Carnitine
Carnitine O-Palmitoyltransferase
Serine C-Palmitoyltransferase
Malonyl Coenzyme A
Palmitoyl Coenzyme A
Acyltransferases
Carnitine Acyltransferases
Carnitine O-Acetyltransferase
Acyl Coenzyme A
Mitochondria, Liver
Palmitoylcarnitine
Sphingolipids
Epoxy Compounds
Acetylcarnitine
Hereditary Sensory and Autonomic Neuropathies
Fatty Acids
Ketone Bodies
Liver
Palmitic Acid
Oxidation-Reduction
gamma-Butyrobetaine Dioxygenase
Rats, Inbred Strains
Organic Cation Transport Proteins
Submitochondrial Particles
Lipid Metabolism, Inborn Errors
Mitochondria, Muscle
Ceramides
Microbodies
Caprylates
Citrate (si)-Synthase
Sphingomonas
Digitonin
Sphingosine N-Acyltransferase
Intracellular Membranes
Isoenzymes
Lipid Metabolism
Escherichia coli O157
Sphingosine
Molecular Sequence Data
Betaine
Acetyl-CoA Carboxylase
Sphingomyelins
Oleic Acids
Mitochondria
Myocardium
Amino Acid Sequence
Muscle, Skeletal
Oleic Acid
Clofibrate
Gene Expression Regulation, Enzymologic
Acyl-CoA Oxidase
3-Hydroxyacyl CoA Dehydrogenases
Acyl-CoA Dehydrogenase, Long-Chain
Acyl-CoA Dehydrogenase
Rats, Wistar
RNA, Messenger
Pichia
Oxygen Consumption
PPAR alpha
Substrate Specificity
Bezafibrate
Esterification
Benzyl Alcohol
Detergents
O(6)-Methylguanine-DNA Methyltransferase
Ceramidases
Base Sequence
Fatty Acids, Nonesterified
Vitamin B Deficiency
Fumonisins
Diabetes Mellitus, Experimental
Energy Metabolism
Diabetic Ketoacidosis
Rats, Sprague-Dawley
Blotting, Western
Sequence Homology, Amino Acid
Cells, Cultured
Sphingomyelin Phosphodiesterase
Binding Sites
Catalysis
Mutation
Octoxynol
Oxidoreductases
DNA, Complementary
DNA Primers
3-Hydroxybutyric Acid
Microsomes
Enzyme Inhibitors
Saccharomyces cerevisiae
Mitochondrial Membranes
AMP-Activated Protein Kinases
Hydroxymethylglutaryl-CoA Synthase
Reye Syndrome
Glucose
Inhibitory Concentration 50
Insulin
Adipose Tissue, Brown
Glucagon
Cloning, Molecular
Lipids
Receptors, Cytoplasmic and Nuclear
Membrane Proteins
Fatty Acid Synthases
Gene Expression
Carrier Proteins
Transcription, Genetic
Hyperammonemia
Dietary Fats
Cell Fractionation
Protein Binding
Organ Specificity
Mutagenesis, Site-Directed
Cricetinae
Cell Membrane
Cattle
Mersalyl
Protein Structure, Tertiary
Mitochondrial Proteins
Fatty Liver
Gene Expression Regulation
Modification of left ventricular hypertrophy by chronic etomixir treatment. (1/672)
1. Etomoxir (2[6(4-chlorophenoxy)hexyl]oxirane-2-carboxylate), an irreversible carnitine palmitoyl-transferase 1 inhibitor, reduces the expression of the myocardial foetal gene programme and the functional deterioration during heart adaption to a pressure-overload. Etomoxir may, however, also improve the depressed myocardial function of hypertrophied ventricles after a prolonged pressure overload. 2. To test this hypothesis, we administered racemic etomoxir (15 mg kg(-1) day(-1) for 6 weeks) to rats with ascending aortic constriction beginning 6 weeks after imposing the pressure overload. 3. The right ventricular/body weight ratio increased (P<0.05) by 20% in etomoxir treated rats (n = 10) versus untreated rats with ascending aortic constriction (n = 10). Left ventricular weight was increased (P<0.05) by 8%. Etomoxir blunted the increase in left ventricular chamber volume. Etomoxir raised the proportion of V1 isomyosin (35+/-4% versus 24+/-2%; P<0.05) and decreased the percentage of V3 isomyosin (36+/-4% versus 48+/-3%; P<0.05). 4. Maximum isovolumically developed pressure was higher in etomoxir treated rats than in untreated pressure overloaded rats (371+/-22 versus 315+/-23 mmHg; P<0.05). Maximum rates of ventricular pressure development (14,800+/-1310 versus 12,340+/-1030mmHg s(-1); P<0.05) and decline (6440+/-750 versus 5040+/-710 mmHg s(-1); P<0.05) were increased as well. Transformation of pressure values to ventricular wall stress data revealed an improved myocardial function which could partially account for the enhanced function of the whole left ventricle. 5. The co-ordinated action of etomoxir on ventricular mass, geometry and myocardial phenotype enhanced thus the pressure generating capacity of hypertrophied pressure-overloaded left ventricles and delayed the deleterious dilative remodelling. (+info)Pharmacokinetic analysis of the cardioprotective effect of 3-(2,2, 2-trimethylhydrazinium) propionate in mice: inhibition of carnitine transport in kidney. (2/672)
The site of action of 3-(2,2,2-trimethylhydrazinium) propionate (THP), a new cardioprotective agent, was investigated in mice and rats. I.p. administration of THP decreased the concentrations of free carnitine and long-chain acylcarnitine in heart tissue. In isolated myocytes, THP inhibited free carnitine transport with a Ki of 1340 microM, which is considerably higher than the observed serum concentration of THP. The major cause of the decreased free carnitine concentration in heart was found to be the decreased serum concentration of free carnitine that resulted from the increased renal clearance of carnitine by THP. The estimated Ki of THP for inhibiting the reabsorption of free carnitine in kidneys was 52.2 microM, which is consistent with the serum THP concentration range. No inhibition of THP on the carnitine palmitoyltransferase activity in isolated mitochondrial fractions was observed. These results indicate that the principal site of action of THP as a cardioprotective agent is the carnitine transport carrier in the kidney, but not the carrier in the heart. (+info)A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA inhibition and high affinity binding. (3/672)
We have recently shown by deletion mutation analysis that the conserved first 18 N-terminal amino acid residues of rat liver carnitine palmitoyltransferase I (L-CPTI) are essential for malonyl-CoA inhibition and binding (Shi, J., Zhu, H., Arvidson, D. N. , Cregg, J. M., and Woldegiorgis, G. (1998) Biochemistry 37, 11033-11038). To identify specific residue(s) involved in malonyl-CoA binding and inhibition of L-CPTI, we constructed two more deletion mutants, Delta12 and Delta6, and three substitution mutations within the conserved first six amino acid residues. Mutant L-CPTI, lacking either the first six N-terminal amino acid residues or with a change of glutamic acid 3 to alanine, was expressed at steady-state levels similar to wild type and had near wild type catalytic activity. However, malonyl-CoA inhibition of these mutant enzymes was reduced 100-fold, and high affinity malonyl-CoA binding was lost. A mutant L-CPTI with a change of histidine 5 to alanine caused only partial loss of malonyl-CoA inhibition, whereas a mutant L-CPTI with a change of glutamine 6 to alanine had wild type properties. These results demonstrate that glutamic acid 3 and histidine 5 are necessary for malonyl-CoA binding and inhibition of L-CPTI by malonyl-CoA but are not required for catalysis. (+info)Comparisons of flux control exerted by mitochondrial outer-membrane carnitine palmitoyltransferase over ketogenesis in hepatocytes and mitochondria isolated from suckling or adult rats. (4/672)
The primary aim of this paper was to calculate and report flux control coefficients for mitochondrial outer-membrane carnitine palmitoyltransferase (CPT I) over hepatic ketogenesis because its role in controlling this pathway during the neonatal period is of academic importance and immediate clinical relevance. Using hepatocytes isolated from suckling rats as our model system, we measured CPT I activity and carbon flux from palmitate to ketone bodies and to CO2 in the absence and presence of a range of concentrations of etomoxir. (This is converted in situ to etomoxir-CoA which is a specific inhibitor of the enzyme.) From these data we calculated the individual flux control coefficients for CPT I over ketogenesis, CO2 production and total carbon flux (0.51 +/- 0.03; -1.30 +/- 0.26; 0.55 +/- 0.07, respectively) and compared them with equivalent coefficients calculated by similar analyses [Drynan, L., Quant, P.A. & Zammit, V.A. (1996) Biochem. J. 317, 791-795] in hepatocytes isolated from adult rats (0.85 +/- 0.20; 0.23 +/- 0.06; 1.06 +/- 0.29). CPT I exerts significantly less control over ketogenesis in hepatocytes isolated from suckling rats than those from adult rats. In the suckling systems the flux control coefficients for CPT I over ketogenesis specifically and over total carbon flux (< 0.6) are not consistent with the enzyme being rate-limiting. Broadly similar results were obtained and conclusions drawn by reanalysis of previous data {from experiments in mitochondria isolated from suckling or adult rats [Krauss, S., Lascelles, C.V., Zammit, V.A. & Quant, P.A. (1996) Biochem. J. 319, 427-433]} using a different approach of control analysis, although it is not strictly valid to compare flux control coefficients from different systems. Our overall conclusion is that flux control coefficients for CPT I over oxidative fluxes from palmitate (or palmitoyl-CoA) differ markedly according to (a) the metabolic state, (b) the stage of development, (c) the specific pathway studied and (d) the model system. (+info)Evidence that carnitine palmitoyltransferase I (CPT I) is expressed in microsomes and peroxisomes of rat liver. Distinct immunoreactivity of the N-terminal domain of the microsomal protein. (5/672)
Mitochondria, microsomes and peroxisomes all express overt (cytosol-facing) carnitine palmitoyltransferase activity that is inhibitable by malonyl-CoA. The overt carnitine palmitoyltransferase activity (CPTo) associated with the different fractions was measured. Mitochondria accounted for 65% of total cellular CPTo activity, with the microsomal and peroxisomal contributions accounting for the remaining 25% and 10%, respectively. In parallel experiments, rat livers were perfused in situ with medium containing dinitrophenyl (DNP)-etomoxir in order to inhibit quantitatively and label covalently (with DNP-etomoxiryl-CoA) the molecular species responsible for CPTo activity in each of the membrane systems under near-physiological conditions. In all three membrane fractions, a single protein with an identical molecular mass of approximately 88,000 kDa (p88) was labelled after DNP-etomoxir perfusion of the liver. The abundance of labelled p88 was quantitatively related to the respective specific activities of CPTo in each fraction. On Western blots the same protein was immunoreactive with three anti-peptide antibodies raised against linear epitopes of the cytosolic N- and C-domains and of the inter-membrane space loop (L) domain of the mitochondrial enzyme (L-CPT I). However, the reaction of the microsomal protein with the anti-N peptide antibody (raised against epitope Val-14-Lys-29 of CPT I) was an order of magnitude stronger than expected from either microsomal CPTo activity or its DNP-etomoxiryl-CoA labelling. This suggests that the N-terminal domain of the microsomal protein differs from that in the mitochondrial or peroxisomal protein. This conclusion was confirmed using antibody back-titration experiments, in which the binding of anti-N and anti-C antibodies by mitochondria and microsomes was quantified. (+info)Expression of the rat liver carnitine palmitoyltransferase I (CPT-Ialpha) gene is regulated by Sp1 and nuclear factor Y: chromosomal localization and promoter characterization. (6/672)
Carnitine palmitoyltransferase (CPT)-I catalyses the transfer of long-chain fatty acids from CoA to carnitine for translocation across the mitochondrial inner membrane. Expression of the 'liver' isoform of the CPT-I gene (CPT-Ialpha) is subject to developmental, hormonal and tissue-specific regulation. To understand the basis for control of CPT-Ialpha gene expression, we have characterized the proximal promoter of the CPT-Ialpha gene. Here, we report the sequence of 6839 base pairs of the promoter and the localization of the rat CPT-Ialpha gene to region q43 on chromosome 1. Our studies show that the first 200 base pairs of the promoter are sufficient to drive transcription of the CPT-Ialpha gene. Within this region are two sites that bind both Sp1 and Sp3 transcription factors. In addition, nuclear factor Y (NF-Y) binds the proximal promoter. Mutation at the Sp1 or NF-Y sites severely decreases transcription from the CPT-Ialpha promoter. Other protein binding sites were identified within the first 200 base pairs of the promoter by DNase I footprinting, and these elements contribute to CPT-Ialpha gene expression. Our studies demonstrate that CPT-Ialpha is a TATA-less gene which utilizes NF-Y and Sp proteins to drive basal expression. (+info)Peroxisome proliferator-activated receptor alpha mediates the adaptive response to fasting. (7/672)
Prolonged deprivation of food induces dramatic changes in mammalian metabolism, including the release of large amounts of fatty acids from the adipose tissue, followed by their oxidation in the liver. The nuclear receptor known as peroxisome proliferator-activated receptor alpha (PPARalpha) was found to play a role in regulating mitochondrial and peroxisomal fatty acid oxidation, suggesting that PPARalpha may be involved in the transcriptional response to fasting. To investigate this possibility, PPARalpha-null mice were subjected to a high fat diet or to fasting, and their responses were compared with those of wild-type mice. PPARalpha-null mice chronically fed a high fat diet showed a massive accumulation of lipid in their livers. A similar phenotype was noted in PPARalpha-null mice fasted for 24 hours, who also displayed severe hypoglycemia, hypoketonemia, hypothermia, and elevated plasma free fatty acid levels, indicating a dramatic inhibition of fatty acid uptake and oxidation. It is shown that to accommodate the increased requirement for hepatic fatty acid oxidation, PPARalpha mRNA is induced during fasting in wild-type mice. The data indicate that PPARalpha plays a pivotal role in the management of energy stores during fasting. By modulating gene expression, PPARalpha stimulates hepatic fatty acid oxidation to supply substrates that can be metabolized by other tissues. (+info)Elevated body fat in rats by the dietary nitric oxide synthase inhibitor, L-N omega nitroarginine. (8/672)
The influence of the dietary nitric oxide (NO) synthase inhibitor, L-N omega nitroarginine (L-NNA) on body fat was examined in rats. In experiment 1, all rats were fed with the same amount of diet with or without 0.02% L-NNA for 8 wk. L-NNA intake caused elevations in serum triglyceride and body fat, and reduction in serum nitrate (a metabolite of nitric oxide). The activity of hepatic carnitine palmitoyltransferase was reduced by L-NNA. In experiment 2, rats were fed for 8 wk with the same amount of diets with or without 0.02% L-NNA supplemented or not with 4% L-arginine. The elevation in body fat, and the reductions in serum nitrate and in the activity of hepatic carnitine palmitoyltransferase by L-NNA were all suppressed by supplemental L-arginine. The results suggest that lower NO generation elevated not only serum triglyceride, but also body fat by reduced fatty acid oxidation. (+info)There are several types of HSANs, each with distinct clinical features and modes of inheritance. Some of the most common forms of HSANs include:
1. Hereditary sensory and autonomic neuropathy type I (HSANI): This is the most common form of HSAN, also known as Familial Dysautonomia (Riley-Day syndrome). It is caused by a mutation in the IVS gene and affects primarily the sensory and autonomic nerves.
2. Hereditary sensory and autonomic neuropathy type II (HSANII): This form of HSAN is caused by mutations in the PMP22 gene and is characterized by progressive weakness and loss of sensation in the limbs, as well as abnormalities in the functioning of the autonomic nervous system.
3. Hereditary sensory and autonomic neuropathy type III (HSANIII): This form of HSAN is caused by mutations in the GRM1 gene and is characterized by progressive loss of sensation and muscle weakness, as well as abnormalities in the functioning of the autonomic nervous system.
4. Hereditary sensory and autonomic neuropathy type IV (HSANIV): This form of HSAN is caused by mutations in the MAG gene and is characterized by progressive loss of sensation and muscle weakness, as well as abnormalities in the functioning of the autonomic nervous system.
The symptoms of HSANs vary depending on the specific type of disorder and can include:
* Progressive loss of sensation in the hands and feet
* Muscle weakness and wasting
* Abnormalities in the functioning of the autonomic nervous system, such as dysfunction of the cardiovascular and gastrointestinal systems
* Abnormalities in the functioning of the sensory nerves, leading to numbness, tingling, or pain
* Abnormalities in the functioning of the motor nerves, leading to weakness and muscle wasting
* Eye problems, such as optic atrophy or difficulty moving the eyes
* Hearing loss or other ear abnormalities
* Cognitive impairment or developmental delays
There is currently no cure for HSANs, but various treatments can help manage the symptoms. These may include:
* Physical therapy to maintain muscle strength and mobility
* Occupational therapy to improve daily functioning and independence
* Pain management medications and other treatments for neuropathic pain
* Assistive devices, such as canes or wheelchairs, to aid with mobility
* Speech therapy to improve communication skills
* Cognitive and behavioral therapies to help manage cognitive impairment and developmental delays
The progression of HSANs can vary depending on the specific type of disorder and the individual affected. Some forms of HSANs may progress slowly over many years, while others may progress more quickly and have a more severe impact on daily functioning. In some cases, HSANs can be associated with other conditions or diseases that can affect the progression of the disorder. For example, some individuals with HSANs may also have other neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) or Alzheimer's disease.
HSANs are rare disorders, and there is currently no cure. However, research into the genetic causes of these disorders is ongoing, and new treatments and therapies are being developed to help manage the symptoms and slow the progression of the disorders. With proper management and support, individuals with HSANs can lead fulfilling lives and achieve their goals.
Starvation is a condition where an individual's body does not receive enough nutrients to maintain proper bodily functions and growth. It can be caused by a lack of access to food, poverty, poor nutrition, or other factors that prevent the intake of sufficient calories and essential nutrients. Starvation can lead to severe health consequences, including weight loss, weakness, fatigue, and even death.
Types of Starvation:
There are several types of starvation, each with different causes and effects. These include:
1. Acute starvation: This occurs when an individual suddenly stops eating or has a limited access to food for a short period of time.
2. Chronic starvation: This occurs when an individual consistently does not consume enough calories and nutrients over a longer period of time, leading to gradual weight loss and other health problems.
3. Malnutrition starvation: This occurs when an individual's diet is deficient in essential nutrients, leading to malnutrition and other health problems.
4. Marasmus: This is a severe form of starvation that occurs in children, characterized by extreme weight loss, weakness, and wasting of muscles and organs.
5. Kwashiorkor: This is a form of malnutrition caused by a diet lacking in protein, leading to edema, diarrhea, and other health problems.
Effects of Starvation on the Body:
Starvation can have severe effects on the body, including:
1. Weight loss: Starvation causes weight loss, which can lead to a decrease in muscle mass and a loss of essential nutrients.
2. Fatigue: Starvation can cause fatigue, weakness, and a lack of energy, making it difficult to perform daily activities.
3. Weakened immune system: Starvation can weaken the immune system, making an individual more susceptible to illnesses and infections.
4. Nutrient deficiencies: Starvation can lead to a deficiency of essential nutrients, including vitamins and minerals, which can cause a range of health problems.
5. Increased risk of disease: Starvation can increase the risk of diseases such as tuberculosis, pellagra, and other infections.
6. Mental health issues: Starvation can lead to mental health issues such as depression, anxiety, and irritability.
7. Reproductive problems: Starvation can cause reproductive problems, including infertility and miscarriage.
8. Hair loss: Starvation can cause hair loss, which can be a sign of malnutrition.
9. Skin problems: Starvation can cause skin problems, such as dryness, irritation, and infections.
10. Increased risk of death: Starvation can lead to increased risk of death, especially in children and the elderly.
It is important to note that these effects can be reversed with proper nutrition and care. If you or someone you know is experiencing starvation, it is essential to seek medical attention immediately.
Here are some possible causes of myoglobinuria:
1. Muscle injury or trauma: This can cause myoglobin to leak into the bloodstream and then into the urine.
2. Muscle disease: Certain muscle diseases, such as muscular dystrophy, can cause myoglobinuria.
3. Kidney damage: Myoglobin can accumulate in the kidneys and cause damage if the kidneys are not functioning properly.
4. Sepsis: Sepsis is a systemic infection that can cause muscle breakdown and myoglobinuria.
5. Burns: Severe burns can cause muscle damage and lead to myoglobinuria.
6. Heart attack: A heart attack can cause muscle damage and myoglobinuria.
7. Rhabdomyolysis: This is a condition where the muscles break down and release myoglobin into the bloodstream. It can be caused by various factors such as medication, infection, or injury.
Symptoms of myoglobinuria may include dark urine, proteinuria (excess protein in the urine), and kidney damage. Treatment depends on the underlying cause and may involve supportive care, medication, or dialysis to remove waste products from the blood.
There are several types of inborn errors of lipid metabolism, each with its own unique set of symptoms and characteristics. Some of the most common include:
* Familial hypercholesterolemia: A condition that causes high levels of low-density lipoprotein (LDL) cholesterol in the blood, which can lead to heart disease and other health problems.
* Fabry disease: A rare genetic disorder that affects the body's ability to break down certain fats, leading to a buildup of toxic substances in the body.
* Gaucher disease: Another rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.
* Lipoid cerebral degeneration: A condition that causes fatty deposits to accumulate in the brain, leading to cognitive decline and other neurological problems.
* Tangier disease: A rare genetic disorder that affects the body's ability to break down certain lipids, leading to a buildup of toxic substances in the body.
Inborn errors of lipid metabolism can be diagnosed through a variety of tests, including blood tests and genetic analysis. Treatment options vary depending on the specific disorder and its severity, but may include dietary changes, medication, and other therapies. With proper treatment and management, many individuals with inborn errors of lipid metabolism can lead active and fulfilling lives.
1. Vitamin B1 (Thiamine): necessary for converting carbohydrates into energy
2. Vitamin B2 (Riboflavin): important for vision health and immune system function
3. Vitamin B3 (Niacin): crucial for energy production and skin health
4. Vitamin B5 (Pantothenic acid): involved in energy production, hormone production, and blood cell formation
5. Vitamin B6: essential for brain function, immune system function, and the synthesis of neurotransmitters
6. Vitamin B7 (Biotin): important for hair, skin, and nail health, as well as energy production
7. Vitamin B9 (Folic acid): crucial for fetal development during pregnancy
8. Vitamin B12: necessary for the production of red blood cells, nerve function, and DNA synthesis.
Vitamin B deficiencies can occur due to several factors, including:
* Poor diet or malnutrition
* Gastrointestinal disorders that impair nutrient absorption (e.g., celiac disease, Crohn's disease)
* Increased demand for vitamins during pregnancy and lactation
* Certain medications (e.g., antacids, proton pump inhibitors) that interfere with nutrient absorption
* Malabsorption due to pancreas or small intestine disorders
* Inherited disorders (e.g., vitamin B12 deficiency due to pernicious anemia)
Symptoms of vitamin B deficiencies can vary depending on the specific vitamin and the severity of the deficiency. Some common symptoms include fatigue, weakness, irritability, depression, skin problems, and impaired cognitive function. Treatment typically involves dietary modifications and supplementation with the appropriate vitamin. In severe cases, hospitalization may be necessary to address any underlying conditions or complications.
The following are some of the most common vitamin B deficiencies:
1. Vitamin B12 deficiency: This is one of the most common vitamin B deficiencies and can cause fatigue, weakness, pale skin, and neurological problems such as numbness or tingling in the hands and feet.
2. Vitamin B6 deficiency: This can cause skin problems, such as acne-like rashes, and neurological symptoms like confusion, convulsions, and weakness in the arms and legs.
3. Folate deficiency: This can cause fatigue, weakness, pale skin, and neurological problems such as memory loss and confusion.
4. Vitamin B2 (riboflavin) deficiency: This can cause cracked lips, skin around the mouth, and tongue, and eyes.
5. Niacin (vitamin B3) deficiency: This can cause pellagra, a condition characterized by diarrhea, dermatitis, and dementia.
6. Vitamin B5 (pantothenic acid) deficiency: This can cause fatigue, weakness, and neurological symptoms like headaches and dizziness.
7. Vitamin B1 (thiamine) deficiency: This can cause beriberi, a condition characterized by weakness, fatigue, and neurological problems such as confusion and memory loss.
8. Biotin deficiency: This is rare but can cause skin problems, such as seborrhea, and neurological symptoms like numbness and tingling in the hands and feet.
9. Vitamin B12 (cobalamin) deficiency: This is common in vegetarians and vegans who do not consume enough animal products, and can cause fatigue, weakness, and neurological problems such as numbness and tingling in the hands and feet.
It's important to note that these deficiencies can have a significant impact on your overall health and well-being, so it's essential to be aware of the signs and symptoms and take steps to ensure you are getting enough of these vitamins in your diet.
Types of Experimental Diabetes Mellitus include:
1. Streptozotocin-induced diabetes: This type of EDM is caused by administration of streptozotocin, a chemical that damages the insulin-producing beta cells in the pancreas, leading to high blood sugar levels.
2. Alloxan-induced diabetes: This type of EDM is caused by administration of alloxan, a chemical that also damages the insulin-producing beta cells in the pancreas.
3. Pancreatectomy-induced diabetes: In this type of EDM, the pancreas is surgically removed or damaged, leading to loss of insulin production and high blood sugar levels.
Experimental Diabetes Mellitus has several applications in research, including:
1. Testing new drugs and therapies for diabetes treatment: EDM allows researchers to evaluate the effectiveness of new treatments on blood sugar control and other physiological processes.
2. Studying the pathophysiology of diabetes: By inducing EDM in animals, researchers can study the progression of diabetes and its effects on various organs and tissues.
3. Investigating the role of genetics in diabetes: Researchers can use EDM to study the effects of genetic mutations on diabetes development and progression.
4. Evaluating the efficacy of new diagnostic techniques: EDM allows researchers to test new methods for diagnosing diabetes and monitoring blood sugar levels.
5. Investigating the complications of diabetes: By inducing EDM in animals, researchers can study the development of complications such as retinopathy, nephropathy, and cardiovascular disease.
In conclusion, Experimental Diabetes Mellitus is a valuable tool for researchers studying diabetes and its complications. The technique allows for precise control over blood sugar levels and has numerous applications in testing new treatments, studying the pathophysiology of diabetes, investigating the role of genetics, evaluating new diagnostic techniques, and investigating complications.
Rhabdomyolysis can be caused by a variety of factors, including:
1. Physical trauma or injury to the muscles
2. Overuse or strain of muscles
3. Poor physical conditioning or training
4. Infections such as viral or bacterial infections that affect the muscles
5. Certain medications or drugs, such as statins and antibiotics
6. Alcohol or drug poisoning
7. Heat stroke or other forms of extreme heat exposure
8. Hypothyroidism (underactive thyroid)
9. Genetic disorders that affect muscle function.
Symptoms of rhabdomyolysis can include:
1. Muscle weakness or paralysis
2. Muscle pain or cramping
3. Confusion or disorientation
4. Dark urine or decreased urine output
5. Fever, nausea, and vomiting
6. Shortness of breath or difficulty breathing
7. Abnormal heart rhythms or cardiac arrest.
If you suspect that someone has rhabdomyolysis, it is important to seek medical attention immediately. Treatment typically involves supportive care, such as fluids and electrolyte replacement, as well as addressing any underlying causes of the condition. In severe cases, hospitalization may be necessary to monitor and treat complications such as kidney failure or cardiac problems.
Symptoms of DKA can include:
* High blood sugar levels (usually above 300 mg/dL)
* High levels of ketones in the blood and urine
* Nausea, vomiting, and abdominal pain
* Fatigue, weakness, and confusion
* Headache and dry mouth
* Flu-like symptoms, such as fever, chills, and muscle aches
If left untreated, DKA can lead to serious complications, such as:
* Dehydration and electrolyte imbalances
* Seizures and coma
* Kidney damage and failure
Treatment of DKA typically involves hospitalization and intravenous fluids to correct dehydration and electrolyte imbalances. Insulin therapy is also started to lower blood sugar levels and promote the breakdown of ketones. In severe cases, medications such as sodium bicarbonate may be given to help neutralize the excess ketones in the blood.
Preventing DKA involves proper management of diabetes, including:
* Taking insulin as prescribed and monitoring blood sugar levels regularly
* Maintaining a healthy diet and exercise program
* Monitoring for signs of infection or illness, which can increase the risk of DKA
Early detection and treatment of DKA are critical to preventing serious complications and improving outcomes for people with diabetes.
Symptoms of Reye Syndrome can include:
* Headache
* Confusion
* Vomiting
* Seizures
* Loss of consciousness
* Yellowing of the skin and eyes (jaundice)
* Fatigue
* Abdominal pain
If you suspect that your child may have Reye Syndrome, it is important to seek medical attention immediately. The condition can be difficult to diagnose, as it can resemble other conditions such as meningitis or encephalitis. A healthcare provider will typically perform a physical examination, take a medical history, and order laboratory tests to confirm the diagnosis.
There is no specific treatment for Reye Syndrome, but the condition is usually managed with supportive care in a hospital setting. Treatment may include:
* Medication to control seizures
* Intravenous fluids and nutrition
* Monitoring of vital signs and liver function
* Antiviral medication in some cases
Reye Syndrome can be fatal if left untreated, so early diagnosis and aggressive management are crucial. The condition is rare, but it is important for parents and healthcare providers to be aware of the signs and symptoms in order to provide prompt and appropriate care.
Causes of Hyperammonemia:
1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.
Symptoms of Hyperammonemia:
1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting
Diagnosis of Hyperammonemia:
1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.
Treatment of Hyperammonemia:
1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.
Complications of Hyperammonemia:
1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.
In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.
There are two main types of fatty liver disease:
1. Alcoholic fatty liver disease (AFLD): This type of fatty liver disease is caused by excessive alcohol consumption and is the most common cause of fatty liver disease in the United States.
2. Non-alcoholic fatty liver disease (NAFLD): This type of fatty liver disease is not caused by alcohol consumption and is the most common cause of fatty liver disease worldwide. It is often associated with obesity, diabetes, and high cholesterol.
There are several risk factors for developing fatty liver disease, including:
* Obesity
* Physical inactivity
* High calorie intake
* Alcohol consumption
* Diabetes
* High cholesterol
* High triglycerides
* History of liver disease
Symptoms of fatty liver disease can include:
* Fatigue
* Abdominal discomfort
* Loss of appetite
* Nausea and vomiting
* Abnormal liver function tests
Diagnosis of fatty liver disease is typically made through a combination of physical examination, medical history, and diagnostic tests such as:
* Liver biopsy
* Imaging studies (ultrasound, CT or MRI scans)
* Blood tests (lipid profile, glucose, insulin, and liver function tests)
Treatment of fatty liver disease depends on the underlying cause and severity of the condition. Lifestyle modifications such as weight loss, exercise, and a healthy diet can help improve the condition. In severe cases, medications such as antioxidants, fibric acids, and anti-inflammatory drugs may be prescribed. In some cases, surgery or other procedures may be necessary.
Prevention of fatty liver disease includes:
* Maintaining a healthy weight
* Eating a balanced diet low in sugar and saturated fats
* Engaging in regular physical activity
* Limiting alcohol consumption
* Managing underlying medical conditions such as diabetes and high cholesterol.
Carnitine palmitoyltransferase II
Carnitine O-palmitoyltransferase
Carnitine palmitoyltransferase I
Carnitine palmitoyltransferase I deficiency
Carnitine palmitoyltransferase II deficiency
Transferase
Carnitine O-acetyltransferase
Carnitine O-octanoyltransferase
CZIB
Combined malonic and methylmalonic aciduria
Perhexiline
Myokymia
CPT2
Hormone-sensitive lipase
Glibenclamide
PPRC1
CHKB (gene)
USF2
Fasciculation
Randle cycle
Palmitoylcarnitine
Carnitine-acylcarnitine translocase deficiency
Protein kinase, AMP-activated, alpha 1
Ketogenesis
AMP-activated protein kinase
Fatty acid oxidation inhibitors
Triheptanoin
Etomoxir
Tumor metabolome
Diagnosis (American TV series)
List of diseases (C)
Palmitoyl-CoA hydrolase
Meldonium
Coenzyme A
Palmitoyl-CoA
ACACB
Beta oxidation
Myalgia
Acyl-CoA
Myoglobinuria
Inner mitochondrial membrane
Pirinixic acid
Fatty-acid metabolism disorder
List of neuromuscular disorders
Carnitine palmitoyltransferase II deficiency: MedlinePlus Genetics
BlueGene: Bovine Carnitine Palmitoyltransferase I ELISA Kit, CPT-1 ELISA
Mouse CPT1A(Carnitine Palmitoyltransferase 1A, Liver) ELISA Kit - World Care Council
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Journal of Pediatric Endocrinology and Metabolism Volume 30 Issue 2
Carnitine Deficiency: Background, Pathophysiology, Epidemiology
MMRRC:044201-MU
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Carnitine Deficiency Follow-up: Further Outpatient Care, Further Inpatient Care, Inpatient & Outpatient Medications
Chromosome 11 (human) - wikidoc
11beta-Hydroxysteroid dehydrogenase type 1 inhibitors: novel agents for the treatment of metabolic syndrome and obesity-related...
Carnosine alleviates diabetic nephropathy by targeting GNMT, a key enzyme mediating renal inflammation and fibrosis | Clinical...
Valproic acid: Indication, Dosage, Side Effect, Precaution | MIMS Indonesia
Changes in Exercise-Induced Gene Expression in 5′-AMP-Activated Protein Kinase γ3-Null and γ3 R225Q Transgenic Mice | Diabetes ...
CONICET | Buscador de Institutos y Recursos Humanos
Appendix F Unrelated Operating Room Procedures (MS-DRGs 981-989
A Phase 1b Study of the Safety of REN001 in Patients With Fatty Acid Oxidation Disorders - Full Text View - ClinicalTrials.gov
IJMS | Free Full-Text | An Isolated Complex V Inefficiency and Dysregulated Mitochondrial Function in Immortalized Lymphocytes...
Comprehensive Metabolic Profiling Reveals a Lipid-Rich Fingerprint of Free Thyroxine Far Beyond Classic Parameters, Journal of...
DeCS
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Pesquisa | Biblioteca Virtual em Saúde - BRASIL
Expression of genes involved in lipid metabolism correlate with peroxisome proliferator-activated receptor gamma expression in...
FDA Approvals, Highlights, and Summaries: Pediatrics
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Find Research outputs - Manipal Academy of Higher Education, Manipal, India
CDC/NIH Web Information Database|Home|PHGKB
Deficiency23
- Carnitine palmitoyltransferase II (CPT II) deficiency is a condition that prevents the body from using certain fats for energy, particularly during periods without food (fasting). (medlineplus.gov)
- Carefully review diet compliance in secondary carnitine deficiency, considering avoidance of fasting, intake of fat-restricted, high-carbohydrate diet, and other dietary supplements that may be needed, such as riboflavin or glycine. (medscape.com)
- Admit patients with carnitine deficiency for medical management of acute metabolic decompensation. (medscape.com)
- Provide intravenous (IV) carnitine if the patient is known to have carnitine deficiency and a defect affecting the oxidation of long chain fatty acids has been excluded. (medscape.com)
- Medications include carnitine for primary and secondary carnitine deficiency, as well as other cofactors that may be needed for different conditions associated with secondary carnitine deficiency (eg, riboflavin, coenzyme Q, biotin, hydroxocobalamin, betaine, glycine). (medscape.com)
- Avoid exercise and dehydration with warm temperatures because attacks of rhabdomyolysis may occur with certain conditions that cause secondary carnitine deficiency. (medscape.com)
- Patients with primary carnitine deficiency have excellent prognosis with oral carnitine supplementation. (medscape.com)
- Prognosis of secondary carnitine deficiency depends on the nature of the disorder. (medscape.com)
- Translocase deficiency and the infantile form of carnitine palmitoyltransferase II (CPT-II) deficiency have very poor prognosis regardless of treatment. (medscape.com)
- Other metabolic disorders that cause secondary carnitine deficiency, such as organic acidemias, require lifelong diet modification and nutritional supplements. (medscape.com)
- Family members should receive education once the work-up initiated after newborn screening results suggests primary carnitine deficiency in the newborn or in the mother. (medscape.com)
- Carnitine deficiency is a metabolic state in which carnitine concentrations in plasma and tissues are less than the levels required for normal function of the organism. (medscape.com)
- Carnitine deficiency may be primary or secondary. (medscape.com)
- Primary carnitine deficiency is caused by a deficiency in the plasma membrane carnitine transporter, with urinary carnitine wasting causing systemic carnitine depletion. (medscape.com)
- [ 1 ] Intracellular carnitine deficiency impairs the entry of long-chain fatty acids into the mitochondrial matrix. (medscape.com)
- Muscle carnitine deficiency (restricted to muscle) is characterized by depletion of carnitine levels in muscle with normal serum concentrations. (medscape.com)
- In secondary carnitine deficiency, which is caused by other metabolic disorders (eg, fatty acid oxidation disorders, organic acidemias), carnitine depletion may be secondary to the formation of acylcarnitine adducts and the inhibition of carnitine transport in renal cells by acylcarnitines. (medscape.com)
- Preterm newborns also may be at risk for developing carnitine deficiency because immature renal tubular function combined with impaired carnitine biosynthesis renders them strictly dependent on exogenous supplies to maintain normal plasma carnitine levels. (medscape.com)
- Valproic acid may cause an acquired type of secondary carnitine deficiency by directly impairing renal tubular reabsorption of carnitine. (medscape.com)
- In a Japanese study, primary systemic carnitine deficiency was estimated to occur in 1 per 40,000 births. (medscape.com)
- In order to abate the mortality and morbidity of undiagnosed primary carnitine deficiency, this condition has been included in the expanded newborn screening program in several states within the United States. (medscape.com)
- This is a Phase 1b, open-label, multiple-dose study of the safety and tolerability of 2 dose levels of REN001 in subjects with fatty acid oxidation disorders (FAODs) with confirmed mutations in the Carnitine palmitoyltransferase II deficiency (CPT2), Very long-chain Acyl-CoA dehydrogenase deficiency (VLCAD), Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHAD) or Trifunctional Protein Deficiency (TFP). (clinicaltrials.gov)
- If the body is deficient in the enzymes that do this, (fatty acid oxidation disorders), either as a "primary " deficiency associated with genetic abnormalities or "secondary" carnitine deficiency, it can lead to increased amounts of acylcarnitine in the blood which may present with brain dysfunction, a weakened heart, confusion, weakness and other signs and symptoms. (healthmatters.io)
Transferase4
- Expression of lipoprotein lipase 1, carnitine palmitoyl transferase 1b, and 3-hydroxyacyl-CoA dehydrogenase was increased in Tg-Prkag3 225Q mice, with opposing effects in Prkag3 −/− mice after exercise. (diabetesjournals.org)
- To examine the potential regulation of genes by PPAR-gamma in human skeletal muscle, we used semiquantitative RT-PCR to determine the expression of PPAR-gamma, lipoprotein lipase (LPL), muscle carnitine palmitoyl transferase-1 (mCPT1), fatty acid-binding protein (FABP), carnitine acylcarnitine transferase (CACT), and glucose transporter-4 (GLUT4) in freeze-dried muscle samples from 14 male subjects. (garvan.org.au)
- Inclusion of 45 mg/kg of dietary Cu in diets for rabbits improved body mass gain by upregulating mRNA transcription of fatty acid transport protein, fatty acid binding protein, and carnitine palmitoyl transferase 1, indicating that dietary Cu may influence post-absorptive metabolism of lipids. (illinois.edu)
- 0.10) abundance of fatty acid binding protein 1, peroxisome proliferator-activated receptor alpha, and carnitine palmitoyl transferase 1 B in liver, skeletal muscle, and subcutaneous adipose tissue, respectively. (illinois.edu)
CPT1A3
- Description: A sandwich quantitative ELISA assay kit for detection of Human Carnitine Palmitoyltransferase 1A, Liver (CPT1A) in samples from tissue homogenates, cell lysates or other biological fluids. (worldcarecouncil.org)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Carnitine Palmitoyltransferase 1A, Liver (CPT1A) in Tissue homogenates, cell lysates and other biological fluids. (worldcarecouncil.org)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Carnitine Palmitoyltransferase 1A, Liver (CPT1A) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (worldcarecouncil.org)
Plasma carnitine levels1
- Carefully monitor adequate carnitine dose in primary and secondary carnitine deficiencies by evaluating plasma carnitine levels during follow-up visits. (medscape.com)
ELISA Kit1
- Bovine Carnitine palmitoyltransferase I ELISA kit is suitable for the detection of samples from Bovine species. (elisakit.cc)
CPT21
- Mutations in the CPT2 gene reduce the activity of carnitine palmitoyltransferase 2. (medlineplus.gov)
Mutations1
- SLC22A5 mutations can affect carnitine transport by impairing maturation of transporters to the plasma membrane. (medscape.com)
Mitochondria2
- A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. (medlineplus.gov)
- Once these fatty acids are inside mitochondria, carnitine palmitoyltransferase 2 removes the carnitine and prepares them for fatty acid oxidation. (medlineplus.gov)
Fatty acids2
- Without enough of this enzyme, carnitine is not removed from long-chain fatty acids. (medlineplus.gov)
- Fatty acids and long-chain acylcarnitines (fatty acids still attached to carnitine) may also build up in cells and damage the liver, heart, and muscles. (medlineplus.gov)
Beta-oxidation1
- The activity and mRNA levels of carnitine palmitoyltransferase I (CPT I) and the rate of beta-oxidation were increased in oxidative muscles of SCD1-/- mice. (nih.gov)
Liver2
- Carnitine is a naturally occurring hydrophilic amino acid derivative, produced endogenously in the kidneys and liver and derived from meat and dairy products in the diet. (medscape.com)
- Carnitine is a generic name given to a number of compounds formed primarily from the building blocks of proteins (amino acids) by the kidneys and liver which play an important role in converting fats into energy for cell function (metabolism). (healthmatters.io)
Enzyme2
- This gene provides instructions for making an enzyme called carnitine palmitoyltransferase 2. (medlineplus.gov)
- The mRNA levels and activity of serine palmitoyltransferase (SPT), a key enzyme in ceramide synthesis, as well as the incorporation of [14C]palmitate into ceramide were decreased by approximately 50% in red muscles of SCD1-/- mice. (nih.gov)
Dehydrogenase1
- For this rare disease, a small double blinded, randomized controlled trial of 32 subjects with LC-FAODs (carnitine palmitoyltransferase-2, very long-chain acylCoA dehydrogenase, trifunctional protein, or long-chain 3-hydroxy acylCoA dehydrogenase deficiencies) were randomly assigned a diet containing 20% of their total daily energy from either triheptanoin or trioctanoin. (medscape.com)
Defect1
- Evidence indicates that the causal factor is a defect in the muscle carnitine transporter. (medscape.com)
Levels1
- Biologic effects of low carnitine levels may not be clinically significant until they reach less than 10-20% of normal. (medscape.com)
Free1
- Carnitine binds acyl residues and helps in their elimination, decreasing the number of acyl residues conjugated with coenzyme A (CoA) and increasing the ratio between free and acylated CoA. (medscape.com)
Palmitoyl transferase1
- Improvement of myocardial function and metabolism in diabetic rats by the carnitine palmitoyl transferase inhibitor Etomoxir. (nih.gov)
Total carnitine4
- Individuals with hepatic encephalopathy typically present with hypoglycemia, absent or low levels of ketones, and elevated serum concentrations of liver transaminases, ammonia, and total carnitine. (nih.gov)
- The University of California San Francisco Laboratory reports the normal values of free and total carnitine in adults as 18-69 μmol/L and 20-71 μmol/L, respectively. (medscape.com)
- Chace et al (2003) examined free and total carnitine levels in newborns. (medscape.com)
- Free and total carnitine levels within the reference range typically indicate adequate intake, stores, and metabolism. (medscape.com)
Fatty10
- A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. (medlineplus.gov)
- Once these fatty acids are inside mitochondria, carnitine palmitoyltransferase 2 removes the carnitine and prepares them for fatty acid oxidation. (medlineplus.gov)
- Without enough of this enzyme, carnitine is not removed from long-chain fatty acids. (medlineplus.gov)
- Fatty acids and long-chain acylcarnitines (fatty acids still attached to carnitine) may also build up in cells and damage the liver, heart, and muscles. (medlineplus.gov)
- Carnitine palmitoyltransferase (CPT) deficiencies are common disorders of mitochondrial fatty acid oxidation. (nih.gov)
- adults need a high-carbohydrate, low-fat diet to provide a constant supply of carbohydrate energy and medium-chain triglycerides to provide approximately one third of total calories (C6-C10 fatty acids do not require the carnitine shuttle for entry into the mitochondrion). (nih.gov)
- Because of these key functions, carnitine is concentrated in tissues that utilize fatty acids as their primary dietary fuel, such as skeletal and cardiac (heart) muscle. (nih.gov)
- Carnitine is studied extensively in part because of the important role it plays in fatty acid oxidation and energy production, and because it is a well-tolerated and generally safe therapeutic agent. (nih.gov)
- Understanding the molecular basis for the disease caused by mutations of the carnitine palmitoyltransferase (CPT)I and CPTII enzymes involved in the transport of fatty acids by L-carnitine into and out of the mitochondria. (nih.gov)
- Carnitine is an important, small water-soluble molecule that binds to long-chain fatty acids and facilitates their transport across the inner mitochondrial membrane and into the mitochondrial matrix to undergo fatty acid oxidation (metabolism). (medscape.com)
Deficiencies2
- Other benefits attributed to carnitine result from the management of secondary carnitine deficiencies. (nih.gov)
- While there is agreement on carnitine's role as a prescription product for the treatment of primary carnitine deficiencies, its benefits as a dietary supplement in individuals who are carnitine sufficient is debated. (nih.gov)
Liver3
- People with this disorder typically also have an enlarged liver (hepatomegaly), muscle weakness, nervous system damage, and elevated levels of carnitine in the blood. (nih.gov)
- gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver. (nih.gov)
- In general, healthy adults do not require dietary carnitine as carnitine stores are replenished through endogenous synthesis from lysine and methionine in the liver and kidneys. (nih.gov)
Disorder1
- The disorder is fatal without treatment, but supplementation with oral carnitine results in elevated carnitine levels and prevents progression of the disease. (medscape.com)
CACT1
- gene provides instructions for making a protein called carnitine -acylcarnitine translocase (CACT). (nih.gov)
Transporter1
- It is proven treatment in children who have recessive defects in the carnitine transporter system and in individuals treated with pivalate containing antibiotics. (nih.gov)
Substance known2
Ammonia1
- Carnitine is a quaternary, water-soluble ammonia compound biosynthesized from lysine and arginine. (medscape.com)
Metabolism2
- disorders of metabolism with elevated butyryl- and isobutyryl- carnitine detected by tandem mass spectrometry newborn screening. (nih.gov)
- The first day addressed the fundamentals of carnitine physiology and pharmacology, issues related to its replacement in health and disease, its effects on skeletal and cardiac or smooth muscle, and its role in fat metabolism and obesity. (nih.gov)
Synthesis1
- Carnitine is derived from both the diet (meats and milk) and synthesis (very slowly) from trimethyllysine. (medscape.com)
Treatment1
- Carnitine research needs emerging from this conference can be grouped under three broad headings, i.e. basic research, as a drug in the treatment and management of disease conditions, and as a dietary supplement. (nih.gov)
Term1
- Carnitine is the generic term for a number of compounds that include L-carnitine, L-acetylcarnitine, acetyl-L-carnitine, and L-propionyl carnitine. (nih.gov)
Essential1
- Carnitine is termed a conditionally essential nutrient, as under certain conditions its requirements may exceed the individual's capacity to synthesize it. (nih.gov)
Diet1
- Carnitine, a natural substance acquired mostly through the diet, is required by cells to process fats and produce energy. (nih.gov)