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Ketogenesis

Ketogenesis is a primarily occurring in the hepatic mitochondria, where derived from fatty acid β-oxidation is converted into —acetoacetate, β-hydroxybutyrate, and acetone—serving as water-soluble alternative fuels for extrahepatic tissues during periods of low glucose availability, such as or . Ketone bodies were first discovered in the mid-19th century in the urine of patients with diabetes mellitus. The process is promoted under conditions of low insulin and high counter-regulatory hormones like , , catecholamines, and . The liver produces but does not utilize due to the absence of the succinyl-CoA:3-ketoacid CoA (SCOT). Physiologically, after prolonged , can supply up to 70% of the brain's requirements and contribute 5–20% to total expenditure, yielding approximately 22 ATP per upon oxidation in peripheral tissues. Beyond provision, they support metabolic flexibility, act as signaling molecules, and inhibit . Clinically, excessive ketogenesis contributes to , while controlled via ketogenic diets offers therapeutic benefits for , neurodegenerative diseases, and certain metabolic disorders.

Overview

Definition and Physiological Role

Ketogenesis is the biochemical process occurring primarily in the mitochondria of hepatocytes, where derived from the beta-oxidation of fatty acids is converted into the acetoacetate, β-hydroxybutyrate, and acetone, serving as an alternative fuel source during periods of limited availability. This pathway enables the liver to export water-soluble into the bloodstream for utilization by extrahepatic tissues unable to directly oxidize fatty acids. Physiologically, ketogenesis plays a crucial role in maintaining energy homeostasis by providing an efficient energy substrate—yielding approximately 22 ATP molecules per ketone body—for vital organs such as the brain, heart, and skeletal muscles when glucose supplies are depleted. In states of carbohydrate limitation, such as fasting, ketone bodies spare glucose for tissues that depend on it exclusively, thereby preventing the breakdown of muscle proteins to generate gluconeogenic substrates and preserving lean body mass. During prolonged fasting, ketone bodies can fulfill up to 60-70% of the brain's energy requirements, supporting cognitive function without risking hypoglycemia. This metabolic adaptation represents an evolutionarily conserved mechanism in mammals, enabling survival during episodes of food scarcity by efficiently mobilizing stored for production. Comparative physiological studies in hibernating , such as ground squirrels, demonstrate elevated serum β-hydroxybutyrate levels during , highlighting ketogenesis's role in sustaining prolonged periods of nutrient deprivation with minimal . The process is initiated under conditions of low insulin levels, which promote in to increase free fatty acid delivery to the liver, thereby fueling production without involving detailed downstream enzymatic steps.

Historical Discovery

The discovery of ketogenesis originated in the mid- with observations of acidic compounds in the of patients with diabetes mellitus. In 1857, Czech physician Wilhelm Petters identified acetone as a component of diabetic , recognizing its distinctive and linking it to metabolic disturbances. This was followed in 1865 by Carl Gerhardt's isolation of (initially termed "diacetic acid") from the same source, which explained the urine's acidic properties. By the late , the fruity of acetone in diabetic breath had been associated with this compound, solidifying early associations between these substances and diabetic pathology. These findings, primarily from European chemists including French and German researchers, marked the initial recognition of as pathological byproducts rather than normal metabolites. The late 19th century saw the identification of the third major ketone body, β-hydroxybutyric acid, isolated from diabetic urine, complementing the known structures of acetone and acetoacetic acid. Breakthroughs in understanding the biosynthetic pathway accelerated in the 1930s, as biochemists linked ketogenesis to breakdown and excess from beta-oxidation. Pioneering work by M. Jowett and J.H. Quastel in 1935, using liver tissue preparations, demonstrated ketone production from , while Philip P. Cohen's 1937 studies further clarified the process in hepatic slices. Concurrently, Hans Adolf Krebs's elucidation of the in 1937 provided the framework for viewing ketogenesis as an "overflow" pathway when was limited, preventing accumulation. These experiments shifted the perspective from mere to a regulated metabolic . Post-1950s research identified key regulatory mechanisms, including the discovery of 3-hydroxy-3-methylglutaryl-CoA () synthase as the rate-limiting enzyme in ketogenesis by Minor J. Coon and B.K. Bachhawat during the 1950s at the University of Illinois, confirming its role in condensing units in liver mitochondria. Clinically, Russell M. Wilder's 1921 proposal of the for —predating modern revivals—highlighted ketogenesis's therapeutic potential by inducing controlled to mimic fasting's effects, a concept validated in trials at the . The 1970s resurgence, led by John M. Freeman and colleagues at , refined dietary protocols and reestablished ketogenesis as a viable intervention for refractory . Recent milestones from the onward have leveraged advanced imaging to explore ketogenesis in normal and disease. () studies in the , such as those by Stephen Cunnane's group, revealed enhanced uptake and utilization of during aging and , compensating for declining glucose with up to 2-3-fold increases in ketone flux. In the 2020s, preclinical research in models has demonstrated that ketogenic interventions improve memory outcomes in studies by enhancing neuronal energy supply via beta-hydroxybutyrate. These advances underscore ketogenesis's evolving role beyond crisis response to neuroprotective adaptation.

Biochemical Pathway

Fatty Acid Mobilization and Beta-Oxidation

Fatty acid mobilization begins with in , where triglycerides stored in adipocytes are hydrolyzed to release free fatty acids (FFAs) and . This process is primarily mediated by hormone-sensitive (HSL), which catalyzes the of triglycerides into FFAs and under conditions of low insulin and high levels, such as during . Low insulin reduces the inhibitory of HSL, while activates adenylate cyclase, increasing levels that promote HSL activation through A-mediated . The released FFAs are transported in the bloodstream bound to , which serves as the primary carrier protein due to its high capacity for long-chain s. Upon reaching the liver, these albumin-bound FFAs dissociate and enter hepatocytes primarily via facilitated mechanisms involving proteins such as ( translocase) and members of the (FATP) family, including FATP1 and FATP5, which enhance uptake across the plasma membrane. Within hepatocytes, FFAs are activated to esters in the and then transported into the mitochondria via the carnitine shuttle system for beta-oxidation, a key catabolic pathway that generates precursors for ketogenesis. Beta-oxidation occurs in the and involves the sequential removal of two-carbon units from the chain, producing , NADH, and FADH₂. The process consists of four enzymatic steps repeated for each two-carbon unit removed:
  1. Dehydrogenation by , forming a trans and reducing to FADH₂.
  2. by enoyl-CoA hydratase, adding water across the double bond to form 3-hydroxyacyl-CoA.
  3. Oxidation by 3-hydroxyacyl-CoA dehydrogenase, converting the hydroxyl group to a keto group and reducing NAD⁺ to NADH.
  4. Thiolysis by beta-ketothiolase, cleaving the beta-ketoacyl-CoA with to yield and a shortened .
For a representative even-chain saturated fatty acid like palmitate (C16:0), which is converted to palmitoyl-CoA, complete beta-oxidation requires seven cycles, yielding eight molecules of along with reduced cofactors: \text{Palmitoyl-CoA} + 7 \text{ CoA} + 7 \text{ FAD} + 7 \text{ NAD}^+ + 7 \text{ H}_2\text{O} \rightarrow 8 \text{ Acetyl-CoA} + 7 \text{ FADH}_2 + 7 \text{ NADH} + 7 \text{ H}^+ This equation illustrates the stoichiometry for palmitoyl-CoA, highlighting the production of as the primary carbon source for downstream . In the context of ketogenesis, conditions such as prolonged fasting lead to elevated rates of beta-oxidation in the liver, generating excess that exceeds the capacity of the tricarboxylic acid () . The high NADH/NAD⁺ ratio resulting from beta-oxidation inhibits key TCA enzymes, including and alpha-ketoglutarate dehydrogenase, thereby limiting acetyl-CoA oxidation and diverting it toward ketone body synthesis. This imbalance ensures that acetyl-CoA accumulates sufficiently to fuel hepatic ketogenesis under energy-demanding states.

Ketone Body Formation

Ketogenesis involves the mitochondrial synthesis of from excess , primarily in the liver, when the capacity of the is exceeded, such as during high rates of beta-oxidation. This pathway diverts units into water-soluble —acetoacetate, β-hydroxybutyrate, and acetone—for export to extrahepatic tissues as an alternative fuel source. The process is irreversible under physiological conditions and is confined to the . The pathway begins with the condensation of two molecules to form acetoacetyl-CoA, catalyzed by the (also known as 3-ketothiolase or acetyl-CoA acetyltransferase). This reversible reaction is followed by the addition of another molecule to acetoacetyl-CoA, yielding 3-hydroxy-3-methylglutaryl-CoA (), in a step mediated by , which is the rate-limiting of ketogenesis. is then cleaved by HMG-CoA lyase to produce acetoacetate and one molecule of . The overall reflects a net conversion where two units yield one acetoacetate and regenerate one , effectively producing one body per two acetyl units entering the pathway. These reactions can be summarized as follows: \begin{align*} &2 \text{ Acetyl-CoA} \rightleftharpoons \text{Acetoacetyl-CoA} + \text{CoA} \quad (\text{thiolase}) \\ &\text{Acetoacetyl-CoA} + \text{Acetyl-CoA} + \text{H}_2\text{O} \rightleftharpoons \text{HMG-CoA} + \text{CoA} \quad (\text{HMG-CoA synthase}) \\ &\text{HMG-CoA} \rightleftharpoons \text{Acetoacetate} + \text{Acetyl-CoA} \quad (\text{HMG-CoA lyase}) \end{align*} Acetoacetate serves as the central intermediate and can undergo further conversions: it is reduced to β-hydroxybutyrate in an NADH-dependent reaction catalyzed by β-hydroxybutyrate dehydrogenase (also called 3-hydroxybutyrate dehydrogenase), which predominates under conditions of high NADH/NAD⁺ ratios. Additionally, acetoacetate spontaneously decarboxylates to form acetone, a non-metabolizable byproduct. The pathway is highly specific to the liver due to the abundant expression of these key enzymes, particularly the mitochondrial isoform of synthase, which is upregulated in hepatocytes. The liver lacks the succinyl-CoA:3-ketoacid CoA (SCOT), preventing the reconversion of back to for its own use and ensuring net production for systemic distribution.

Ketone Bodies

Chemical Structures

The three primary produced during ketogenesis are acetoacetate, β-hydroxybutyrate, and acetone. Acetoacetate, with the molecular formula CH₃COCH₂COO⁻, serves as the central precursor among these compounds. It is relatively unstable and possesses a low of approximately 3.6, allowing it to dissociate readily and contribute to acidification when present in excess. β-Hydroxybutyrate, represented by the formula CH₃CH(OH)CH₂COO⁻, is the reduced form of acetoacetate and constitutes the majority of circulating , typically 70-80%. It exhibits greater stability than acetoacetate and interconverts with it through the action of β-hydroxybutyrate dehydrogenase, a process governed by the cellular NADH/NAD⁺ ratio. With a of about 4.7, it remains more protonated under physiological conditions compared to acetoacetate. Acetone, having the formula CH₃COCH₃, is a minor ketone body formed via the irreversible of acetoacetate, yielding acetone and CO₂. It is volatile and lacks significant energy-yielding value, primarily serving as a waste product excreted through breath and . The interconversions among these are key to their dynamics: acetoacetate reversibly equilibrates with β-hydroxybutyrate in a dehydrogenase-catalyzed reaction, while its conversion to acetone is non-enzymatic and irreversible. , β-hydroxybutyrate predominates due to the reductive hepatic environment favoring its formation. Collectively, these molecules are water-soluble and amphipathic, featuring both polar groups and hydrophobic alkyl chains that facilitate their without requiring lipoproteins.

Transport and Utilization

Once synthesized in the liver, ketone bodies such as acetoacetate and β-hydroxybutyrate are exported into the bloodstream primarily via the (MCT1), a proton-linked that facilitates their release down a concentration gradient. This mechanism ensures efficient distribution to extrahepatic tissues, where ketone bodies serve as an source during periods of low glucose availability. In the fed state or brief , circulating ketone body concentrations remain low at less than 0.5 mM, but they can rise to 5-7 mM during prolonged or nutritional , reflecting increased hepatic production and systemic demand. In peripheral tissues including the brain, skeletal muscle, and heart, ketone bodies are taken up via MCT1 and MCT2, which exhibit high affinity for these substrates (Km values around 3-11 mM for MCT1 and lower for MCT2). Upon entry into cells, the rate-limiting step of utilization involves succinyl-CoA:3-ketoacid CoA-transferase (SCOT), a mitochondrial enzyme that activates acetoacetate by transferring CoA from succinyl-CoA, yielding acetoacetyl-CoA and succinate: \text{Acetoacetate} + \text{succinyl-CoA} \rightarrow \text{acetoacetyl-CoA} + \text{succinate} This reaction is reversible and essential for ketone body catabolism in extrahepatic tissues. β-Hydroxybutyrate must first be oxidized to acetoacetate by β-hydroxybutyrate dehydrogenase before undergoing this transfer. Notably, the liver lacks SCOT expression, preventing it from reutilizing the ketone bodies it produces and ensuring net export to other organs. Acetoacetyl-CoA is then cleaved by mitochondrial (ACAT1) into two molecules of , which enter the tricarboxylic acid () by condensing with oxaloacetate to form citrate, ultimately generating ATP through : \text{Acetoacetyl-CoA} + \text{CoA} \rightarrow 2 \text{ [acetyl-CoA](/page/Acetyl-CoA)} Each yields approximately 10 ATP via the and electron transport chain, resulting in a net production of about 22 ATP per molecule of acetoacetate oxidized—less than the 30-32 ATP from complete glucose oxidation but efficient for fuel-sparing during deficits. This process provides a substantial source, with ketones contributing up to two-thirds of the brain's fuel needs after . Tissue-specific adaptations enhance ketone utilization efficiency. In the brain, MCT1 expression is upregulated over several days of , increasing transport capacity and allowing gradual reliance on s to spare glucose. and heart, with abundant MCT1/2 and SCOT, rapidly oxidize s during exercise or , supporting high-energy demands without accumulation. These mechanisms underscore ketogenesis as a conserved pathway for metabolic flexibility across organs.

Regulation

Hormonal Influences

Ketogenesis is primarily regulated by hormonal signals that respond to nutritional states, with insulin acting as the dominant inhibitor and counter-regulatory hormones promoting the process during low-glucose conditions. Low circulating insulin levels de-repress hormone-sensitive lipase (HSL) in , thereby enhancing and the release of free fatty acids (FFAs) that serve as substrates for hepatic ketogenesis. Additionally, suppressed insulin inhibits (ACC), reducing the production of , which normally inhibits carnitine palmitoyltransferase-1 (CPT-1) and thereby blocks beta-oxidation of FFAs in the liver. Insulin concentrations below 10 μU/mL are particularly effective in triggering rapid FFA release, shifting metabolism toward ketone body production. Glucagon, secreted by pancreatic alpha cells in response to low blood glucose, directly stimulates ketogenesis by activating adenylate cyclase in hepatocytes, which elevates levels and subsequently activates . then phosphorylates and activates HSL to promote , while also phosphorylating and inactivating to further decrease inhibition of beta-oxidation. This glucagon-mediated pathway ensures that ketogenesis ramps up efficiently during , complementing the effects of insulin suppression. Other counter-regulatory hormones also contribute to ketogenesis under stress or prolonged . Epinephrine and norepinephrine, released via sympathetic activation, bind to β-adrenergic receptors on adipocytes, stimulating adenylate cyclase and to enhance HSL activity and , thereby increasing FFA availability for hepatic production. , a hormone, indirectly supports ketogenesis by promoting in the liver, which sustains blood glucose while sparing FFAs for oxidation and synthesis during energy deficits. , such as (T3), also promote ketogenesis by enhancing oxidation and in the liver, contributing to increased body production during energy deficits. The interplay between these hormones is critical, with high glucagon-to-insulin molar ratios serving as a key determinant of ketogenesis rate by favoring and FFA flux to the liver. Diurnal variations in states further modulate this , as ketone levels often peak in the early morning due to overnight declines in insulin and rises in and .

Enzymatic and Genetic Controls

Ketogenesis is tightly regulated at the enzymatic level, with mitochondrial 3-hydroxy-3-methylglutaryl-CoA 2 (HMGCS2) serving as the rate-limiting in the pathway. HMGCS2 catalyzes the formation of from acetoacetyl-CoA and , and its expression is upregulated by the alpha (PPARα) , which is activated in response to elevated free fatty acids (FFAs) during states of nutrient deprivation. This induction enhances the flux through the ketogenic pathway, ensuring efficient production of when glucose is scarce. Other key enzymes in ketogenesis, such as acetoacetyl-CoA thiolase (ACAT1) and HMG-CoA lyase (HMGCL), are similarly induced by PPARα, coordinating the overall increase in ketogenic capacity alongside beta-oxidation enzymes. In contrast, the interconversion between acetoacetate and β-hydroxybutyrate is modulated by β-hydroxybutyrate dehydrogenase 1 (BDH1), whose activity is governed by the mitochondrial NADH/NAD⁺ ratio; a high NADH/NAD⁺ favors β-hydroxybutyrate formation, while a low ratio promotes acetoacetate production, thereby adapting ketone body speciation to conditions. Transcriptional and post-translational networks further fine-tune ketogenesis during energy deficits. (AMPK), activated by elevated AMP/ATP ratios, phosphorylates downstream targets to enhance fatty acid oxidation and indirectly promote ketogenesis by increasing availability for HMGCS2. Complementing this, sirtuin 3 (SIRT3), a mitochondrial deacetylase upregulated in , deacetylates and activates HMGCS2 and other beta-oxidation enzymes like long-chain , improving their catalytic efficiency and supporting sustained production. The alpha (PPARα) and forkhead box A2 (FOXA2) transcription factors further regulate this process, with FOXA2 activating genes involved in and ketogenesis during . Genetic variations in ketogenesis genes influence pathway efficiency. Mutations in the HMGCS2 gene, such as missense or splice-site variants, impair enzyme function and lead to hypoketotic , characterized by inadequate production during . Additionally, single nucleotide polymorphisms (SNPs) in HMGCS2 have been associated with altered susceptibility, as seen in where certain variants confer resistance to clinical by modulating enzyme expression. Feedback mechanisms provide negative regulation to prevent excessive ketogenesis. Elevated ketone bodies, particularly β-hydroxybutyrate, inhibit hormone-sensitive lipase (HSL) in , reducing and FFA release through binding to the (HCAR2), though the full downstream signaling remains under investigation. Upstream, produced by (ACC) allosterically inhibits carnitine palmitoyltransferase-1 (CPT-1), blocking entry into mitochondria and thereby limiting beta-oxidation and supply for ketogenesis.

Physiological Contexts

During Fasting and Starvation

During , the body undergoes a phased transition to ketogenesis to maintain as stores diminish. Within 12 to 24 hours, hepatic and muscle reserves are largely depleted, prompting a in from under the influence of counter-regulatory hormones such as and catecholamines. This shift elevates free fatty acid (FFA) availability for hepatic beta-oxidation, initiating body production. By 72 hours, concentrations typically reach 1-2 mM, rising to 4-6 mM after several days, with acetone detectable in breath as a non-invasive marker of . Ketogenesis progressively supplies up to 50% of the 's energy needs by day 3-4, reducing the obligatory glucose requirement from approximately 120 g/day to about 40 g/day, primarily for red blood cells and residual brain demands. In prolonged , whole-body adapts to prioritize fat-derived fuels, with FFAs and accounting for over 90% of expenditure after about two weeks. play a critical role in protein sparing, suppressing from and reducing by up to 50%—from initial rates of 10-12 g/day to 4-6 g/day after several days—as the and other tissues increasingly utilize ketones. This adaptation includes enhanced ketone clearance mechanisms, preventing excessive accumulation while sustaining fuel delivery. Hormonal changes further support the process; for instance, elevated levels amplify , increasing FFA flux to the liver and bolstering ketogenesis without significantly altering insulin dynamics. Metabolic adaptations at the cellular level reinforce ketogenesis' efficiency during nutrient deprivation. In the , (MCT1) expression is upregulated at the blood-brain barrier via peroxisome proliferator-activated receptor delta (PPARδ) activation, facilitating influx and enabling up to two-thirds of cerebral energy from after weeks of . These changes collectively avert by minimizing glucose dependence and conserving lean mass. Evolutionarily, ketogenesis likely conferred survival advantages to early humans, supporting endurance during periods characteristic of lifestyles, where food scarcity was common.

In Exercise and Metabolic Stress

During moderate-intensity , ketogenesis is induced through enhanced and beta-oxidation in the liver, leading to a 2- to 3-fold increase in circulating body concentrations, which can reach 0.5–1.0 mmol/L after prolonged sessions. These s provide an alternative fuel source for , contributing approximately 10–20% of energy demands under fasted conditions, thereby supporting sustained oxidative without excessive reliance on . This shift helps maintain as availability diminishes over time. Key mechanisms underlying this process include the release of catecholamines, such as epinephrine and norepinephrine, which accelerate free fatty acid (FFA) mobilization from , providing substrates for hepatic beta-oxidation and subsequent ketone production. In , upregulation of (MCT1) enhances uptake and oxidation, particularly following adaptations that increase MCT1 expression by up to 50–100% in response to repeated aerobic stimuli. Post-exercise, elevated s facilitate recovery by suppressing accumulation—reducing plasma levels by 20–50% compared to carbohydrate-fueled conditions—and mitigating through anti-glycolytic effects. In metabolic stress scenarios like sepsis or trauma, cortisol and epinephrine drive ketogenesis by promoting lipolysis and FFA delivery to the liver, despite inflammatory suppression of beta-oxidation and elevated insulin. This adaptive response protects tissues from oxidative damage, as ketones such as β-hydroxybutyrate act as antioxidants by activating pathways like Nrf2 and inhibiting histone deacetylases, thereby reducing reactive oxygen species by 30–50% in affected organs like the heart and kidneys. Such mechanisms underscore ketones' role in preserving mitochondrial function during acute inflammatory states. Trained endurance athletes exhibit heightened ketogenic capacity, with long-term adaptations allowing fat oxidation rates to increase by 20–30% during submaximal exercise, as seen in ultra-endurance runners maintaining 1.5–2.0 g/min utilization after keto-adaptation. Low-carbohydrate training regimens further amplify this by enhancing enzymatic expression for beta-oxidation and , improving overall metabolic flexibility and delaying fatigue in prolonged events. However, limitations arise in intense , where high glycolytic demands elevate insulin and , suppressing ketogenesis and reducing oxidation to negligible levels due to preferential use. Over-reliance on ketogenesis without complete can lead to incomplete fuel switching, risking and impaired high-intensity performance, as evidenced by 10–20% decrements in anaerobic power output during early phases.

Clinical Implications

Pathological Disorders

Pathological disorders of ketogenesis arise from dysregulation in ketone body production, leading to either excessive accumulation causing life-threatening or deficient production resulting in metabolic crises such as . These conditions highlight the critical balance of ketogenesis in maintaining during nutrient scarcity, with disruptions often triggered by underlying diseases, genetic defects, or environmental factors. Excessive ketogenesis, as seen in various forms of , overwhelms buffering systems and leads to severe , while deficiencies impair the adaptive response to , precipitating hypoketotic states. Diabetic ketoacidosis (DKA) is the most common pathological excess of ketogenesis, primarily occurring in due to absolute insulin deficiency, which promotes unchecked and hepatic ketone production. This results in , , and characterized by arterial pH below 7.3, serum bicarbonate less than 18 mEq/L, and an elevated greater than 10 mEq/L, with serum levels often exceeding 3 mmol/L for β-hydroxybutyrate. In severe cases, total concentrations can surpass 15 mmol/L, exacerbating through accumulation of acetoacetate and β-hydroxybutyrate, which dissociate into hydrogen ions. , another form of excessive ketogenesis, typically affects chronic alcohol users who experience acute superimposed on consumption; inhibits while promoting fatty acid oxidation, leading to buildup without significant . This condition presents with , elevated , and β-hydroxybutyrate levels often above 3 mmol/L, compounded by and low stores. Deficiency syndromes in ketogenesis stem from inborn errors impairing the pathway, notably mitochondrial 3-hydroxy-3-methylglutaryl-CoA 2 (HMGCS2) deficiency and medium-chain (MCAD) deficiency. HMGCS2 mutations disrupt the rate-limiting step in ketogenesis, causing hypoketotic that manifests in infancy, typically before age 3, with recurrent episodes of , , seizures, and during fasting or illness; affected individuals exhibit low serum β-hydroxybutyrate despite , reflecting impaired ketone synthesis. MCAD deficiency, the most prevalent oxidation disorder, impairs β-oxidation of medium-chain s, indirectly reducing availability for ketogenesis and leading to hypoketotic , , and in young children, often triggered by fasting or infection. These genetic defects are autosomal recessive and diagnosed through or acute presentations. Other pathologies include starvation ketoacidosis, observed in severe where prolonged caloric restriction depletes and induces excessive ketogenesis, resulting in with β-hydroxybutyrate levels above 3 mmol/L and potential euglycemia. In the , euglycemic DKA has been increasingly reported in patients on sodium-glucose cotransporter 2 (SGLT2) inhibitors, where these drugs promote glucosuria and relative insulin deficiency, leading to accumulation with blood glucose below 250 mg/dL, pH less than 7.3, and above 12, often in or infectious settings. Diagnosis of these disorders relies on clinical presentation combined with laboratory findings, including serum β-hydroxybutyrate greater than 3 mmol/L indicating significant , alongside an exceeding 12 mEq/L for confirmation; gas showing below 7.3 and low further supports . For inborn errors like HMGCS2 or MCAD deficiencies, via targeted sequencing or newborn metabolic screening identifies mutations, often accompanied by urinary analysis revealing dicarboxylic aciduria in oxidation defects. Outcomes vary by condition and timeliness of intervention; untreated DKA carries a of 1-5%, primarily from , arrhythmias, or multiorgan failure, though rates drop below 1% with prompt treatment. Enzyme deficiencies such as HMGCS2 and MCAD are managed lifelong by frequent feeding every 4-6 hours to prevent -induced crises, avoidance of prolonged , and provision during illness, significantly improving prognosis and preventing seizures or .

Therapeutic Uses

The , characterized by a high-fat, low-carbohydrate composition typically in a 4:1 ratio of fats to proteins and carbohydrates combined, serves as an established for refractory in children, achieving greater than 50% reduction in approximately half of treated patients. This efficacy stems from mechanisms such as enhanced synthesis in the and modulation of ATP levels in neuronal mitochondria, which contribute to effects. Additionally, the primary body beta-hydroxybutyrate reduces seizure-like activity through KATP channel and GABAB receptor-dependent pathways. In metabolic therapies, the shows promise for by providing ketones as an alternative energy source to bypass glucose hypometabolism in the brain, with clinical trials in the demonstrating improvements in cognitive outcomes, such as enhanced and executive function in patients with . For cancer, it targets the Warburg effect—where tumor cells preferentially rely on —by reducing circulating glucose and inducing , potentially enhancing efficacy through increased in tumors while lowering basal stress levels. A 2025 systematic review and confirmed that ketogenic diets may improve cancer patient outcomes, including survival and , though evidence remains preliminary and varies by cancer type. Other applications include , where the diet offers to neurons and improves motor symptoms like and stiffness, as evidenced by studies from the onward. For , it suppresses appetite via cholecystokinin release, promoting sustained energy restriction without compensatory hunger increases. In management, meta-analyses confirm it improves insulin sensitivity, glycemic control, and profiles, often outperforming other low-carbohydrate approaches. Emerging evidence as of 2025 also supports therapeutic ketogenesis in disorders, with a indicating modest improvements in depressive symptoms and anxiety through ketogenic diets, potentially via effects and enhanced . Additionally, ketone supplementation has shown benefits in , improving cardiac function particularly in patients with heart failure with reduced (HFrEF), according to a 2025 randomized trial. Modern variants encompass supplements, such as beta-hydroxybutyrate esters and salts, which induce rapid without dietary restriction and are well-tolerated in clinical settings for elevating blood levels. Intermittent fasting protocols, when combined with ketogenic principles, further support therapeutic ketogenesis by enhancing production and aiding in chronic disease management, including remission in select cases. Despite these benefits, therapeutic ketogenesis requires monitoring for risks, including deficiencies (e.g., vitamins and minerals) and potential kidney strain from high protein loads or , which can be tracked using ketone strips or beta-hydroxybutyrate meters to maintain safe levels.

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