Hi there! Newbie just joined this week but have been listening to two keto dudes for a while and off and on trying to figure out keto.
I’ve been pretty good getting back on track. Today I actually had an amazing day, and only had about 10 carbs and high levels of fat. Haven’t eaten for a few hours and all of a sudden I feel nauseas and kind of shaky.
I measured my glucose and it’s at 208 mg/dL. I’ve never had high glucose readings… what could be going on?
And now, less than an hour later, I’m feeling better and I’m back down to 90.
Could have been a strip error or your blood glucose went very low so your liver helped out by dumping some for you.
I’m thinking it had to be an error… It was just odd that it coincided with me feeling weird.
I’d go with error plus coincidence for now. I’m pre-diabetic & I’ve never seen a number that high. If you get the same feeling again then test again but make sure your hands are well washed & dried.
Stress hormones can raise glucose in even perfectly healthy people. Not sure if you’re familiar with Mike Mutzel from High Intensity Health but his glucose spiked to 190 or something when he nearly missed a connecting flight & he’s a seriously healthy specimen. So long as it’s rare & short lived I’m not sure it’s a problem 
Just a surface guess (in-case it is not just a faulty reading) but amongst other possible causes; it could be a combination of your own body fat and maybe (a big maybe?) exceeding your carbohydrate intake with too much fat (a possible type of carbohydrate) and your body is trying to compensate for the lack of carbohydrates; in other words 10 grams of carbs (if I am interpreting your post correctly?) may be too low for a beginner (…and if you are diabetic?) and it is being turned back into glucose and that is a very slow conversionary process and your just starting out so that may explain the high glucose readings!
References:
- Turning Fats Into Glucose: Excess glucose in the body is converted into stored fat under certain conditions, so it seems logical that glucose could be derived from fats. This process is called gluconeogenesis, and there are multiple pathways the body can use to achieve this conversion. Gluconeogenesis generally occurs only when the body cannot produce sufficient glucose from carbohydrates, such as during starvation or on a low-carbohydrate diet. This is less efficient than producing glucose through the metabolizing of carbohydrates, but it is possible under the right conditions. …More
- The Bottom Line: Your body cannot convert fats directly into muscle-ready glycogen. However, through a series of metabolic processes that result from conditions of depleted carbohydrates, it is possible for stored fats to be broken down into glucose, which can then be converted into glycogen. But carbohydrates are immediately and easily converted into glucose, so metabolizing them is the most efficient way for your body to produce glycogen. …More
- Correcting glutathione deficiency to restore mitochondrial fat oxidation in aging: Supplementing diets of older mice with cysteine and glycine for 6-weeks corrected GSH deficiency in muscle and liver, restored whole-body NEFA oxidation, and lowered total body fat, hepatic fat and body weight. These data suggest that in aging, GSH deficiency predisposes to impaired NEFA oxidation and excess body and tissue fat; correcting GSH deficiency by supplementing cysteine and glycine in the diet restores NEFA oxidation and reverses these defects. …More
Wow! That’s a lot of science!
Not a diabetics, I’ve actually never had a high glucose reading. Ever. However, today is probably the lowest I’ve kept my carbs and the highest level of fat intake I’ve consumed. I’m just going to keep a close eye on how I react over the weekend. Very strange for me.
Yes a close eye on that glucose! Another good read if you have time:
Fat and Diabetes: Bad Press, Good Paper, and the Reemergence of Our Good Friend Glutathione - Chris Masterjohn “… The authors of this study did not measure glutathione levels, but the hypothesis that glutathione is protective is consistent with a study I wrote about in a post back in January, “Eating Fat and Diabetes.” In that study (6), high-fat diets depleted glutathione and impaired insulin sensitivity and glucose tolerance in rats and mice, but treating the rats with a mitochondrial antioxidant and genetically engineering the mice to make lots of the antioxidant enzyme catalase both reversed these effects. Catalase is an enzyme that converts hydrogen peroxide to water. …” “…If this is correct, does a “high-fat diet” cause diabetes? The obvious question that must follow is “which high-fat diet?” An anti-inflammatory, invigorating, nutrient-dense diet likely protects against diabetes regardless of whether it is low or high in fat. …”
How Does This All Fit Together?
When mitochondria are overloaded with more energy than they can handle, they begin making increasing amounts of the free radical superoxide. Superoxide carries out important signaling roles. Among them, it directs excess energy into fat synthesis. But it can also wreak havoc on the cell by forming oxidants that can damage vulnerable proteins, lipids, and other important molecules. Thus, a manganese-dependent enzyme called superoxide dismutase converts it into hydrogen peroxide. Hydrogen peroxide can also damage important molecules, but increasing evidence suggests it also regulates the activity of hundreds of proteins by controlling several “redox switches,” including glutathione.
An interesting picture begins to emerge as a working hypothesis:
- When the mitochondria’s capacity to burn lipids and fats in order to make ATP is overloaded, it makes signals such as superoxide that will redirect incoming energy to be stored as fat.
- Superoxide also generates hydrogen peroxide, which oxidizes glutathione and thereby flips a “redox switch” controlling a multitude of proteins. These proteins may then help the cell stop responding to insulin in order to minimize energy overload.
- This is a desperate attempt of the cell to protect itself from oxidants that would otherwise destroy its basic machinery, and has the unfortunate consequence of increasing glucose and other forms of energy in the blood, and thus contributing to the metabolic abnormalities we associate with diabetes.
- Supporting the cell’s antioxidant defense network helps it to handle more energy and thereby protects against this entire process. Thus, providing NAC to cells, synthetic mitochondrial antioxidants to rats, or extra catalase to mice all seem protect against the development of diabetes-like features in the face of energy overload. …More
Overview on working hypothesis:
Glycine (searchable database of the methionine/glycine balance of almost 4000 foods)
Cysteine (Top 10 Foods Highest in Cysteine)
Glutathione & Glutathione synthetase deficiency (10 Natural Ways to Increase Your Glutathione Levels)
Catalase (Vegetable & Fruit Sources of Catalase) Onions (highest concentrations) & Wheat Grass
Deficiencies could impair weight loss on a high fat diet or low fat diet and contribute to diabetes and possibly liver damage?
Footnotes:
- “… A 2011 study published in the American Journal of Clinical Nutrition found that although glutathione deficiency in elderly people occurs because of a marked reduction in synthesis, supplementation with the glutathione precursors cysteine and glycine fully restores glutathione synthesis. This helps increase concentrations and lowers levels of oxidative stress and oxidant damages that lead to aging. (7) - Dr. Josh Axe
- “…The reason it is important to balance these amino acids is that consuming too much methionine can deplete our glycine levels. Methionine is especially abundant in eggs, dairy, meat, poultry, and fish. Glycine is especially abundant in skin and bones. While our ancestors tended to eat “nose-to-tail,” making liberal use of the skin and bones of the animals they ate, we tend to eat the meat and throw out the skin and bones. For example, skinless, boneless chicken breast is rich in methionine, but the glycine-rich skin and bones have been removed. …” - Chris Masterjohn
- Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen peroxide to water and oxygen.[5] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.[6] …More
- “…Some research has indicated that a lack of catalase can lead to the development of type 2 diabetes. It seems that some other molecules within living organisms are able to sufficiently break down hydrogen peroxide—enough to sustain life. The toxic nature of hydrogen peroxide also makes it a powerful disinfectant. …” …More
- Human catalase: Looking for complete identity: There are very few articles available on the synthesis of catalase in mammalian systems. The events occur during the synthesis of catalase by which heme is loaded in tetramer and the entry into peroxisomes is not clearly elucidated. The computer simulation proved that SNP (single nucleotide polymorphism) in catalase gene may translate in the form of presence of different amino acid in wild type polypeptide chain. This can cause decrease or complete loss of enzyme activity (Wood et al., 2008). In the face of few available reports, detail screening is required to identify these variations. In a recent review some gray areas related to catalase structure, function and mechanism of action have been discussed (Kirkman and Gaetan, 2007). It shows that the presence of NADPH with enzyme is not completely under-stood. The conversion of DNA damaging solar radiation into less energetic oxidant species ROS by catalase is novel and previously unrecognized activity (Heck et al., 2003). In erythrocytes, GPx is capable to remove endogenously produced H2O2 thus the role of catalase is thought to be to remove exogenous H2O2 (Johnson et al., 2010). As erythrocytes circulate in the entire body system, the role of catalase in regulation of systemic radox status (H2O2 flux) and comparative load bearing capacity against stress among other antioxidant enzymes like glutathion peroxidase and thioredoxin is yet to be explored. As Kirkman and Gaetani (2007) titled the mammalian catalase ‘a venerable enzyme with new mysteries’, the enzyme coming out with new unexplained properties corroborates with the title and presents a scope for further research …More
- Glutathione peroxidase (GPx) (EC 1.11.1.9) is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water. …More