino acids as their protein source (20% cal in the diet). Overall, this was not a deficient diet at all. On the contrary, a very rich diet that excluded unnecessary amino acids—which the body can synthesize as needed—ensured the mice’s health. This could serve as a warning for us: restricting these indispensable nutrients might not be such a good idea, as it may not lead to better health or longer life. Still, in some cases, it might appear that way. Let’s try a different approach. We know of one amino acid that has a proven effect on cellular aging. It’s called taurine. We’ve already come across it once before when I discussed the effects of restricting s...

The content of individual specific amino acids in proteins seems to be key to maintaining a healthy metabolism. A change in composition by restricting certain amino acids leads to overeating, but also to greater wasting of energy as heat, so weight gain does not occur . Recent studies in mouse models clearly show that branched-chain (BCAA) and sulfur amino acids (SAA) play an interesting role here. While the mechanism for branched-chain ones is still very unclear, for sulfur amino acids the most likely mechanism of action appears to be S-sulfhydration of enzymes . For branched-chain acids, I would guess that the mechanism could be transamination to glutamate, which is metabolized in the TCA cycle in two different ways depending on the metabolic state. Either it is further processed via oxaloacetate into glucose, and then everything works normally, or it is processed by reverse run of IDH2 into citrate and then into fat . And that is the essential difference, which however is not descr...

This post will once again be dedicated to hydrogen sulfide (H2S). The studies mentioned in previous posts have shown quite clearly how beneficial hydrogen sulfide produced in liver cells by the enzyme CSE can be. It can even be transported further into the whole body through S-sulfhydration of blood albumin . But will this also apply to hydrogen sulfide produced in the colon? Let’s take a look at what the authors of a study examining the influence of hydrogen sulfide on intestinal epithelial cell metabolism found. They also studied this in connection with obesity and a diet rich in fats and sugars. The basic idea is that the effect of a diet high in saturated fats on the development of obesity could be either supported or, conversely, blocked by hydrogen sulfide. We first need to clarify the conditions under which this research was conducted. It was done on obese mice, where obesity was induced by a fatty diet high in coconut oil and sugar, together with a low content of polyunsaturat...

We continue with the effects of hydrogen sulfide on enzyme activity. We have already seen that H₂S affects the S-sulfhydration of sirtuins, i.e., the activity of deacetylases that change the activity of many enzymes by preventing their “decoration” with an acetyl group . In the case of sirtuin modification, for example, this facilitates the “decoration” of some enzymes with ubiquitin, which leads to their removal. Or it increases their activity after the removal of acetyl “decoration,” if that decoration interferes with the enzyme’s function. Even at this level, things are already quite complicated. But that’s not all. S-sulfhydration of certain sites can occur on many proteins, not just on sirtuins! Research shows that H₂S also sulfhydrates the enzyme pyruvate carboxylase (PC) and also the key metabolic switch, the enzyme AMPK. That would explain further phenomena observed both in vitro (in the test tube) and in vivo (in whole organisms) related to changes in hydrogen sulfide levels. ...