Lipoprotein Lipase
Lipase
Lipoproteins
Lipoproteins, LDL
Lipoproteins, VLDL
Lipoproteins, HDL
Hyperlipoproteinemia Type I
Apolipoprotein C-II
Lipoprotein(a)
Chylomicrons
Heparin
Apolipoproteins C
Apolipoproteins
Receptors, Lipoprotein
Lipolysis
Adipose Tissue
Cholesterol
Lipids
Apolipoproteins B
Receptors, LDL
Cholesterol, HDL
Lipoproteins, IDL
Lipoprotein Lipase Activators
Liver
Apolipoproteins E
Lipid Metabolism
Lipoproteins, HDL2
Lipoproteins, HDL3
Cholesterol Esters
Hyperlipoproteinemias
Sterol Esterase
Angiopoietins
Low Density Lipoprotein Receptor-Related Protein-1
Cholesterol, LDL
Monoacylglycerol Lipases
Apolipoprotein C-III
Apolipoproteins A
Milk
Fatty Acids, Nonesterified
Cholesterol, VLDL
Dietary Fats
Apolipoprotein B-100
Heparin Lyase
Fatty Acids
Arteriosclerosis
Hyperlipoproteinemia Type IV
Molecular Sequence Data
Emulsions
Hyperlipidemia, Familial Combined
Apolipoprotein A-II
Cells, Cultured
RNA, Messenger
Apolipoprotein B-48
Cattle
Cholesterol Ester Transfer Proteins
Macrophages
Colipases
Ultracentrifugation
Insulin
Hypercholesterolemia
Phospholipids
Carrier Proteins
Base Sequence
Adipocytes
Amino Acid Sequence
Lipid Mobilization
Hyperlipoproteinemia Type III
Phosphatidylcholine-Sterol O-Acyltransferase
Myocardium
Hyperlipoproteinemia Type V
Rats, Inbred Strains
Esterification
Polysaccharide-Lyases
Hyperlipoproteinemia Type II
Hypolipidemic Agents
Protein Binding
Heterozygote
Apolipoprotein E2
Adipose Tissue, Brown
Oleic Acid
Body Weight
Mutation
Electrophoresis, Polyacrylamide Gel
Oleic Acids
Chromatography, Affinity
Biological Transport
LDL-Receptor Related Protein-Associated Protein
Pancreas
Deoxyribonuclease HindIII
Cricetinae
Oxidation-Reduction
Atherosclerosis
Heparan Sulfate Proteoglycans
Binding Sites
Carboxylic Ester Hydrolases
Mice, Knockout
Apoproteins
Chromatography, Agarose
alpha-Macroglobulins
Scavenger Receptors, Class B
Hypolipoproteinemias
Protamines
Heparitin Sulfate
CHO Cells
Antigens, CD36
Receptors, Immunologic
Gene Expression Regulation, Enzymologic
Apolipoprotein C-I
Rabbits
Obesity
Glycoproteins
Genotype
Glycerol
Reference Values
Apolipoprotein E3
Gene Expression
Enzyme Activation
Receptors, Scavenger
Mice, Transgenic
Structure-Activity Relationship
Rhizopus
Phosphatidylcholines
Apoprotein(a)
Dyslipidemias
Lactones
Blotting, Northern
Chromatography, Gel
Phospholipid Transfer Proteins
Coronary Disease
LDL-Receptor Related Proteins
Sterol O-Acyltransferase
Lipid Metabolism, Inborn Errors
Geotrichum
Iodine Radioisotopes
Transfection
Hydroxymethylglutaryl CoA Reductases
Muscle, Skeletal
Electrophoresis, Agar Gel
Insulin Resistance
Gene Expression Regulation
Rats, Sprague-Dawley
Caloric restriction leads to regional specialisation of adipocyte function in the rat. (1/1971)
The study analysed the responses of three metabolic parameters in five distinct adipose tissue depots to caloric restriction (4 weeks) in the rat. The aims were to evaluate whether specific adipose tissue depots were recruited for triacylglycerol (TAG) storage and/or mobilisation, and to determine to what extent specific adipose tissue depots exhibited preferences for the source of fatty acid (FA) for TAG storage. Caloric restriction led to a general enhancement of the response of lipoprotein lipase (LPL), FA synthesis and glucose utilisation to a meal. Effects were particularly marked in the parametrial, perirenal and interscapular depots compared with mesenteric and subcutaneous depots. There was no evidence that individual depots selectively expressed a preference for the pathways concerned with the generation of FA for storage (the exogenous (LPL) and the endogenous (synthesis) pathway). However, the temporal sequence of activation of these pathways differed in a manner consistent with a switch from preponderant use of FA produced via de novo synthesis during the very early phase of feeding towards later use of FA derived from circulating TAG. The overall excursions in insulin levels observed in the calorie-restricted rats were comparable to those found in free-feeding rats, but the magnitude and the rapidity of the individual metabolic responses of the adipocyte were augmented. The data are consistent with a general enhancement of insulin sensitivity and responsiveness in adipose tissue of calorie-restricted rats, together with adaptive regional specialisation of adipocyte function. These adaptations would be predicted to facilitate the immediate conservation of dietary nutrients by promoting their storage as the FA or glycerol moieties of adipose tissue TAG and thereby to ensure the regulated release of FA and glycerol from adipose tissue in accordance with the requirement for glucose conservation and/or production. (+info)Binding of beta-VLDL to heparan sulfate proteoglycans requires lipoprotein lipase, whereas ApoE only modulates binding affinity. (2/1971)
The binding of beta-VLDL to heparan sulfate proteoglycans (HSPG) has been reported to be stimulated by both apoE and lipoprotein lipase (LPL). In the present study we investigated the effect of the isoform and the amount of apoE per particle, as well as the role of LPL on the binding of beta-VLDL to HSPG. Therefore, we isolated beta-VLDL from transgenic mice, expressing either APOE*2(Arg158-->Cys) or APOE*3-Leiden (E2-VLDL and E3Leiden-VLDL, respectively), as well as from apoE-deficient mice containing no apoE at all (Enull-VLDL). In the absence of LPL, the binding affinity and maximal binding capacity of all beta-VLDL samples for HSPG-coated microtiter plates was very low. Addition of LPL to this cell-free system resulted in a 12- to 55-fold increase in the binding affinity and a 7- to 15-fold increase in the maximal binding capacity (Bmax). In the presence of LPL, the association constant (Ka) tended to increase in the order Enull-VLDLInduced mutant mouse lines that express lipoprotein lipase in cardiac muscle, but not in skeletal muscle and adipose tissue, have normal plasma triglyceride and high-density lipoprotein-cholesterol levels. (3/1971)
The tissue-specific expression of lipoprotein lipase (LPL) in adipose tissue (AT), skeletal muscle (SM), and cardiac muscle (CM) is rate-limiting for the uptake of triglyceride (TG)-derived free fatty acids and decisive in the regulation of energy balance and lipoprotein metabolism. To investigate the tissue-specific metabolic effects of LPL, three independent transgenic mouse lines were established that expressed a human LPL (hLPL) minigene predominantly in CM. Through cross-breeding with heterozygous LPL knockout mice, animals were generated that produced hLPL mRNA and enzyme activity in CM but lacked the enzyme in SM and AT because of the absence of the endogenous mouse LPL gene (L0-hLPL). LPL activity in CM and postheparin plasma of L0-hLPL mice was reduced by 34% and 60%, respectively, compared with control mice. This reduced LPL expression was sufficient to rescue LPL knockout mice from neonatal death. L0-hLPL animals developed normally with regard to body weight and body-mass composition. Plasma TG levels in L0-hLPL animals were increased up to 10-fold during the suckling period but normalized after weaning and decreased in adult animals. L0-hLPL mice had normal plasma high-density lipoprotein (HDL)-cholesterol levels, indicating that LPL expression in CM alone was sufficient to allow for normal HDL production. The absence of LPL in SM and AT did not cause detectable morphological or histopathological changes in these tissues. However, the lipid composition in AT and SM exhibited a marked decrease in polyunsaturated fatty acids. From this genetic model of LPL deficiency in SM and AT, it can be concluded that CM-specific LPL expression is a major determinant in the regulation of plasma TG and HDL-cholesterol levels. (+info)Response of adipose tissue lipoprotein lipase to the cephalic phase of insulin secretion. (4/1971)
Modulation of lipoprotein lipase (LPL) allows a tissue-specific partitioning of triglyceride-derived fatty acids, and insulin is a major modulator of its activity. The present studies were aimed to assess in rats the contribution of insulin to the response of adipose tissue and muscle LPL to food intake. Epididymal and retroperitoneal adipose LPL rose 65% above fasting values as early as 1 h after the onset of a 30-min high-carbohydrate meal, with a second activity peak 1 h later that was maintained for an additional 2 h. Soleus muscle LPL was decreased by 25% between 0.5 and 4 h after meal intake. The essential contribution of insulin to the LPL response to food intake was determined by preventing the full insulin response to meal intake by administration of diazoxide (150 mg/kg body wt, in the meal). The usual postprandial changes in adipose and muscle LPL did not occur in the absence of an increase in insulinemia. However, the early (60 min) increase in adipose tissue LPL was not prevented by the drug, likely because of the maintenance of the early centrally mediated phase of insulin secretion. In a subsequent study, rats chronically implanted with a gastric cannula were used to demonstrate that the postprandial rise in adipose LPL is independent of nutrient absorption and can be elicited by the cephalic (preabsorptive) phase of insulin secretion. Obese Zucker rats were used because of their strong cephalic insulin response. After an 8-h fast, rats were fed a liquid diet ad libitum (orally, cannula closed), sham fed (orally, cannula opened), or fed directly into the stomach via the cannula during 4 h. Insulinemia increased 10-fold over fasting levels in ad libitum- and intragastric-fed rats and threefold in sham-fed rats. Changes in adipose tissue LPL were proportional to the elevation in plasma insulin levels, demonstrating that the cephalic-mediated rise in insulinemia, in the absence of nutrient absorption, stimulates adipose LPL. These results demonstrate the central role of insulin in the postprandial response of tissue LPL, and they show that cephalically mediated insulin secretion is able to stimulate adipose LPL. (+info)Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. (5/1971)
Lipoprotein lipase and the receptor-associated protein (RAP) bind to overlapping sites on the low density lipoprotein receptor-related protein/alpha2-macroglobulin receptor (LRP). We have investigated if lipoprotein lipase interacts with the RAP binding but structurally distinct receptor sortilin/neurotensin receptor-3. We show, by chemical cross-linking and surface plasmon resonance analysis, that soluble sortilin binds lipoprotein lipase with an affinity similar to that of LRP. The binding was inhibited by heparin and RAP and by the newly discovered sortilin ligand neurotensin. In 35S-labeled 3T3-L1 adipocytes treated with the cross-linker dithiobis(succinimidyl propionate), lipoprotein lipase-containing complexes were isolated by anti-sortilin antibodies. To elucidate function in cells, sortilin-negative Chinese hamster ovary cells were transfected with full-length sortilin and shown to express about 8% of the receptors on the cell surface. These cells degraded 125I-labeled lipoprotein lipase much faster than the wild-type cells. The degradation was inhibited by unlabeled lipoprotein lipase, indicating a saturable pathway, and by RAP and heparin. Moreover, inhibition by the weak base chloroquine suggested that degradation occurs in an acidic vesicle compartment. The results demonstrate that sortilin is a multifunctional receptor that binds lipoprotein lipase and, when expressed on the cell surface, mediates its endocytosis and degradation. (+info)Role of protein kinase C in the translational regulation of lipoprotein lipase in adipocytes. (6/1971)
The hypertriglyceridemia of diabetes is accompanied by decreased lipoprotein lipase (LPL) activity in adipocytes. Although the mechanism for decreased LPL is not known, elevated glucose is known to increase diacylglycerol, which activates protein kinase C (PKC). To determine whether PKC is involved in the regulation of LPL, we studied the effect of 12-O-tetradecanoyl phorbol 13-acetate (TPA) on adipocytes. LPL activity was inhibited when TPA was added to cultures of 3T3-F442A and rat primary adipocytes. The inhibitory effect of TPA on LPL activity was observed after 6 h of treatment, and was observed at a concentration of 6 nM. 100 nM TPA yielded maximal (80%) inhibition of LPL. No stimulation of LPL occurred after short term addition of TPA to cultures. To determine whether TPA treatment of adipocytes decreased LPL synthesis, cells were labeled with [35S]methionine and LPL protein was immunoprecipitated. LPL synthetic rate decreased after 6 h of TPA treatment. Western blot analysis of cell lysates indicated a decrease in LPL mass after TPA treatment. Despite this decrease in LPL synthesis, there was no change in LPL mRNA in the TPA-treated cells. Long term treatment of cells with TPA is known to down-regulate PKC. To assess the involvement of the different PKC isoforms, Western blotting was performed. TPA treatment of 3T3-F442A adipocytes decreased PKC alpha, beta, delta, and epsilon isoforms, whereas PKC lambda, theta, zeta, micro, iota, and gamma remained unchanged or decreased minimally. To directly assess the effect of PKC inhibition, PKC inhibitors (calphostin C and staurosporine) were added to cultures. The PKC inhibitors inhibited LPL activity rapidly (within 60 min). Thus, activation of PKC did not increase LPL, but inhibition of PKC resulted in decreased LPL synthesis by inhibition of translation, indicating a constitutive role of PKC in LPL gene expression. (+info)Association of lipoprotein lipase gene polymorphisms with coronary artery disease. (7/1971)
OBJECTIVES: The purpose of this study was to test whether the HindIII (+) and PvuII (-) or (+) restriction enzyme-defined alleles are associated with angiographic coronary artery disease (CAD). BACKGROUND: Lipoprotein lipase (LPL) plays a central role in lipid metabolism, hydrolyzing triglyceride in chylomicrons and very low density lipoproteins. Polymorphic variants of the LPL gene are common and might affect risk of CAD. METHODS: Blood was drawn from 725 patients undergoing coronary angiography. Leukocyte deoxyribonucleic acid segments containing the genomic sites were amplified by the polymerase chain reaction and digested, and polymorphisms were identified after electrophoresis in 1.5% agarose gel. RESULTS: In no-CAD control subjects (n = 168), HindIII (-) and (+) allelic frequencies were 28.6% and 71.4%, and (-) and (+) alleles were carried by 44.0% and 86.9% of subjects, respectively. Control PvuII (-) and (+) allelic frequencies were 41.7% and 58.3%, and (-) and (+) alleles were carried by 64.3% and 81.0%, respectively. In CAD patients (>60% stenosis; n = 483), HindIII (+) allelic carriage was increased (93.8% of patients, odds ratio [OR] = 2.28, confidence interval [CI] 1.27 to 4.00). Also, PvuII (-) allelic carriage tended to be more frequent in CAD patients (OR = 1.33, CI 0.92 to 1.93). Adjusted for six CAD risk factors and the other polymorphism, HindIII (+) carriage was associated with an OR = 2.86, CI 1.50 to 5.42, p = 0.0014, and PvulI (-) carriage, OR = 1.42, CI 0.95 to 2.12, p = 0.09. The two polymorphisms were in strong linkage disequilibrium, and a haplotype association was suggested. CONCLUSIONS: The common LPL polymorphic allele, HindIII (+), is moderately associated with CAD, and the PvuII (-) allele is modestly associated (trend). Genetic variants of LPL deserve further evaluation as risk factors for CAD. (+info)Lipoprotein lipase activity is decreased in a large cohort of patients with coronary artery disease and is associated with changes in lipids and lipoproteins. (8/1971)
Lipoprotein lipase (LPL) is crucial in the hydrolysis of triglycerides (TG) in TG-rich lipoproteins in the formation of HDL particles. As both these lipoproteins play an important role in the pathogenesis of atherosclerotic vascular disease, we sought to assess the relationship between post-heparin LPL (PH-LPL) activity and lipids and lipoproteins in a large, well-defined cohort of Dutch males with coronary artery disease (CAD). These subjects were drawn from the REGRESS study, totaled 730 in number and were evaluated against 75 healthy, normolipidemic male controls. Fasting mean PH-LPL activity in the CAD subjects was 108 46 mU/ml, compared to 138 44 mU/ml in controls (P < 0.0001). When these patients were divided into activity quartiles, those in the lowest versus the highest quartile had higher levels of TG (P < 0.001), VLDLc and VLDL-TG (P = 0.001). Conversely, levels of TC, LDL, and HDLc were lower in these patients (P = 0.001, P = 0.02, and P = 0.001, respectively). Also, in this cohort PH-LPL relationships with lipids and lipoproteins were not altered by apoE genotypes. The frequency of common mutations in the LPL gene associated with partial LPL deficiency (N291S and D9N carriers) in the lowest quartile for LPL activity was more than double the frequency in the highest quartile (12.0% vs. 5.0%; P = 0.006). By contrast, the frequency of the S447X LPL variant rose from 11.5% in the lowest to 18.3% (P = 0.006) in the highest quartile. This study, in a large cohort of CAD patients, has shown that PH-LPL activity is decreased (22%; P = 0.001) when compared to controls; that the D9N and N291S, and S447X LPL variants are genetic determinants, respectively, in CAD patients of low and high LPL PH-LPL activities; and that PH-LPL activity is strongly associated with changes in lipids and lipoproteins. (+info)The condition is caused by mutations in the genes that code for proteins involved in cholesterol transport and metabolism, particularly the low-density lipoprotein receptor gene. This leads to a deficiency of functional LDL receptors on the surface of liver cells, resulting in excessive accumulation of LDL cholesterol in the bloodstream.
Symptoms of hyperlipoproteinemia Type I can include xanthomas (yellowish deposits of cholesterol in the skin), corneal arcus (a white deposit on the edge of the cornea), and early-onset cardiovascular disease, such as heart attacks or strokes.
Treatment for hyperlipoproteinemia Type I typically involves a combination of dietary changes, such as reducing intake of saturated and trans fats and cholesterol, and medications, such as statins, to lower LDL cholesterol levels. In some cases, medical procedures such as liver transplantation or gene therapy may be necessary to treat the condition.
There are several causes of hypertriglyceridemia, including:
* Genetics: Some people may inherit a tendency to have high triglyceride levels due to genetic mutations that affect the genes involved in triglyceride metabolism.
* Obesity: Excess body weight is associated with higher triglyceride levels, as there is more fat available for energy.
* Diabetes: Both type 1 and type 2 diabetes can lead to high triglyceride levels due to insulin resistance and altered glucose metabolism.
* High-carbohydrate diet: Consuming high amounts of carbohydrates, particularly refined or simple carbohydrates, can cause a spike in blood triglycerides.
* Alcohol consumption: Drinking too much alcohol can increase triglyceride levels in the blood.
* Certain medications: Some drugs, such as anabolic steroids and some antidepressants, can raise triglyceride levels.
* Underlying medical conditions: Certain medical conditions, such as hypothyroidism, kidney disease, and polycystic ovary syndrome (PCOS), can also contribute to high triglyceride levels.
Hypertriglyceridemia is typically diagnosed with a blood test that measures the level of triglycerides in the blood. Treatment options for hypertriglyceridemia depend on the underlying cause of the condition, but may include lifestyle modifications such as weight loss, dietary changes, and medications to lower triglyceride levels.
There are several types of hyperlipoproteinemias, each with distinct clinical features and laboratory findings. The most common forms include:
1. Familial hypercholesterolemia (FH): This is the most common type of hyperlipoproteinemia, caused by mutations in the LDLR gene that codes for the low-density lipoprotein receptor. FH is characterized by extremely high levels of low-density lipoprotein (LDL) cholesterol in the blood, which can lead to premature cardiovascular disease, including heart attacks and strokes.
2. Familial hypobetalipoproteinemia (FHBL): This rare disorder is caused by mutations in the APOB100 gene that codes for a protein involved in lipid metabolism. FHBL is characterized by very low levels of low-density lipoprotein (LDL) and high-density lipoprotein (HDL) cholesterol, as well as a deficiency of Apolipoprotein B-100, a protein that helps transport lipids in the blood.
3. Hypertriglyceridemia: This condition is caused by mutations in genes that regulate triglyceride metabolism, leading to extremely high levels of triglycerides in the blood. Hypertriglyceridemia can increase the risk of pancreatitis and other health problems.
4. Lipoprotein lipase deficiency: This rare disorder is caused by mutations in the LPL gene that codes for the enzyme lipoprotein lipase, which helps break down triglycerides in the blood. Lipoprotein lipase deficiency can lead to very high levels of triglycerides and cholesterol in the blood, increasing the risk of pancreatitis and other health problems.
5. Familial dyslipidemia: This is a group of rare inherited disorders that affect lipid metabolism and can cause extremely high or low levels of various types of cholesterol and triglycerides in the blood. Some forms of familial dyslipidemia are caused by mutations in genes that code for enzymes involved in lipid metabolism, while others may be caused by unknown factors.
6. Chylomicronemia: This rare disorder is characterized by extremely high levels of chylomicrons (type of triglyceride-rich lipoprotein) in the blood, which can increase the risk of pancreatitis and other health problems. The exact cause of chylomicronemia is not fully understood, but it may be related to genetic mutations or other factors that affect lipid metabolism.
7. Hyperchylomicronemia: This rare disorder is similar to chylomicronemia, but it is characterized by extremely high levels of chylomicrons in the blood, as well as very low levels of HDL (good) cholesterol. Hyperchylomicronemia can increase the risk of pancreatitis and other health problems.
8. Hypoalphalipoproteinemia: This rare disorder is characterized by extremely low levels of apolipoprotein A-I (ApoA-I), a protein that plays a key role in lipid metabolism and helps to regulate the levels of various types of cholesterol and triglycerides in the blood. Hypoalphalipoproteinemia can increase the risk of pancreatitis and other health problems.
9. Hypobetalipoproteinemia: This rare disorder is characterized by extremely low levels of apolipoprotein B (ApoB), a protein that helps to regulate the levels of various types of cholesterol and triglycerides in the blood. Hypobetalipoproteinemia can increase the risk of pancreatitis and other health problems.
10. Sitosterolemia: This rare genetic disorder is caused by mutations in the gene that codes for sterol-CoA-desmethylase (SCD), an enzyme involved in the metabolism of plant sterols. Sitosterolemia can cause elevated levels of plant sterols and sitosterol in the blood, which can increase the risk of pancreatitis and other health problems.
11. Familial hyperchylomicronemia type 1 (FHMC1): This rare genetic disorder is caused by mutations in the gene that codes for apolipoprotein C-II (APOC2), a protein that helps to regulate the levels of various types of cholesterol and triglycerides in the blood. FHMC1 can cause elevated levels of chylomicrons and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
12. Familial hyperchylomicronemia type 2 (FHMC2): This rare genetic disorder is caused by mutations in the gene that codes for apolipoprotein A-IV (APOA4), a protein that helps to regulate the levels of various types of cholesterol and triglycerides in the blood. FHMC2 can cause elevated levels of chylomicrons and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
13. Lipoprotein (a) deficiency: This rare genetic disorder is caused by mutations in the gene that codes for apolipoprotein (a), a protein that helps to regulate the levels of lipoproteins in the blood. Lipoprotein (a) deficiency can cause low levels of lipoprotein (a) and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
14. Chylomicron retention disease: This rare genetic disorder is caused by mutations in the gene that codes for apolipoprotein C-II (APOC2), a protein that helps to regulate the levels of chylomicrons in the blood. Chylomicron retention disease can cause elevated levels of chylomicrons and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
15. Hypertriglyceridemia-apolipoprotein C-II deficiency: This rare genetic disorder is caused by mutations in the gene that codes for apolipoprotein C-II (APOC2), a protein that helps to regulate the levels of triglycerides in the blood. Hypertriglyceridemia-apolipoprotein C-II deficiency can cause elevated levels of triglycerides and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
16. Familial partial lipodystrophy (FPLD): This rare genetic disorder is characterized by the loss of fat tissue in certain areas of the body, such as the arms, legs, and buttocks. FPLD can cause elevated levels of lipids in the blood, which can increase the risk of pancreatitis and other health problems.
17. Lipodystrophy: This rare genetic disorder is characterized by the loss of fat tissue in certain areas of the body, such as the face, arms, and legs. Lipodystrophy can cause elevated levels of lipids in the blood, which can increase the risk of pancreatitis and other health problems.
18. Abetalipoproteinemia: This rare genetic disorder is caused by mutations in the gene that codes for apolipoprotein B, a protein that helps to regulate the levels of lipids in the blood. Abetalipoproteinemia can cause elevated levels of triglycerides and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
19. Chylomicronemia: This rare genetic disorder is characterized by the presence of excessively large amounts of chylomicrons (type of lipid particles) in the blood. Chylomicronemia can cause elevated levels of triglycerides and other lipids in the blood, which can increase the risk of pancreatitis and other health problems.
20. Hyperlipidemia due to medications: Certain medications, such as corticosteroids and some anticonvulsants, can cause elevated levels of lipids in the blood.
It's important to note that many of these disorders are rare and may not be common causes of high triglycerides. Additionally, there may be other causes of high triglycerides that are not listed here. It's important to talk to a healthcare provider for proper evaluation and diagnosis if you have concerns about your triglyceride levels.
There are several types of hyperlipidemia, including:
1. High cholesterol: This is the most common type of hyperlipidemia and is characterized by elevated levels of low-density lipoprotein (LDL) cholesterol, also known as "bad" cholesterol.
2. High triglycerides: This type of hyperlipidemia is characterized by elevated levels of triglycerides in the blood. Triglycerides are a type of fat found in the blood that is used for energy.
3. Low high-density lipoprotein (HDL) cholesterol: HDL cholesterol is known as "good" cholesterol because it helps remove excess cholesterol from the bloodstream and transport it to the liver for excretion. Low levels of HDL cholesterol can contribute to hyperlipidemia.
Symptoms of hyperlipidemia may include xanthomas (fatty deposits on the skin), corneal arcus (a cloudy ring around the iris of the eye), and tendon xanthomas (tender lumps under the skin). However, many people with hyperlipidemia have no symptoms at all.
Hyperlipidemia can be diagnosed through a series of blood tests that measure the levels of different types of cholesterol and triglycerides in the blood. Treatment for hyperlipidemia typically involves dietary changes, such as reducing intake of saturated fats and cholesterol, and increasing physical activity. Medications such as statins, fibric acid derivatives, and bile acid sequestrants may also be prescribed to lower cholesterol levels.
In severe cases of hyperlipidemia, atherosclerosis (hardening of the arteries) can occur, which can lead to cardiovascular disease, including heart attacks and strokes. Therefore, it is important to diagnose and treat hyperlipidemia early on to prevent these complications.
Arteriosclerosis can affect any artery in the body, but it is most commonly seen in the arteries of the heart, brain, and legs. It is a common condition that affects millions of people worldwide and is often associated with aging and other factors such as high blood pressure, high cholesterol, diabetes, and smoking.
There are several types of arteriosclerosis, including:
1. Atherosclerosis: This is the most common type of arteriosclerosis and occurs when plaque builds up inside the arteries.
2. Arteriolosclerosis: This type affects the small arteries in the body and can cause decreased blood flow to organs such as the kidneys and brain.
3. Medial sclerosis: This type affects the middle layer of the artery wall and can cause stiffness and narrowing of the arteries.
4. Intimal sclerosis: This type occurs when plaque builds up inside the innermost layer of the artery wall, causing it to become thick and less flexible.
Symptoms of arteriosclerosis can include chest pain, shortness of breath, leg pain or cramping during exercise, and numbness or weakness in the limbs. Treatment for arteriosclerosis may include lifestyle changes such as a healthy diet and regular exercise, as well as medications to lower blood pressure and cholesterol levels. In severe cases, surgery may be necessary to open up or bypass blocked arteries.
The condition is caused by mutations in genes that code for enzymes involved in lipid metabolism, such as ACY1 and APOB100. These mutations lead to a deficiency in the breakdown and transport of lipids in the body, resulting in the accumulation of chylomicrons and other lipoproteins in the blood.
Symptoms of hyperlipoproteinemia Type IV can include abdominal pain, fatigue, and joint pain, as well as an increased risk of pancreatitis and cardiovascular disease. Treatment typically involves a combination of dietary modifications, such as reducing intake of saturated fats and cholesterol, and medications to lower lipid levels. In severe cases, liver transplantation may be necessary.
Hyperlipoproteinemia Type IV is a rare disorder, and the prevalence is not well-defined. However, it is estimated to affect approximately 1 in 100,000 individuals worldwide. The condition can be diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis.
In summary, hyperlipoproteinemia Type IV is a rare genetic disorder that affects the metabolism of lipids and lipoproteins in the body, leading to elevated levels of chylomicrons and other lipoproteins in the blood, as well as low levels of HDL. The condition can cause a range of symptoms and is typically treated with dietary modifications and medications.
The condition is caused by mutations in genes that code for proteins involved in lipid metabolism, such as the low-density lipoprotein receptor gene (LDLR), apolipoprotein A-1 gene (APOA1), and proprotein convertase subtilisin/kexin type 9 (PCSK9) genes. These mutations can lead to the overproduction or underexpression of certain lipids, leading to the characteristic lipid abnormalities seen in HeFH.
HeFH is usually inherited in an autosomal dominant manner, meaning that a single copy of the mutated gene is enough to cause the condition. However, some cases may be caused by recessive inheritance or de novo mutations. The condition can affect both children and adults, and it is important for individuals with HeFH to be monitored closely by a healthcare provider to manage their lipid levels and reduce the risk of cardiovascular disease.
Treatment for HeFH typically involves a combination of dietary modifications, such as reducing saturated fat intake and increasing fiber and omega-3 fatty acid intake, and medications, such as statins, to lower cholesterol levels. In some cases, apheresis or liver transplantation may be necessary to reduce lipid levels. Early detection and management of HeFH can help prevent or delay the development of cardiovascular disease, which is the leading cause of death worldwide.
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 condition is caused by mutations in the genes that code for proteins involved in lipid metabolism, such as the LDL receptor gene or the apoB100 gene. These mutations lead to a deficiency of functional LDL receptors on the surface of liver cells, which results in reduced clearance of LDL cholesterol from the blood and increased levels of LDL-C.
The main symptom of hyperlipoproteinemia type III is very high levels of LDL-C (>500 mg/dL) and low levels of HDL-C (<20 mg/dL). Other signs and symptoms may include xanthomas (fatty deposits in the skin), corneal arcus (a cloudy ring around the cornea of the eye), and an increased risk of cardiovascular disease.
Treatment for hyperlipoproteinemia type III typically involves a combination of dietary changes, such as reducing intake of saturated fats and cholesterol, and medications, such as statins or other lipid-lowering drugs, to lower LDL-C levels. In severe cases, a liver transplant may be necessary.
Hyperlipoproteinemia type III is an autosomal dominant disorder, meaning that a single copy of the mutated gene is enough to cause the condition. It is important to identify and treat individuals with this condition early to prevent or delay the development of cardiovascular disease.
People with hyperlipoproteinemia type V often have a history of low birth weight and growth retardation, and may experience a range of health problems including fatigue, muscle weakness, and liver disease. The disorder is usually inherited in an autosomal recessive pattern, meaning that a person must inherit two copies of the mutated gene - one from each parent - to develop the condition.
Treatment for hyperlipoproteinemia type V typically involves a combination of dietary changes and medication. Dietary recommendations may include avoiding foods high in saturated fats and cholesterol, and increasing intake of unsaturated fats, such as those found in nuts and vegetable oils. Medications may include drugs that raise HDL levels or lower LDL levels, such as niacin or statins. In severe cases, liver transplantation may be necessary.
In summary, hyperlipoproteinemia type V is a rare genetic disorder that affects the metabolism of lipids and lipoproteins in the body, leading to extremely low levels of LDL cholesterol and high levels of HDL cholesterol. Treatment typically involves a combination of dietary changes and medication, and may include liver transplantation in severe cases.
The condition is caused by mutations in the genes that code for proteins involved in cholesterol transport and metabolism, such as the low-density lipoprotein receptor gene (LDLR) or the PCSK9 gene. These mutations lead to a decrease in the ability of the liver to remove excess cholesterol from the bloodstream, resulting in high levels of LDL cholesterol and low levels of HDL cholesterol.
Hyperlipoproteinemia type II is usually inherited in an autosomal dominant pattern, meaning that a single copy of the mutated gene is enough to cause the condition. However, some cases can be caused by spontaneous mutations or incomplete penetrance, where not all individuals with the mutated gene develop the condition.
Symptoms of hyperlipoproteinemia type II can include xanthomas (yellowish deposits of cholesterol in the skin), corneal arcus (a white, waxy deposit on the iris of the eye), and tendon xanthomas (small, soft deposits of cholesterol under the skin). Treatment typically involves a combination of dietary changes and medication to lower LDL cholesterol levels and increase HDL cholesterol levels. In severe cases, liver transplantation may be necessary.
Hyperlipoproteinemia type II is a serious condition that can lead to cardiovascular disease, including heart attacks, strokes, and peripheral artery disease. Early diagnosis and treatment are important to prevent or delay the progression of the disease and reduce the risk of complications.
Body weight is an important health indicator, as it can affect an individual's risk for certain medical conditions, such as obesity, diabetes, and cardiovascular disease. Maintaining a healthy body weight is essential for overall health and well-being, and there are many ways to do so, including a balanced diet, regular exercise, and other lifestyle changes.
There are several ways to measure body weight, including:
1. Scale: This is the most common method of measuring body weight, and it involves standing on a scale that displays the individual's weight in kg or lb.
2. Body fat calipers: These are used to measure body fat percentage by pinching the skin at specific points on the body.
3. Skinfold measurements: This method involves measuring the thickness of the skin folds at specific points on the body to estimate body fat percentage.
4. Bioelectrical impedance analysis (BIA): This is a non-invasive method that uses electrical impulses to measure body fat percentage.
5. Dual-energy X-ray absorptiometry (DXA): This is a more accurate method of measuring body composition, including bone density and body fat percentage.
It's important to note that body weight can fluctuate throughout the day due to factors such as water retention, so it's best to measure body weight at the same time each day for the most accurate results. Additionally, it's important to use a reliable scale or measuring tool to ensure accurate measurements.
The disease begins with endothelial dysfunction, which allows lipid accumulation in the artery wall. Macrophages take up oxidized lipids and become foam cells, which die and release their contents, including inflammatory cytokines, leading to further inflammation and recruitment of more immune cells.
The atherosclerotic plaque can rupture or ulcerate, leading to the formation of a thrombus that can occlude the blood vessel, causing ischemia or infarction of downstream tissues. This can lead to various cardiovascular diseases such as myocardial infarction (heart attack), stroke, and peripheral artery disease.
Atherosclerosis is a multifactorial disease that is influenced by genetic and environmental factors such as smoking, hypertension, diabetes, high cholesterol levels, and obesity. It is diagnosed by imaging techniques such as angiography, ultrasound, or computed tomography (CT) scans.
Treatment options for atherosclerosis include lifestyle modifications such as smoking cessation, dietary changes, and exercise, as well as medications such as statins, beta blockers, and angiotensin-converting enzyme (ACE) inhibitors. In severe cases, surgical interventions such as bypass surgery or angioplasty may be necessary.
In conclusion, atherosclerosis is a complex and multifactorial disease that affects the arteries and can lead to various cardiovascular diseases. Early detection and treatment can help prevent or slow down its progression, reducing the risk of complications and improving patient outcomes.
The most common form of hypolipoproteinemia is familial hypobetalipoproteinemia (FHBL), which is caused by mutations in the gene encoding apoB, a protein component of low-density lipoproteins (LDL). People with FHBL have extremely low levels of LDL cholesterol and often develop symptoms such as fatty liver disease, liver cirrhosis, and cardiovascular disease.
Another form of hypolipoproteinemia is familial hypoalphalipoproteinemia (FHAL), which is caused by mutations in the gene encoding apoA-I, a protein component of high-density lipoproteins (HDL). People with FHAL have low levels of HDL cholesterol and often develop symptoms such as cardiovascular disease and premature coronary artery disease.
Hypolipoproteinemia can be diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment for the disorder typically involves managing associated symptoms and reducing lipid levels through diet, exercise, and medication. In some cases, liver transplantation may be necessary.
Prevention of hypolipoproteinemia is challenging, as it is often inherited in an autosomal recessive pattern, meaning that both parents must be carriers of the mutated gene to pass it on to their children. However, genetic counseling and testing can help identify carriers and allow for informed family planning.
Overall, hypolipoproteinemia is a rare and complex group of disorders that affect lipid metabolism and transport. While treatment and management options are available, prevention and early diagnosis are key to reducing the risk of complications associated with these disorders.
There are several different types of obesity, including:
1. Central obesity: This type of obesity is characterized by excess fat around the waistline, which can increase the risk of health problems such as type 2 diabetes and cardiovascular disease.
2. Peripheral obesity: This type of obesity is characterized by excess fat in the hips, thighs, and arms.
3. Visceral obesity: This type of obesity is characterized by excess fat around the internal organs in the abdominal cavity.
4. Mixed obesity: This type of obesity is characterized by both central and peripheral obesity.
Obesity can be caused by a variety of factors, including genetics, lack of physical activity, poor diet, sleep deprivation, and certain medications. Treatment for obesity typically involves a combination of lifestyle changes, such as increased physical activity and a healthy diet, and in some cases, medication or surgery may be necessary to achieve weight loss.
Preventing obesity is important for overall health and well-being, and can be achieved through a variety of strategies, including:
1. Eating a healthy, balanced diet that is low in added sugars, saturated fats, and refined carbohydrates.
2. Engaging in regular physical activity, such as walking, jogging, or swimming.
3. Getting enough sleep each night.
4. Managing stress levels through relaxation techniques, such as meditation or deep breathing.
5. Avoiding excessive alcohol consumption and quitting smoking.
6. Monitoring weight and body mass index (BMI) on a regular basis to identify any changes or potential health risks.
7. Seeking professional help from a healthcare provider or registered dietitian for personalized guidance on weight management and healthy lifestyle choices.
There are several types of dyslipidemias, including:
1. Hyperlipidemia: Elevated levels of lipids and lipoproteins in the blood, which can increase the risk of CVD.
2. Hypolipidemia: Low levels of lipids and lipoproteins in the blood, which can also increase the risk of CVD.
3. Mixed dyslipidemia: A combination of hyperlipidemia and hypolipidemia.
4. Familial dyslipidemia: An inherited condition that affects the levels of lipids and lipoproteins in the blood.
5. Acquired dyslipidemia: A condition caused by other factors, such as poor diet or medication side effects.
Dyslipidemias can be diagnosed through a variety of tests, including fasting blood sugar (FBS), lipid profile, and apolipoprotein testing. Treatment for dyslipidemias often involves lifestyle changes, such as dietary modifications and increased physical activity, as well as medications to lower cholesterol and triglycerides.
In conclusion, dyslipidemias are abnormalities in the levels or composition of lipids and lipoproteins in the blood that can increase the risk of CVD. They can be caused by a variety of factors and diagnosed through several tests. Treatment often involves lifestyle changes and medications to lower cholesterol and triglycerides.
Coronary disease is often caused by a combination of genetic and lifestyle factors, such as high blood pressure, high cholesterol levels, smoking, obesity, and a lack of physical activity. It can also be triggered by other medical conditions, such as diabetes and kidney disease.
The symptoms of coronary disease can vary depending on the severity of the condition, but may include:
* Chest pain or discomfort (angina)
* Shortness of breath
* Fatigue
* Swelling of the legs and feet
* Pain in the arms and back
Coronary disease is typically diagnosed through a combination of physical examination, medical history, and diagnostic tests such as electrocardiograms (ECGs), stress tests, and cardiac imaging. Treatment for coronary disease may include lifestyle changes, medications to control symptoms, and surgical procedures such as angioplasty or bypass surgery to improve blood flow to the heart.
Preventative measures for coronary disease include:
* Maintaining a healthy diet and exercise routine
* Quitting smoking and limiting alcohol consumption
* Managing high blood pressure, high cholesterol levels, and other underlying medical conditions
* Reducing stress through relaxation techniques or therapy.
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.
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.
There are several factors that can contribute to the development of insulin resistance, including:
1. Genetics: Insulin resistance can be inherited, and some people may be more prone to developing the condition based on their genetic makeup.
2. Obesity: Excess body fat, particularly around the abdominal area, can contribute to insulin resistance.
3. Physical inactivity: A sedentary lifestyle can lead to insulin resistance.
4. Poor diet: Consuming a diet high in refined carbohydrates and sugar can contribute to insulin resistance.
5. Other medical conditions: Certain medical conditions, such as polycystic ovary syndrome (PCOS) and Cushing's syndrome, can increase the risk of developing insulin resistance.
6. Medications: Certain medications, such as steroids and some antipsychotic drugs, can increase insulin resistance.
7. Hormonal imbalances: Hormonal changes during pregnancy or menopause can lead to insulin resistance.
8. Sleep apnea: Sleep apnea can contribute to insulin resistance.
9. Chronic stress: Chronic stress can lead to insulin resistance.
10. Aging: Insulin resistance tends to increase with age, particularly after the age of 45.
There are several ways to diagnose insulin resistance, including:
1. Fasting blood sugar test: This test measures the level of glucose in the blood after an overnight fast.
2. Glucose tolerance test: This test measures the body's ability to regulate blood sugar levels after consuming a sugary drink.
3. Insulin sensitivity test: This test measures the body's ability to respond to insulin.
4. Homeostatic model assessment (HOMA): This is a mathematical formula that uses the results of a fasting glucose and insulin test to estimate insulin resistance.
5. Adiponectin test: This test measures the level of adiponectin, a protein produced by fat cells that helps regulate blood sugar levels. Low levels of adiponectin are associated with insulin resistance.
There is no cure for insulin resistance, but it can be managed through lifestyle changes and medication. Lifestyle changes include:
1. Diet: A healthy diet that is low in processed carbohydrates and added sugars can help improve insulin sensitivity.
2. Exercise: Regular physical activity, such as aerobic exercise and strength training, can improve insulin sensitivity.
3. Weight loss: Losing weight, particularly around the abdominal area, can improve insulin sensitivity.
4. Stress management: Strategies to manage stress, such as meditation or yoga, can help improve insulin sensitivity.
5. Sleep: Getting adequate sleep is important for maintaining healthy insulin levels.
Medications that may be used to treat insulin resistance include:
1. Metformin: This is a commonly used medication to treat type 2 diabetes and improve insulin sensitivity.
2. Thiazolidinediones (TZDs): These medications, such as pioglitazone, improve insulin sensitivity by increasing the body's ability to use insulin.
3. Sulfonylureas: These medications stimulate the release of insulin from the pancreas, which can help improve insulin sensitivity.
4. DPP-4 inhibitors: These medications, such as sitagliptin, work by reducing the breakdown of the hormone incretin, which helps to increase insulin secretion and improve insulin sensitivity.
5. GLP-1 receptor agonists: These medications, such as exenatide, mimic the action of the hormone GLP-1 and help to improve insulin sensitivity.
It is important to note that these medications may have side effects, so it is important to discuss the potential benefits and risks with your healthcare provider before starting treatment. Additionally, lifestyle modifications such as diet and exercise can also be effective in improving insulin sensitivity and managing blood sugar levels.
Lipoprotein lipase
Lipoprotein lipase deficiency
List of OMIM disorder codes
Pancreatic lipase family
Ibrolipim
Triacylglycerol lipase
Lipid metabolism
Apolipoprotein C-III
Omega-3 acid ethyl esters
GPIHBP1
Omega-3 carboxylic acids
Ethyl eicosapentaenoic acid
Chylomicron
Exoenzyme
Hepatic lipase
ANGPTL8
Sortilin 1
Claire Weekes
Placentation
Pseudemoia entrecasteauxii
Gene therapy
Lacteal
Carbonyl cyanide m-chlorophenyl hydrazone
ANGPTL4
Alipogene tiparvovec
Robert H. Eckel
Gemfibrozil
David J. Galton
Familial hypertriglyceridemia
Angiostrongylus cantonensis
LDL receptor
Index of biochemistry articles
Coconut oil
Lipid signaling
Wolfgang Patsch
Fenofibrate
List of skin conditions
Halobacterium
Medication-induced hyperlipoproteinemia
Fat globule
High-density lipoprotein
Low-density lipoprotein
Apolipoprotein C-II
Retina
PAFAH2
Hemophagocytic lymphohistiocytosis
Juliane Bogner-Strauß
Abetalipoproteinemia
Monoglyceride
LDL-receptor-related protein-associated protein
Fat embolism syndrome
Glycocalyx
List of enzymes
Lecithin-cholesterol acyltransferase
LRP1
Familial lipoprotein lipase deficiency - About the Disease - Genetic and Rare Diseases Information Center
Familial lipoprotein lipase deficiency: MedlinePlus Medical Encyclopedia
Familial lipoprotein lipase deficiency: MedlinePlus Medical Encyclopedia
Familial lipoprotein lipase deficiency: MedlinePlus Genetics
Human/Mouse Lipoprotein Lipase/LPL Antibody AF7197: R&D Systems
Familial Lipoprotein Lipase Deficiency - GeneReviews® - NCBI Bookshelf
Molecular pathobiology of the human lipoprotein lipase gene - PubMed
Lipoproteins - lipoprotein lipase Archives - Peter Attia
Human LIPD(Lipase, Lipoprotein) ELISA Kit - Global Life Sciences Conference in Warsaw
IMSEAR at SEARO: Recurrent Acute Pancreatitis Secondary to Lipoprotein Lipase Deficiency
Lipoprotein Lipase: Is It a Magic Target for the Treatment of Hypertriglyceridemia. | Endocrinol Metab (Seoul);37(4): 575-586,...
Control Set | MyBiosource | Europe & UK Distribution
Frontiers | Why Do Men Accumulate Abdominal Visceral Fat?
Is type 2 diabetes genetic? Causes, genes, and prevention
K. D. Taylor | RAND
NIH Guide: PROTEASE INHIBITOR RELATED ATHEROSCLEROSIS IN HIV INFECTION
Fenofibrate Capsules, USP
Publication Detail
Biomarkers Search
The Heterogeneity of White Adipose Tissue | IntechOpen
2016 A-M | Avon Longitudinal Study of Parents and Children | University of Bristol
Disuse-associated loss of the protease LONP1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass...
Hypertriglyceridemia: Practice Essentials, Pathophysiology, Etiology
Korn, Edward 2019 - Office of NIH History and Stetten Museum
Academic Success Week 07 - Lipid Metabolism & System-based Practice - ProProfs Quiz
Deficiency17
- Familial lipoprotein lipase deficiency is a rare genetic disorder is which a person lacks the enzyme lipoprotein lipase, a protein needed to break down fat molecules. (nih.gov)
- Familial lipoprotein lipase deficiency is caused by changes in the LPL gene. (nih.gov)
- When Do Symptoms of Familial lipoprotein lipase deficiency Begin? (nih.gov)
- Familial lipoprotein lipase deficiency is a genetic disease, which means that it is caused by one or more genes not working correctly. (nih.gov)
- Familial lipoprotein lipase deficiency is caused by a defective gene that is passed down through families. (nih.gov)
- Risk factors include a family history of lipoprotein lipase deficiency. (nih.gov)
- Pancreatitis that is related to lipoprotein lipase deficiency responds to treatments for that disorder. (nih.gov)
- Call your provider for screening if someone in your family has lipoprotein lipase deficiency. (nih.gov)
- Familial lipoprotein lipase deficiency is an inherited condition that disrupts the normal breakdown of fats in the body, resulting in an increase of certain kinds of fats. (nih.gov)
- People with familial lipoprotein lipase deficiency typically develop signs and symptoms before age 10, with one-quarter showing symptoms by age 1. (nih.gov)
- Approximately half of individuals with familial lipoprotein lipase deficiency develop small yellow deposits of fat under the skin called eruptive xanthomas. (nih.gov)
- The blood of people with familial lipoprotein lipase deficiency can have a milky appearance due to its high fat content. (nih.gov)
- In people with familial lipoprotein lipase deficiency, increased fat levels can also cause neurological features, such as depression , memory loss, and mild intellectual decline (dementia). (nih.gov)
- Mutations in the LPL gene cause familial lipoprotein lipase deficiency. (nih.gov)
- Mutations that cause familial lipoprotein lipase deficiency lead to a reduction or elimination of lipoprotein lipase activity, which prevents the enzyme from effectively breaking down triglycerides. (nih.gov)
- As a result, triglycerides attached to lipoproteins build up in the blood and tissues, leading to the signs and symptoms of familial lipoprotein lipase deficiency. (nih.gov)
- Familial lipoprotein lipase (LPL) deficiency usually presents in childhood and is characterized by very severe hypertriglyceridemia with episodes of abdominal pain, recurrent acute pancreatitis, eruptive cutaneous xanthomata, and hepatosplenomegaly. (nih.gov)
Triglycerides8
- This enzyme helps break down fats called triglycerides, which are carried by molecules called lipoproteins . (nih.gov)
- Lipoprotein lipase (LPL) is a key enzyme of lipid metabolism that hydrolyses triglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins. (inrae.fr)
- LPL is next bound by glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) and transported into the capillary, where it acts on chylomicrons and very-low-density lipoproteins (VLDLs) to hydrolyze packaged triglycerides and release FFAs. (inrae.fr)
- High levels of triglycerides (TG) and triglyceride -rich lipoproteins (TGRLs) confer a residual risk of cardiovascular disease after optimal low-density lipoprotein cholesterol (LDL-C)-lowering therapy . (bvsalud.org)
- In this paper, we propose that this congestion predisposes the chylomicron triglycerides to hydrolysis by lipoprotein lipase (LPL). (frontiersin.org)
- This is the enzyme lipoprotein lipase, which breaks down triglycerides (fats). (medicalnewstoday.com)
- Fenofibric acid, the active metabolite of fenofibrate, produces reductions in total cholesterol, LDL cholesterol, apolipoprotein B, total triglycerides and triglyceride rich lipoprotein (VLDL) in treated patients. (nih.gov)
- the triglycerides are subsequently transported throughout the circulation by triglyceride-rich lipoproteins. (medscape.com)
Hepatic lipase4
- Human LPL is a member of a superfamily of lipases that includes hepatic lipase and pancreatic lipase. (nih.gov)
- 25. Lipoprotein lipase and hepatic lipase: the role of asparagine-linked glycosylation in the expression of a functional enzyme. (nih.gov)
- 40. Domain exchange: characterization of a chimeric lipase of hepatic lipase and lipoprotein lipase. (nih.gov)
- Pregnancy effect on serum lipids.12 During pregnancy, there is an is associated with significant change in the functions of increase in the hepatic lipase activity and decrease in the normal liver. (who.int)
Lipids6
- The lipolytic processing of triglyceride-rich lipoproteins (TRLs) by lipoprotein lipase (LPL) is crucial for the delivery of dietary lipids to the heart, skeletal muscle, and adipose tissue. (inrae.fr)
- Valimaki M, Maass L, Harno K, Nikkila EA "Lipoprotein lipids and apoproteins during beta-blocker administration: comparison of penbutolol and atenolol. (drugs.com)
- Effects of pindolol and metoprolol on plasma lipids and lipoproteins. (drugs.com)
- Terent A, Ribacke M, Carlson LA "Long-term effect of pindolol on lipids and lipoproteins in men with newly diagnosed hypertension. (drugs.com)
- Effects of pindolol on serum lipids, apolipoproteins, and lipoproteins in patients with mild to moderate essential hypertension. (drugs.com)
- In clinical chemistry, over the last decade however, lipids have become associated with lipoprotein metabolism and atherosclerosis. (randox.com)
Lipid10
- Lipoprotein lipase (LPL) is a key regulator for TGs that hydrolyzes TGs to glycerol and free fatty acids in lipoprotein particles for lipid storage and consumption in peripheral organs. (bvsalud.org)
- 24. Lipoprotein lipase with a defect in lipid interface recognition in a case with type I hyperlipidaemia. (nih.gov)
- 27. Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding. (nih.gov)
- 31. Effect of lipid composition on lipoprotein lipase activity measured by a continuous fluorescence assay: effect of cholesterol supports an interfacial surface penetration model. (nih.gov)
- 33. Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets. (nih.gov)
- Lipid profile results showed that TG was significantly lipoproteins (LDLs) and increased triglyceride (TG) lower in the control group than in pregnant women. (who.int)
- Lipoprotein lipase -- An enzyme crucial to blood lipid metabolism. (nih.gov)
- Effect of metoprolol and pindolol monotherapy on plasma lipid- and lipoprotein-cholesterol levels (including the HDL subclasses) in mild hypertensive males and females. (drugs.com)
- Cholesterol measurements are used in the diagnosis and treatments of lipid lipoprotein metabolism disorders. (randox.com)
- Oxidised low-density lipoprotein concentration-early marker of an altered lipid metabolism in young women with PCOS. (randox.com)
Human lipoprotein7
- Detects human Lipoprotein Lipase/LPL in direct ELISAs and less than 1% cross-reactivity with recombinant human (rh) LIPG, rhLIPI, and rhPNLIPRP1 is observed. (rndsystems.com)
- Detection of Human Lipoprotein Lipase/LPL by Western Blot. (rndsystems.com)
- Lipoprotein Lipase/LPL was detected in immersion fixed SH-SY5Y human neuroblastoma cell line using Goat Anti-Human Lipoprotein Lipase/LPL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7197) at 10 µg/mL for 3 hours at room temperature. (rndsystems.com)
- 22. Construction and functional characterization of recombinant fusion proteins of human lipoprotein lipase and apolipoprotein CII. (nih.gov)
- 26. Structure-function analysis of D9N and N291S mutations in human lipoprotein lipase using molecular modelling. (nih.gov)
- 29. Effects of substitutions of glycine and asparagine for serine132 on activity and binding of human lipoprotein lipase to very low density lipoproteins. (nih.gov)
- 37. Mutagenesis in four candidate heparin binding regions (residues 279-282, 291-304, 390-393, and 439-448) and identification of residues affecting heparin binding of human lipoprotein lipase. (nih.gov)
Hydrolysis4
- 28. Post-heparin plasma hepatic triacylglycerol lipase-catalyzed hydrolysis of tributyrin. (nih.gov)
- 35. Severely impaired activity of lipoprotein lipase Arg243His is partially ameliorated by emulsifying phospholipids in in vitro triolein hydrolysis analysis. (nih.gov)
- 39. Preparation of chylomicrons and VLDL with monoacid-rich triacylglycerol and characterization of kinetic parameters in lipoprotein lipase-mediated hydrolysis in chickens. (nih.gov)
- It was out of this creative, heady atmosphere that Dr. Korn began his research, first in the lab of Chris Anfinsen working on the hydrolysis of lipoproteins. (nih.gov)
Metabolism1
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1), the protein that shuttles LPL to the capillary lumen, is essential for plasma triglyceride metabolism. (nih.gov)
Serum8
- Description: A sandwich quantitative ELISA assay kit for detection of Mouse Lipase, Lipoprotein (LIPD) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (lscwarsaw.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Lipase, Lipoprotein (LIPD) in serum, plasma, tissue homogenates, cell lysates and other biological fluids. (lscwarsaw.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Lipase, Lipoprotein (LIPD) in samples from serum, plasma, tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (lscwarsaw.com)
- Rossner S, Weiner L "Atenolol and metoprolol: comparison of effects on blood pressure and serum lipoproteins, and side effects. (drugs.com)
- Darga LL, Hakim MJ, Lucas CP, Franklin BA "Comparison of the effects of guanadrel sulfate and propranolol on blood pressure, functional capacity, serum lipoproteins and glucose in systemic hypertension. (drugs.com)
- Carlson LA, Ribacke M, Terent A "A long-term study on the effect of pindolol on serum lipoproteins: a preliminary report. (drugs.com)
- Effect of nandrolone decanoate on serum lipoprotein (a) and its isoforms in hemodialysis patients. (randox.com)
- Níveis Plasmàticos Elevados de Lipoproteína(a) Correlacionados com a Gravidade da Doenca Arterial Coronariana em Pacientes Submetidos à Angiografia (Increased Serum Levels of Lipoprotein(a) Correlated with the Severity of Coronary Artery Disease in Patients Submitted to Angiography. (randox.com)
Gene3
- These lipases are characterized by extensive homology, both at the level of the gene and the mature protein, suggesting that they have a common evolutionary origin. (nih.gov)
- Endothelial lipase (encoded by the LIPG gene) regulates the circulating level of high density lipoprotein cholesterol (HDL-C). It can also form a molecular bridge between endothelial cells and lipoproteins or circulating macrophages through interaction with heparan sulfate proteoglycans. (inrae.fr)
- lipoprotein lipase]Product Gene. (biocheminfo.org)
Chylomicrons1
- Since dietary fat is absorbed by the enterocytes and transported to the circulation in the forms of chylomicrons and very low density lipoproteins (VLDLs), it is crucial to understand how these lipoproteins are different between men and women. (frontiersin.org)
VLDL1
- VLDL = very low-density lipoprotein. (medscape.com)
Cholesterol2
- A variety of studies have demonstrated that elevated levels of total cholesterol (total-C), low density lipoprotein cholesterol (LDL-C), and apolipoprotein B (apo B), an LDL membrane complex, are associated with human atherosclerosis. (nih.gov)
- Similarly, decreased levels of high density lipoprotein cholesterol (HDL-C) and its transport complex, apolipoprotein A (apo AI and apo AII) are associated with the development of atherosclerosis. (nih.gov)
Particles2
- Through this mechanism, fenofibrate increases lipolysis and elimination of triglyceride-rich particles from plasma by activating lipoprotein lipase and reducing production of apoproteins C-III (an inhibitor of lipoprotein lipase activity). (nih.gov)
- Hyperlipoproteinemia is a metabolic disorder characterized by abnormally elevated concentrations of specific lipoprotein particles in the plasma. (medscape.com)
Hydrolyzes1
- It hydrolyzes, or breaks down, lipoprotein triacylglycerols. (nih.gov)
Atherosclerosis1
- This nonenzymatic action can increase cellular lipoprotein uptake and monocyte adhesion and contribute to atherosclerosis. (inrae.fr)
Antibody3
- PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse Lipoprotein Lipase/LPL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7197) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017 ). (rndsystems.com)
- Lipoprotein Lipase/LPL was detected in immersion fixed paraffin-embedded sections of human heart using Goat Anti-Human/Mouse Lipoprotein Lipase/LPL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7197) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC004 ). (rndsystems.com)
- 38. Identification of the epitope of a monoclonal antibody that inhibits heparin binding of lipoprotein lipase: new evidence for a carboxyl-terminal heparin-binding domain. (nih.gov)
Hypertriglyceridemia2
- Lipoprotein Lipase: Is It a Magic Target for the Treatment of Hypertriglyceridemia. (bvsalud.org)
- Determining which lipoprotein abnormality is the cause of hypertriglyceridemia is less straightforward. (medscape.com)
Density3
- The binding of LPL to glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 protects against LPL unfolding. (inrae.fr)
- Omega-3 fatty acids and fibrates are used to reduce TG levels, but many patients still have high TG and TGRL levels combined with low high-density lipoprotein concentration that need to be ideally treated. (bvsalud.org)
- In addition, treatment with fenofibrate results in increases in high density lipoprotein (HDL) and apoproteins apo AI and apo AII. (nih.gov)
Cardiovascular disease1
- Genest J, Libby P. Lipoprotein disorders and cardiovascular disease. (nih.gov)
Molecular1
- Lipoprotein lipase: recent contributions from molecular biology. (nih.gov)
Obese1
- The heparan sulfate mimetic Muparfostat aggravates steatohepatitis in obese mice due to its binding affinity to lipoprotein lipase. (nih.gov)
Insulin1
- Cardiac-specific VEGFB overexpression minimizes lipoprotein lipase task and increases insulin actions in rat center. (topoisomerasesignaling.com)
Activity3
- This test looks for lipoprotein lipase activity in your blood. (nih.gov)
- Because of a decrease in the activity of TG was highest in first trimester pregnancy and least lipoprotein lipase, very-LDL remains in the plasma for in the control group. (who.int)
- Although the precise mechanisms un- lipoprotein lipase activity.12. (who.int)
Expression1
- 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)
Alteration1
- 36. Alteration of chain length selectivity of a Rhizopus delemar lipase through site-directed mutagenesis. (nih.gov)
Approximately1
- A specific band was detected for Lipoprotein Lipase/LPL at approximately 55 kDa (as indicated). (rndsystems.com)
Storage2
- 21. The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage. (nih.gov)
- It blocks fat storage (the lipoprotein lipase enzyme) and keeps fat from returning post cut. (ironmagazine.com)
People1
- People with this condition lack an enzyme called lipoprotein lipase. (nih.gov)
Domain3
- publish that the intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding. (inrae.fr)
- 32. Site-directed mutagenesis of a putative heparin binding domain of avian lipoprotein lipase. (nih.gov)
- 34. Lipoprotein lipase domain function. (nih.gov)