SKP Cullin F-Box Protein Ligases
Acetyl Coenzyme A
RING Finger Domains
RNA Ligase (ATP)
Hydroxymethylglutaryl CoA Reductases
Molecular Sequence Data
Amino Acid Sequence
Endosomal Sorting Complexes Required for Transport
Proteasome Endopeptidase Complex
Protein Structure, Tertiary
Ubiquitin-Protein Ligase Complexes
Sequence Homology, Amino Acid
Proto-Oncogene Proteins c-cbl
Hydroxymethylglutaryl-CoA Reductase Inhibitors
S-Phase Kinase-Associated Proteins
Protein Inhibitors of Activated STAT
Small Ubiquitin-Related Modifier Proteins
Palmitoyl Coenzyme A
Malonyl Coenzyme A
Saccharomyces cerevisiae Proteins
Amino Acid Motifs
Cell Cycle Proteins
Vitamin B 12
Receptors, Autocrine Motility Factor
Protein Processing, Post-Translational
Two-Hybrid System Techniques
Recombinant Fusion Proteins
Gene Expression Regulation, Enzymologic
Genetic Complementation Test
Proto-Oncogene Proteins c-mdm2
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum-Associated Degradation
Protein Interaction Domains and Motifs
Gene Expression Regulation, Plant
Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome
Magnetic Resonance Spectroscopy
Intracellular Signaling Peptides and Proteins
NADH, NADPH Oxidoreductases
Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells. (1/783)Epidermal growth factor (EGF) has been reported to stimulate carbohydrate, amino acid, and electrolyte transport in the small intestine, but its effects on lipid transport are poorly documented. This study aimed to investigate EGF effects on fatty acid uptake and esterification in a human enterocyte cell line (Caco-2). EGF inhibited cell uptake of [14C]palmitate and markedly reduced its incorporation into triglycerides. In contrast, the incorporation in phospholipids was enhanced. To elucidate the mechanisms involved, key steps of lipid synthesis were investigated. The amount of intestinal fatty acid-binding protein (I-FABP), which is thought to be important for fatty acid absorption, and the activity of diacylglycerol acyltransferase (DGAT), an enzyme at the branch point of diacylglycerol utilization, were reduced. EGF effects on DGAT and on palmitate esterification occurred at 2-10 ng/ml, whereas effects on I-FABP and palmitate uptake occurred only at 10 ng/ml. This suggests that EGF inhibited palmitate uptake by reducing the I-FABP level and shifted its utilization from triglycerides to phospholipids by inhibiting DGAT. This increase in phospholipid synthesis might play a role in the restoration of enterocyte absorption function after intestinal mucosa injury. (+info)
The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat. (2/783)1. The specific activities of long-chain fatty acid-CoA ligase (EC184.108.40.206) and of long-chain fatty acyl-CoA hydrolase (EC220.127.116.11) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids. (+info)
Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane. (3/783)Long-chain fatty acyl-CoA synthetase (FACS) catalyzes esterification of long-chain fatty acids (LCFAs) with coenzyme A (CoA), the first step in fatty acid metabolism. FACS has been shown to play a role in LCFA import into bacteria and implicated to function in mammalian cell LCFA import. In the present study, we demonstrate that FACS overexpression in fibroblasts increases LCFA uptake, and overexpression of both FACS and the fatty acid transport protein (FATP) have synergistic effects on LCFA uptake. To explore how FACS contributes to LCFA import, we examined the subcellular location of this enzyme in 3T3-L1 adipocytes which natively express this protein and which efficiently take up LCFAs. We demonstrate for the first time that FACS is an integral membrane protein. Subcellular fractionation of adipocytes by differential density centrifugation reveals immunoreactive and enzymatically active FACS in several membrane fractions, including the plasma membrane. Immunofluorescence studies on adipocyte plasma membrane lawns confirm that FACS resides at the plasma membrane of adipocytes, where it co-distributes with FATP. Taken together, our data support a model in which imported LCFAs are immediately esterified at the plasma membrane upon uptake, and in which FATP and FACS function coordinately to facilitate LCFA movement across the plasma membrane of mammalian cells. (+info)
Development and initial evaluation of a novel method for assessing tissue-specific plasma free fatty acid utilization in vivo using (R)-2-bromopalmitate tracer. (4/783)We describe a method for assessing tissue-specific plasma free fatty acid (FFA) utilization in vivo using a non-beta-oxidizable FFA analog, [9,10-3H]-(R)-2-bromopalmitate (3H-R-BrP). Ideally 3H-R-BrP would be transported in plasma, taken up by tissues and activated by the enzyme acyl-CoA synthetase (ACS) like native FFA, but then 3H-labeled metabolites would be trapped. In vitro we found that 2-bromopalmitate and palmitate compete equivalently for the same ligand binding sites on albumin and intestinal fatty acid binding protein, and activation by ACS was stereoselective for the R-isomer. In vivo, oxidative and non-oxidative FFA metabolism was assessed in anesthetized Wistar rats by infusing, over 4 min, a mixture of 3H-R-BrP and [U-14C] palmitate (14C-palmitate). Indices of total FFA utilization (R*f) and incorporation into storage products (Rfs') were defined, based on tissue concentrations of 3H and 14C, respectively, 16 min after the start of tracer infusion. R*f, but not Rfs', was substantially increased in contracting (sciatic nerve stimulated) hindlimb muscles compared with contralateral non-contracting muscles. The contraction-induced increases in R*f were completely prevented by blockade of beta-oxidation with etomoxir. These results verify that 3H-R-BrP traces local total FFA utilization, including oxidative and non-oxidative metabolism. Separate estimates of the rates of loss of 3H activity indicated effective 3H metabolite retention in most tissues over a 16-min period, but appeared less effective in liver and heart. In conclusion, simultaneous use of 3H-R-BrP and [14C]palmitate tracers provides a new useful tool for in vivo studies of tissue-specific FFA transport, utilization and metabolic fate, especially in skeletal muscle and adipose tissue. (+info)
Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35. (5/783)A pimeloyl-CoA synthetase from Pseudomonas mendocina 35 was purified and characterized, the DNA sequence determined, and the gene cloned into Escherichia coli to yield an active enzyme. The purified enzyme had a pH optimum of approximately 8.0, Km values of 0.49 mM for pimelic acid, 0.18 mM for CoA and 0.72 mM for ATP, a subunit Mr of approximately 80000 as determined by SDS/PAGE, and was found to be a tetramer by gel-filtration chromatography. The specific activity of the purified enzyme was 77.3 units/mg of protein. The enzyme was not absolutely specific for pimelic acid. The relative activity for adipic acid (C6) was 72% and for azaleic acid (C9) was 18% of that for pimelic acid (C7). The N-terminal amino acid was blocked to amino acid sequencing, but controlled proteolysis resulted in three peptide fragments for which amino acid sequences were obtained. An oligonucleotide gene probe corresponding to one of the amino acid sequences was synthesized and used to isolate the gene (pauA, pimelic acid-utilizing A) coding for pimeloyl-CoA synthetase. The pauA gene, which codes for a protein with a theoretical Mr of 74643, was then sequenced. The deduced amino acid sequence of the enzyme showed similarity to hypothetical proteins from Archaeoglobus fulgidus, Methanococcus jannaschii, Pyrococcus horikoshii, E. coli and Streptomyces coelicolor, and some limited similarity to microbial succinyl-CoA synthetases. The similarity with the protein from A. fulgidus was especially strong, thus indicating a function for this unidentified protein. The pauA gene was cloned into E. coli, where it was expressed and resulted in an active enzyme. (+info)
Preventing neurodegeneration in the Drosophila mutant bubblegum. (6/783)The Drosophila melanogaster recessive mutant bubblegum (bgm) exhibits adult neurodegeneration, with marked dilation of photoreceptor axons. The bubblegum mutant shows elevated levels of very long chain fatty acids (VLCFAs), as seen in the human disease adrenoleukodystrophy (ALD). In ALD, the excess can be lowered by dietary treatment with "Lorenzo's oil," a mixture of unsaturated fatty acids. Feeding the fly mutant one of the components, glyceryl trioleate oil, blocked the accumulation of excess VLCFAs as well as development of the pathology. Mutant flies thus provide a potential model system for studying mechanisms of neurodegenerative disease and screening drugs for treatment. (+info)
The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. (7/783)Biochemical and genetic evidence is presented to demonstrate that the prpE gene of Salmonella typhimurium encodes propionyl-CoA synthetase, an enzyme required for the catabolism of propionate in this bacterium. While prpE mutants used propionate as carbon and energy source, prpE mutants that lacked acetyl-CoA synthetase (encoded by acs) did not, indicating that Acs can compensate for the lack of PrpE in prpE mutants. Cell-free extracts enriched for PrpE catalysed the formation of propionyl-CoA in a propionate-, ATP-, Mg2+- and HS-CoA dependent manner. Acetate substituted for propionate in the reaction at 48% the rate of propionate; butyrate was not a substrate for PrpE. The propionyl-CoA synthetase activity of PrpE was specific for ATP. GTP, ITP, CTP and TTP were not used as substrates by the enzyme. UV-visible spectrophotometry, HPLC and MS data demonstrated that propionyl-CoA was the product of the reaction catalysed by PrpE. (+info)
Biosynthesis of 1,2-dieicosapentaenoyl-sn-glycero-3-phosphocholine in Caenorhabditis elegans. (8/783)Previously, we showed that lowering the growth temperature increased the level of eicosapentaenoic acid (EPA) in the phosphatidylcholine (PtdCho) of Caenorhabditis elegans. In this study, we investigated the molecular species composition of PtdCho of C. elegans, with an emphasis on EPA-containing species. C. elegans contained a substantial amount of 1,2-dipolyunsaturated fatty acid-containing PtdCho (1,2-diPUFA-PtdCho) species, such as arachidonic acid/EPA and EPA/EPA, which are unusual phospholipids in higher animals. The EPA/EPA-PtdCho content was significantly increased in C. elegans grown at a low temperature. To examine the possibility that the acyltransferase activity involved in the remodeling of phospholipids accounts for the production of 1,2-diPUFA-PtdCho, we investigated the substrate specificity of this enzyme in C. elegans and found that it did not exhibit a preference for saturated fatty acid for acylation to the sn-1 position of PtdCho. The efficacy of the esterification of EPA to the sn-1 position was almost equal to that of stearic acid. The lack of preference for a saturated fatty acid for acylation to the sn-1 position of PtdCho is thought to result in the existence of the unusual 1,2-diEPA-PtdCho in C. elegans. (+info)
There are several types of muscular atrophy, including:
1. Disuse atrophy: This type of atrophy occurs when a muscle is not used for a long period, leading to its degeneration.
2. Neurogenic atrophy: This type of atrophy occurs due to damage to the nerves that control muscles.
3. Dystrophic atrophy: This type of atrophy occurs due to inherited genetic disorders that affect muscle fibers.
4. Atrophy due to aging: As people age, their muscles can degenerate and lose mass and strength.
5. Atrophy due to disease: Certain diseases such as cancer, HIV/AIDS, and muscular dystrophy can cause muscular atrophy.
6. Atrophy due to infection: Infections such as polio and tetanus can cause muscular atrophy.
7. Atrophy due to trauma: Traumatic injuries can cause muscular atrophy, especially if the injury is severe and leads to prolonged immobilization.
Muscular atrophy can lead to a range of symptoms depending on the type and severity of the condition. Some common symptoms include muscle weakness, loss of motor function, muscle wasting, and difficulty performing everyday activities. Treatment for muscular atrophy depends on the underlying cause and may include physical therapy, medication, and lifestyle changes such as exercise and dietary modifications. In severe cases, surgery may be necessary to restore muscle function.
There are several methods for diagnosing myringosclerosis, including:
1. Otoscopy: an examination of the outer ear and eardrum using a specialized instrument called an otoscope.
2. Tympanometry: a test that measures the movement of the eardrum and the reflexes of the middle ear muscles.
3. Acoustic reflectometry: a test that uses sound waves to measure the stiffness of the eardrum.
4. Auditory brainstem response (ABR) testing: a test that measures the electrical activity of the hearing nerve in response to sound.
There is no cure for myringosclerosis, but there are several treatment options available, including:
1. Hearing aids: devices that amplify sound and can help improve hearing.
2. Cochlear implants: devices that bypass the damaged part of the ear and directly stimulate the auditory nerve.
3. Surgery: in some cases, surgery may be necessary to remove the affected portion of the eardrum.
4. Medications: certain medications, such as corticosteroids, may be prescribed to help reduce inflammation and improve hearing.
It is important to seek medical attention if you experience any symptoms of myringosclerosis, as early diagnosis and treatment can help improve outcomes.
There are several types of genomic instability, including:
1. Chromosomal instability (CIN): This refers to changes in the number or structure of chromosomes, such as aneuploidy (having an abnormal number of chromosomes) or translocations (the movement of genetic material between chromosomes).
2. Point mutations: These are changes in a single base pair in the DNA sequence.
3. Insertions and deletions: These are changes in the number of base pairs in the DNA sequence, resulting in the insertion or deletion of one or more base pairs.
4. Genomic rearrangements: These are changes in the structure of the genome, such as chromosomal breaks and reunions, or the movement of genetic material between chromosomes.
Genomic instability can arise from a variety of sources, including environmental factors, errors during DNA replication and repair, and genetic mutations. It is often associated with cancer, as cancer cells have high levels of genomic instability, which can lead to the development of resistance to chemotherapy and radiation therapy.
Research into genomic instability has led to a greater understanding of the mechanisms underlying cancer and other diseases, and has also spurred the development of new therapeutic strategies, such as targeted therapies and immunotherapies.
In summary, genomic instability is a key feature of cancer cells and is associated with various diseases, including cancer, neurodegenerative disorders, and aging. It can arise from a variety of sources and is the subject of ongoing research in the field of molecular biology.
PKAN typically presents in children during the first few years of life, and is characterized by progressive loss of motor skills, cognitive decline, and vision loss. Affected individuals may also experience seizures, difficulty with speech and communication, and changes in behavior. The disorder is often diagnosed based on a combination of clinical features, genetic testing, and imaging studies such as magnetic resonance imaging (MRI) or positron emission tomography (PET).
The underlying pathology of PKAN involves the accumulation of a toxic protein called aggregated pantothenate kinase, which disrupts normal cellular function and leads to progressive degeneration of brain cells. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression. This may include medications to control seizures and muscle spasticity, physical therapy to maintain mobility and strength, and supportive care to address cognitive and behavioral changes.
PKAN is a rare disorder, and the prevalence is not well-defined. However, it is estimated to affect approximately 1 in 200,000 individuals worldwide. The progression of PKAN can be variable, with some individuals experiencing a rapid decline in cognitive and motor functions, while others may have a more gradual course.
In summary, pantothenate kinase-associated neurodegeneration (PKAN) is a rare genetic disorder that affects the brain and spinal cord, causing progressive loss of motor skills, cognitive decline, and vision loss. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression.
Neoplasm refers to an abnormal growth of cells that can be benign (non-cancerous) or malignant (cancerous). Neoplasms can occur in any part of the body and can affect various organs and tissues. The term "neoplasm" is often used interchangeably with "tumor," but while all tumors are neoplasms, not all neoplasms are tumors.
Types of Neoplasms
There are many different types of neoplasms, including:
1. Carcinomas: These are malignant tumors that arise in the epithelial cells lining organs and glands. Examples include breast cancer, lung cancer, and colon cancer.
2. Sarcomas: These are malignant tumors that arise in connective tissue, such as bone, cartilage, and fat. Examples include osteosarcoma (bone cancer) and soft tissue sarcoma.
3. Lymphomas: These are cancers of the immune system, specifically affecting the lymph nodes and other lymphoid tissues. Examples include Hodgkin lymphoma and non-Hodgkin lymphoma.
4. Leukemias: These are cancers of the blood and bone marrow that affect the white blood cells. Examples include acute myeloid leukemia (AML) and chronic lymphocytic leukemia (CLL).
5. Melanomas: These are malignant tumors that arise in the pigment-producing cells called melanocytes. Examples include skin melanoma and eye melanoma.
Causes and Risk Factors of Neoplasms
The exact causes of neoplasms are not fully understood, but there are several known risk factors that can increase the likelihood of developing a neoplasm. These include:
1. Genetic predisposition: Some people may be born with genetic mutations that increase their risk of developing certain types of neoplasms.
2. Environmental factors: Exposure to certain environmental toxins, such as radiation and certain chemicals, can increase the risk of developing a neoplasm.
3. Infection: Some neoplasms are caused by viruses or bacteria. For example, human papillomavirus (HPV) is a common cause of cervical cancer.
4. Lifestyle factors: Factors such as smoking, excessive alcohol consumption, and a poor diet can increase the risk of developing certain types of neoplasms.
5. Family history: A person's risk of developing a neoplasm may be higher if they have a family history of the condition.
Signs and Symptoms of Neoplasms
The signs and symptoms of neoplasms can vary depending on the type of cancer and where it is located in the body. Some common signs and symptoms include:
1. Unusual lumps or swelling
4. Weight loss
5. Change in bowel or bladder habits
6. Unexplained bleeding
7. Coughing up blood
8. Hoarseness or a persistent cough
9. Changes in appetite or digestion
10. Skin changes, such as a new mole or a change in the size or color of an existing mole.
Diagnosis and Treatment of Neoplasms
The diagnosis of a neoplasm usually involves a combination of physical examination, imaging tests (such as X-rays, CT scans, or MRI scans), and biopsy. A biopsy involves removing a small sample of tissue from the suspected tumor and examining it under a microscope for cancer cells.
The treatment of neoplasms depends on the type, size, location, and stage of the cancer, as well as the patient's overall health. Some common treatments include:
1. Surgery: Removing the tumor and surrounding tissue can be an effective way to treat many types of cancer.
2. Chemotherapy: Using drugs to kill cancer cells can be effective for some types of cancer, especially if the cancer has spread to other parts of the body.
3. Radiation therapy: Using high-energy radiation to kill cancer cells can be effective for some types of cancer, especially if the cancer is located in a specific area of the body.
4. Immunotherapy: Boosting the body's immune system to fight cancer can be an effective treatment for some types of cancer.
5. Targeted therapy: Using drugs or other substances to target specific molecules on cancer cells can be an effective treatment for some types of cancer.
Prevention of Neoplasms
While it is not always possible to prevent neoplasms, there are several steps that can reduce the risk of developing cancer. These include:
1. Avoiding exposure to known carcinogens (such as tobacco smoke and radiation)
2. Maintaining a healthy diet and lifestyle
3. Getting regular exercise
4. Not smoking or using tobacco products
5. Limiting alcohol consumption
6. Getting vaccinated against certain viruses that are associated with cancer (such as human papillomavirus, or HPV)
7. Participating in screening programs for early detection of cancer (such as mammograms for breast cancer and colonoscopies for colon cancer)
8. Avoiding excessive exposure to sunlight and using protective measures such as sunscreen and hats to prevent skin cancer.
It's important to note that not all cancers can be prevented, and some may be caused by factors that are not yet understood or cannot be controlled. However, by taking these steps, individuals can reduce their risk of developing cancer and improve their overall health and well-being.
A vitamin B6 deficiency happens when the body does not get enough of this essential nutrient. Vitamin B6 is needed for many bodily functions, such as making new blood cells, keeping the nervous system healthy, and helping to convert food into energy.
The symptoms of a vitamin B6 deficiency can range from mild to severe and may include:
1. Fatigue or weakness: A lack of vitamin B6 can cause tiredness, weakness, and a general feeling of being unwell.
2. Irritability or depression: Vitamin B6 plays a role in the production of neurotransmitters, such as serotonin and dopamine, which are important for mood regulation. A deficiency can lead to feelings of irritability, anxiety, and depression.
3. Nausea and vomiting: Vitamin B6 helps with the absorption of nutrients from food, so a deficiency can cause nausea and vomiting.
4. Skin problems: Vitamin B6 is important for the health of the skin, and a deficiency can lead to conditions such as acne, eczema, and dermatitis.
5. Weight loss: A vitamin B6 deficiency can make it harder to gain weight or maintain weight loss.
Causes of Vitamin B6 Deficiency:
1. Poor diet: A diet that is low in vitamin B6 can lead to a deficiency. Foods rich in vitamin B6 include meat, fish, poultry, whole grains, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease or inflammatory bowel disease, can make it harder for the body to absorb vitamin B6 from food.
3. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher need for vitamin B6 and may be more likely to develop a deficiency if they do not consume enough of this nutrient.
4. Alcoholism: Heavy alcohol consumption can interfere with the absorption of vitamin B6, leading to a deficiency.
5. Certain medications: Some medications, such as antidepressants and anti-inflammatory drugs, can interfere with the absorption of vitamin B6.
Signs and Symptoms of Vitamin B6 Deficiency:
1. Depression or anxiety
2. Fatigue or weakness
3. Irritability or mood swings
4. Skin problems, such as acne or eczema
5. Nausea and vomiting
6. Weight loss or difficulty gaining weight
7. Difficulty walking or maintaining balance
8. Headaches or migraines
9. Muscle weakness or cramps
10. Seizures or convulsions (in severe cases)
Treatment of Vitamin B6 Deficiency:
1. Dietary changes: Increasing the intake of vitamin B6-rich foods, such as lean meats, whole grains, and vegetables, can help treat a deficiency.
2. Supplements: Taking a vitamin B6 supplement can help treat a deficiency. The recommended daily dose is 1.3-2.0 mg per day for adults.
3. Addressing underlying causes: If the deficiency is caused by an underlying medical condition, such as celiac disease or alcoholism, treating the condition can help resolve the deficiency.
4. Vitamin B complex supplements: Taking a vitamin B complex supplement that contains all eight B vitamins can help ensure that the body is getting enough of this essential nutrient.
In conclusion, vitamin B6 is an essential nutrient that plays a crucial role in many bodily functions. Deficiency in this vitamin can lead to a range of health problems, from mild discomforts like fatigue and nausea to more severe conditions like seizures and convulsions. Treatment of a deficiency typically involves dietary changes, supplements, and addressing any underlying medical conditions. It is important to seek medical advice if symptoms persist or worsen over time.
There are several types of hypercholesterolemia, including:
1. Familial hypercholesterolemia: This is an inherited condition that causes high levels of low-density lipoprotein (LDL) cholesterol, also known as "bad" cholesterol, in the blood.
2. Non-familial hypercholesterolemia: This type of hypercholesterolemia is not inherited and can be caused by a variety of factors, such as a high-fat diet, lack of exercise, obesity, and certain medical conditions, such as hypothyroidism or polycystic ovary syndrome (PCOS).
3. Mixed hypercholesterolemia: This type of hypercholesterolemia is characterized by high levels of both LDL and high-density lipoprotein (HDL) cholesterol in the blood.
The diagnosis of hypercholesterolemia is typically made based on a physical examination, medical history, and laboratory tests, such as a lipid profile, which measures the levels of different types of cholesterol and triglycerides in the blood. Treatment for hypercholesterolemia usually involves lifestyle changes, such as a healthy diet and regular exercise, and may also include medication, such as statins, to lower cholesterol levels.
The exact cause of cachexia is not fully understood, but it is thought to be related to a combination of factors such as inflammation, hormonal imbalances, and changes in metabolism. Treatment for cachexia often focuses on addressing the underlying cause of the wasting, such as managing cancer or HIV/AIDS, as well as providing nutritional support and addressing any related complications.
In the medical field, cachexia is a serious condition that requires careful management to improve quality of life and outcomes for patients. It is important for healthcare providers to be aware of the signs and symptoms of cachexia and to provide appropriate treatment and support to affected individuals.
Mitochondrial encephalomyopathies can be classified into several types based on the specific symptoms and the location of the mutations in the mitochondrial DNA. Some of the most common forms of these disorders include:
1. MELAS syndrome (mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes): This is a rare condition that affects the brain, muscles, and other organs. It is characterized by recurrent stroke-like episodes, seizures, and muscle weakness.
2. Kearns-Sayre syndrome: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive weakness and paralysis of the muscles, as well as vision loss and cognitive impairment.
3. Chronic progressive external ophthalmoplegia (CPEO): This is a rare disorder that affects the muscles of the eyes and the extraocular system. It is characterized by progressive weakness of the eye muscles, which can lead to droopy eyelids, double vision, and other vision problems.
4. Mitochondrial DNA depletion syndrome: This is a group of disorders that are caused by a decrease in the amount of mitochondrial DNA. These disorders can affect various parts of the body, including the brain, muscles, and other organs. They can cause a wide range of symptoms, including muscle weakness, seizures, and vision loss.
5. Myoclonic dystonia: This is a rare genetic disorder that affects the muscles and the nervous system. It is characterized by muscle stiffness, spasms, and myoclonus (involuntary jerky movements).
6. Neuronal ceroid lipofuscinoses (NCL): These are a group of rare genetic disorders that affect the brain and the nervous system. They can cause progressive loss of cognitive and motor functions, as well as vision loss and seizures.
7. Spinocerebellar ataxia: This is a group of rare genetic disorders that affect the cerebellum and the spinal cord. They can cause progressive weakness, coordination problems, and other movement disorders.
8. Friedreich's ataxia: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive loss of coordination and balance, as well as muscle weakness and wasting.
9. Charcot-Marie-Tooth disease: This is a group of rare genetic disorders that affect the peripheral nerves. They can cause muscle weakness, numbness or tingling in the hands and feet, and other problems with movement and sensation.
10. Progressive supranuclear palsy: This is a rare genetic disorder that affects the brain and the nervous system. It is characterized by progressive loss of movement control, as well as dementia and behavioral changes.
It is important to note that this list is not exhaustive and there may be other rare movement disorders that are not included here. If you suspect that you or a loved one may have a rare movement disorder, it is important to consult with a healthcare professional for proper diagnosis and treatment.
Coenzyme F420-0:L-glutamate ligase
Coenzyme F420-1:gamma-L-glutamate ligase
Coenzyme gamma-F420-2:alpha-L-glutamate ligase
Very long-chain acyl-CoA synthetase
Succinyl coenzyme A synthetase
Acid-CoA ligase (GDP-forming)
List of EC numbers (EC 6)
Succinate-CoA ligase (ADP-forming)
List of enzymes
Coenzyme A Ligases - Medical Dictionary
Intraorganellar localization of CoASH-independent phytanic acid oxidation in human liver peroxisomes
Succinate-CoA ligase deficiency: MedlinePlus Genetics
Chromosome 6 - wikidoc
Nanoparticles of Titanium and Zinc Oxides as Novel Agents in Tumor Treatment: a Review | SpringerLink
Cullin Proteins | Profiles RNS
Pesquisa | Portal Regional da BVS
Aligments for a candidate for acs in Magnetospirillum magneticum AMB-1
Polyketide Synthases | Colorado PROFILES
Silibinin Ameliorates Formaldehyde-Induced Cognitive Impairment by Inhibiting Oxidative Stress
Heterologous production of the antifugal polyketide antibiotic soraphen A of Sorangium cellulosum So ce26 in Streptomyces...
Kromosomang 6 (tao) - Wikipedia, ang malayang ensiklopedya
View source for FF:10693-109F9 - resource browser
Biosynthesis and Regulation of Antioxidant Flavonolignans in Milk Thistle | IntechOpen
phosphatase complex - Ontology Browser - Rat Genome Database
Center for Drug Discovery - Research output - Research Profiles at Washington University School of Medicine
Pre GI: Gene
Dichloromethane dehalogenase - Wikipedia
Skeletal muscle mitochondrial interactome remodeling is linked to functional decline in aged female mice | Nature Aging
LOCUS BAB96591.1 69 aa PRT BCT 29-SEP-2018
PhD Students | Max Planck Institute for Plant Breeding Research
Making Cholesterol-Lowering Statin Drugs More Effective Against Cancer - Cancer Treatments - from Research to Application
- 6. Ligases : Enzymes catalysing the synthetic reactions (Greek : ligate-to bind) where two molecules are joined together and ATP is used. (slideshare.net)
- Specifically, we identify age-related changes in protein cross-links relating to assembly of electron transport system complexes I and IV, activity of glutamate dehydrogenase, and coenzyme-A binding in fatty acid β-oxidation and tricarboxylic acid cycle enzymes. (nature.com)
- coenzyme (non-protein organic part). (slideshare.net)
- Studies of the intraorganellar site of alpha-oxidation of [1-14C]phytanic acid to pristanic acid in peroxisomes isolated from human liver demonstrate that phytanoyl-CoA ligase is present in the peroxisomal membrane and that the enzyme system for alpha-oxidation of phytanic acid to pristanic acid is in the peroxisomal matrix. (nih.gov)
- The SUCLA2 and SUCLG1 genes each provide instructions for making one part (subunit) of an enzyme called succinate-CoA ligase. (medlineplus.gov)
- Each enzyme is given a specific name indicating the substrate, coenzyme (if any) and the type of the reaction catalysed by the enzyme. (slideshare.net)
- Glutamate-cysteine ligase family 2(GCS2) [Interproscan]. (ntu.edu.sg)
- 3, 363-377 (1996) REFERENCE 7 AUTHORS Arn,E.A. and Abelson,J.N. TITLE The 2'-5' RNA ligase of Escherichia coli. (nig.ac.jp)
- Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. (uchicago.edu)
Live only into childhood or adolescence1
- These infections can be life-threatening, and most people with succinate-CoA ligase deficiency live only into childhood or adolescence. (medlineplus.gov)
- DNA sequencing revealed a homozygous 2-bp deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle enzyme succinate-coenzyme A ligase (SUCL). (nih.gov)
- The SUCLA2 and SUCLG1 genes each provide instructions for making one part (subunit) of an enzyme called succinate-CoA ligase. (medlineplus.gov)
- Succinate-CoA ligase deficiency is an inherited disorder that affects the early development of the brain and other body systems. (medlineplus.gov)
- Most children with succinate-CoA ligase deficiency also experience a failure to thrive, which means that they gain weight and grow more slowly than expected. (medlineplus.gov)
- Succinate-CoA ligase deficiency causes breathing difficulties that often lead to recurrent infections of the respiratory tract. (medlineplus.gov)
- A few individuals with succinate-CoA ligase deficiency have had an even more severe form of the disorder known as fatal infantile lactic acidosis. (medlineplus.gov)
- Although the exact prevalence of succinate-CoA ligase deficiency is unknown, it appears to be very rare. (medlineplus.gov)
- Succinate-CoA ligase deficiency results from mutations in the SUCLA2 or SUCLG1 gene. (medlineplus.gov)
- These problems lead to hypotonia, muscle weakness, and the other characteristic features of succinate-CoA ligase deficiency. (medlineplus.gov)
- Mutations in either the SUCLA2 or SUCLG1 gene disrupt the normal function of succinate-CoA ligase. (medlineplus.gov)