Ceruloplasmin is a blue copper-containing protein primarily synthesized in the liver, functioning as a ferroxidase enzyme involved in iron homeostasis and contributing to copper transportation in the body.
A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.
A rare autosomal recessive disease characterized by the deposition of copper in the BRAIN; LIVER; CORNEA; and other organs. It is caused by defects in the ATP7B gene encoding copper-transporting ATPase 2 (EC 3.6.3.4), also known as the Wilson disease protein. The overload of copper inevitably leads to progressive liver and neurological dysfunction such as LIVER CIRRHOSIS; TREMOR; ATAXIA and intellectual deterioration. Hepatic dysfunction may precede neurologic dysfunction by several years.
Disorders in the processing of iron in the body: its absorption, transport, storage, and utilization. (From Mosby's Medical, Nursing, & Allied Health Dictionary, 4th ed)
Inborn errors of metal metabolism refer to genetic disorders resulting from mutations in genes encoding proteins involved in the transportation, storage, or utilization of essential metals, leading to imbalances that can cause toxicity or deficiency and subsequent impairment of normal physiological processes.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
An iron-binding beta1-globulin that is synthesized in the LIVER and secreted into the blood. It plays a central role in the transport of IRON throughout the circulation. A variety of transferrin isoforms exist in humans, including some that are considered markers for specific disease states.
A transient dilatation of the lymphatic vessels.
A condition produced by dietary or metabolic deficiency. The term includes all diseases caused by an insufficient supply of essential nutrients, i.e., protein (or amino acids), vitamins, and minerals. It also includes an inadequacy of calories. (From Dorland, 27th ed; Stedman, 25th ed)
The concrete oleoresin obtained from Pinus palustris Mill. (Pinaceae) and other species of Pinus. It contains a volatile oil, to which its properties are due, and to which form it is generally used. (Dorland, 28th ed) Turpentine is used as a solvent and an experimental irritant in biomedical research. Turpentine toxicity is of medical interest.
Anserine is a muscle fiber protein, specifically a myosin heavy chain isoform, which is predominantly found in slow-twitch, type I muscle fibers and contributes to their contractile properties, playing a role in force production and fatigue resistance.
Plasma glycoproteins that form a stable complex with hemoglobin to aid the recycling of heme iron. They are encoded in man by a gene on the short arm of chromosome 16.
Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
A sulfate salt of copper. It is a potent emetic and is used as an antidote for poisoning by phosphorus. It also can be used to prevent the growth of algae.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Serum globulins with high molecular weight. (Dorland, 28th ed)

The inhibition of myeloperoxidase by ceruloplasmin can be reversed by anti-myeloperoxidase antibodies. (1/796)

BACKGROUND: The purpose of this study was to characterize the recently reported inhibition of myeloperoxidase (MPO) by ceruloplasmin and to determine whether this may be disturbed in the presence of anti-MPO antibodies. METHODS: Specificity of the binding between ceruloplasmin and MPO was confirmed by Western blotting and enzyme-linked immunosorbent assay (ELISA), and the enzymatic activity of MPO was measured in the presence of ceruloplasmin, affinity-purified anti-MPO antibodies, or both. The affinity of the binding between MPO and ceruloplasmin and MPO and the anti-MPO antibodies was measured using a biosensor, with the results confirmed by chaotrope ELISA. RESULTS: Affinity-purified anti-MPO antibodies from patients with microscopic polyangiitis and florid renal vasculitis inhibited the binding between ceruloplasmin and MPO to a maximum of 72.9 +/- 12.8%, whereas those from patients with Wegener's granulomatosis and only minimal renal involvement inhibited the binding to a maximum of only 36.8 +/- 10.9% (P < 0. 001), with comparable reversal of the ceruloplasmin-mediated inhibition of MPO activity. Measurement of the affinity of the interactions demonstrated that binding between MPO and the anti-MPO antibodies is stronger than that between MPO and ceruloplasmin (1.61 x 107 to 1.33 x 108 vs. 7.46 x 106 m-1), indicating that binding to the autoantibody would be favored in vivo. CONCLUSIONS: This study confirms a role for ceruloplasmin as a physiological inhibitor of MPO, and demonstrates how the inhibition may be disrupted in the presence of anti-MPO antibodies. Because a majority (16 of 21) of the antibodies did not themselves inhibit MPO activity, their interference with the inhibition mediated by ceruloplasmin may be brought about by steric hindrance consequent upon the binding of the antibody to a dominant epitope at or near the active site.  (+info)

Ferroxidase activity of ferritin: effects of pH, buffer and Fe(II) and Fe(III) concentrations on Fe(II) autoxidation and ferroxidation. (2/796)

It is widely accepted that iron deposition in the iron storage protein ferritin in vitro involves Fe(II) oxidation, and that ferritin facilitates this oxidation at a ferroxidase site on the protein. However, these views have recently been questioned, with the protein ferroxidase activity instead being attributed to autoxidation from the buffer alone. Ligand exchange between another protein with ferroxidase activity and ferritin has been proposed as an alternative mechanism for iron incorporation into ferritin. In the present work, a pH stat apparatus is used to eliminate the influence of buffers on iron(II) oxidation. Here we show that the recent experiments questioning the ferroxidase activity of ferritin were flawed by inadequate pH control, that buffers actually retard rather than facilitate iron(II) oxidation, and that horse spleen ferritin has ferroxidase activity when measured under proper experimental conditions. Furthermore, high pH (7.0), a high Fe(II) concentration and the presence of Fe(III) all favour Fe(II) autoxidation in the presence or absence of ferritin.  (+info)

Copper metabolism in retinitis pigmentosa. (3/796)

Clinically and electrophysiologically confirmed cases of primary retinitis pigmentosa have been investigated regarding their copper metabolic state. It is observed that these patients show a normal or near normal serum copper concentration, very low plasma caeruloplasmin concentration, and a very high copper urinary excretion. A similarity between this condition and hepatolenticular degeneration is drawn and it is suggested that retinitis pigmentosa may also be a condition caused by an inborn error of copper metabolism.  (+info)

Caeruloplasmin isoforms in Wilson's disease in neonates. (4/796)

AIM: To investigate the neonatal diagnosis of Wilson's disease from caeruloplasmin isoforms in cord blood. METHODS: Serum caeruloplasmin isoforms were measured in 5-10 ml cord blood from 10 fresh umbilical cords using sodium dodecyl polyacrylamide gel electrophoresis (SDS PAGE) and western blotting and analysed by densitometry. Total caeruloplasmin concentrations were determined by nephelometry and caeruloplasmin oxidase by p-nitrophenyldiamine. RESULTS: Although total caeruloplasmin concentrations are reduced in neonates, the plasma isoform was significantly reduced or absent in patients with Wilson's disease. Sera from healthy neonates and from those with Wilson's disease had reduced biliary isoforms. CONCLUSION: Identification of caeruloplasmin isoforms may be a marker for Wilson's disease in neonates.  (+info)

The reactions of copper proteins with nitric oxide. (5/796)

Nitric oxide (NO) can act as a ligand for copper atoms and may also engage in redox chemistry with the metal once bound. Furthermore NO posses an unpaired electron which can couple with the unpaired electron on Cu2+. These properties have been exploited to probe the active sites of copper-containing enzymes and proteins. We review these studies. In addition to the use as a spectroscopic probe for the active site we draw attention to the rapid reactions of NO at the copper sites in Cytochrome c oxidase (CcO) and laccase. These reactions in CcO occur in the ms time range, at low NO concentrations and in the presence of oxygen and may therefore be of physiological relevance to the control of respiration. Finally we speculate on the wider role that NO may play in regulation of an important group of Type 2 copper containing enzymes.  (+info)

Abnormality in urinary protein excretion in Japanese men with impaired glucose tolerance. (6/796)

OBJECTIVE: To examine whether subjects with impaired glucose tolerance (IGT) for more than 2 years have any abnormality in the kidney. RESEARCH DESIGN AND METHODS: We measured urinary excretion rate and clearance of various plasma proteins with different molecular radii and different isoelectric points in 22 Japanese men with IGT (IGT group) and 37 age-matched healthy control subjects (control group). RESULTS: Clearance of ceruloplasmin (molecular radius approximately 45 A; isoelectric point 4.4), IgG4 (molecular radius 55 A; isoelectric point 5.4), and IgG (molecular radius 55 A; isoelectric point 7.4) was significantly higher in the IGT group than in the control group, whereas there were no significant differences in urinary excretion rate of albumin (molecular radius 36 A; isoelectric points 4.8-5.2) and clearance of alpha 2-macroglobulin (molecular radius 88 A; isoelectric point 5.4) between the two groups. CONCLUSIONS: In the present study, we found that clearance of neutral-charged IgG, negatively charged IgG4, and ceruloplasmin with molecular radii of approximately 45-55 A was selectively increased in IGT subjects. This finding does not seem to be explained by impairment of charge and pore-size selectivity in the glomerulus. Therefore, considering the present result together with our recent finding that enhanced glomerular filtration rate (GFR) after acute protein loading in healthy subjects induced a selective increase in clearance of IgG, IgG4, and ceruloplasmin, we suggest that increased intraglomerular hydraulic pressure, although enhanced GFR was not demonstrated, may be at work in these mildly hyperglycemic subjects.  (+info)

Hepatic hyperplasia and cancer in rats: alterations in copper metabolism. (7/796)

We previously demonstrated that rats exposed to the peroxisome proliferator (PP) diethylhexylphthalate (DEHP) had reduced serum ceruloplasmin (CP) oxidase activity, which suggests tissue copper deposition. Copper is highly toxic in excess, and results in cellular damage and hepatocellular carcinomas (HCC). This study addresses changes in expression of copper-related genes and metal accumulation in hyperplastic liver and tumors induced by PP. Male rats were fed diets containing DEHP or clofibrate (CLF) for 3-60 days (hyperplasia) and 4-chloro-6-(2,3 xylidino)-2-pyrimidinyl-thio(N-beta-hydroxyethyl) acetamide for 10 months (HCC). During hyperplasia, an immediate and progressive decrease in serum CP activity was observed (P < 0.05), as were reductions in mRNA levels for both CP and Wilson's disease gene (WD gene, a P-type ATPase) (P < 0.05). Tumor-bearing rats had lower serum CP activity (P < 0.05), and CP and WD gene mRNA levels were reduced in tumors (P < 0.05), and in liver surrounding tumors (SL) (P < 0.05). Metallothionein mRNA showed no consistent changes during hyperplasia. Tumors showed a 2.5-fold induction of metallothionein mRNA (P < 0.05), and a 1.2-fold increase in SL. Temporal increases in liver copper content occurred during hyperplasia, with increases of 2-fold (DEHP) and 3.3-fold (CLF) at 60 days (P < 0.05). Copper content was 2.2-fold higher in tumors (P < 0.05) and 1.7-fold higher in SL; iron did not increase and zinc decreased temporally. Thus, copper accumulation and changes in copper-related gene expression may be contributing factors in liver neoplasia in PP-treated rats. Loss of CP results in decreased free radical scavenger capacity and thus may enhance oxidative damage induced by PPs.  (+info)

Hemolytic activity of copper sulfate as influenced by epinephrine and chelating thiols. (8/796)

AIM: To study the effects of epinephrine, homocysteine, and other complexing agents on the cytotoxicity of copper sulfate. METHODS: In vitro suspensions of human red cells incubated with cupric sulfate were used, and hemolysis was determined by extracellular hemoglobin. RESULTS: The hemolytic activity of CuSO4 (0.3 mmol.L-1) was enhanced by the presence of epinephrine and to a lesser extent by homocysteine, whereas D-penicillamine, succimer, and mercaptodextran reduced the copper-induced hemolysis. The latter 3 chelating thiols also reduced the copper-epinephrine-induced hemolysis. The plasma protein ceruloplasmin reduced markedly the copper-epinephrine-induced hemolysis, even upon concentrations < 20% of that of copper. Chromic chloride, as well, acted anti-hemolytically. CONCLUSION: The latter protectors may interact with the production or activity of toxic oxygen, while classical copper chelators sequester cupric ions from interaction with epinephrine or homocysteine.  (+info)

Ceruloplasmin is a protein found in blood plasma that binds and transports copper ions. It plays a crucial role in copper metabolism, including the oxidation of ferrous iron to ferric iron, which is necessary for the incorporation of iron into transferrin, another protein responsible for transporting iron throughout the body. Ceruloplasmin also acts as an antioxidant by scavenging free radicals and has been implicated in neurodegenerative disorders like Alzheimer's disease and Wilson's disease, a genetic disorder characterized by abnormal copper accumulation in various organs.

Copper is a chemical element with the symbol Cu (from Latin: *cuprum*) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. Copper is found as a free element in nature, and it is also a constituent of many minerals such as chalcopyrite and bornite.

In the human body, copper is an essential trace element that plays a role in various physiological processes, including iron metabolism, energy production, antioxidant defense, and connective tissue synthesis. Copper is found in a variety of foods, such as shellfish, nuts, seeds, whole grains, and organ meats. The recommended daily intake of copper for adults is 900 micrograms (mcg) per day.

Copper deficiency can lead to anemia, neutropenia, impaired immune function, and abnormal bone development. Copper toxicity, on the other hand, can cause nausea, vomiting, abdominal pain, diarrhea, and in severe cases, liver damage and neurological symptoms. Therefore, it is important to maintain a balanced copper intake through diet and supplements if necessary.

Hepatolenticular degeneration, also known as Wilson's disease, is a rare genetic disorder of copper metabolism. It is characterized by the accumulation of copper in various organs, particularly the liver and brain. This leads to progressive damage and impairment of their functions.

The medical definition of Hepatolenticular degeneration (Wilson's disease) is:

A genetic disorder caused by a mutation in the ATP7B gene, resulting in impaired biliary excretion of copper and its accumulation within hepatocytes. This causes liver damage, which can manifest as acute hepatitis, cirrhosis, or fulminant hepatic failure. Additionally, excess copper is released into the bloodstream and deposited in various tissues, including the basal ganglia of the brain, leading to neurological symptoms such as tremors, rigidity, dysarthria, and behavioral changes. Other features include Kayser-Fleischer rings (copper deposition in the cornea), splenomegaly, and hemolytic anemia. Early diagnosis and treatment with copper-chelating agents can significantly improve outcomes and prevent complications.

Iron metabolism disorders are a group of medical conditions that affect the body's ability to absorb, transport, store, or utilize iron properly. Iron is an essential nutrient that plays a crucial role in various bodily functions, including oxygen transportation and energy production. However, imbalances in iron levels can lead to several health issues.

There are two main types of iron metabolism disorders:

1. Iron deficiency anemia (IDA): This condition occurs when the body lacks adequate iron to produce sufficient amounts of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. Causes of IDA may include inadequate dietary iron intake, blood loss, or impaired iron absorption due to conditions like celiac disease or inflammatory bowel disease.
2. Hemochromatosis: This is a genetic disorder characterized by excessive absorption and accumulation of iron in various organs, including the liver, heart, and pancreas. Over time, this excess iron can lead to organ damage and diseases such as cirrhosis, heart failure, diabetes, and arthritis. Hemochromatosis is typically caused by mutations in the HFE gene, which regulates iron absorption in the intestines.

Other iron metabolism disorders include:

* Anemia of chronic disease (ACD): A type of anemia that occurs in individuals with chronic inflammation or infection, where iron is not efficiently used for hemoglobin production due to altered regulation.
* Sideroblastic anemias: These are rare disorders characterized by the abnormal formation of ringed sideroblasts (immature red blood cells containing iron-laden mitochondria) in the bone marrow, leading to anemia and other symptoms.
* Iron-refractory iron deficiency anemia (IRIDA): A rare inherited disorder caused by mutations in the TMPRSS6 gene, resulting in impaired regulation of hepcidin, a hormone that controls iron absorption and distribution in the body. This leads to both iron deficiency and iron overload.

Proper diagnosis and management of iron metabolism disorders are essential to prevent complications and maintain overall health. Treatment options may include dietary modifications, iron supplementation, phlebotomy (bloodletting), or chelation therapy, depending on the specific disorder and its severity.

Inborn errors of metal metabolism refer to genetic disorders that affect the way the body processes and handles certain metallic elements. These disorders can result in an accumulation or deficiency of specific metals, leading to various clinical manifestations. Examples of such conditions include:

1. Wilson's disease: An autosomal recessive disorder caused by a mutation in the ATP7B gene, which results in abnormal copper metabolism and accumulation in various organs, particularly the liver and brain.
2. Menkes disease: An X-linked recessive disorder caused by a mutation in the ATP7A gene, leading to impaired copper transport and deficiency, affecting the brain, bones, and connective tissue.
3. Hemochromatosis: An autosomal recessive disorder characterized by excessive iron absorption and deposition in various organs, causing damage to the liver, heart, and pancreas.
4. Acrodermatitis enteropathica: A rare autosomal recessive disorder caused by a mutation in the SLC39A4 gene, resulting in zinc deficiency and affecting the skin, gastrointestinal system, and immune function.
5. Disturbances in manganese metabolism: Rare genetic disorders that can lead to either manganese accumulation or deficiency, causing neurological symptoms.

These conditions often require specialized medical management, including dietary modifications, chelation therapy, and/or supplementation to maintain appropriate metal homeostasis and prevent organ damage.

In the context of medicine, iron is an essential micromineral and key component of various proteins and enzymes. It plays a crucial role in oxygen transport, DNA synthesis, and energy production within the body. Iron exists in two main forms: heme and non-heme. Heme iron is derived from hemoglobin and myoglobin in animal products, while non-heme iron comes from plant sources and supplements.

The recommended daily allowance (RDA) for iron varies depending on age, sex, and life stage:

* For men aged 19-50 years, the RDA is 8 mg/day
* For women aged 19-50 years, the RDA is 18 mg/day
* During pregnancy, the RDA increases to 27 mg/day
* During lactation, the RDA for breastfeeding mothers is 9 mg/day

Iron deficiency can lead to anemia, characterized by fatigue, weakness, and shortness of breath. Excessive iron intake may result in iron overload, causing damage to organs such as the liver and heart. Balanced iron levels are essential for maintaining optimal health.

Transferrin is a glycoprotein that plays a crucial role in the transport and homeostasis of iron in the body. It's produced mainly in the liver and has the ability to bind two ferric (Fe3+) ions in its N-lobe and C-lobe, thus creating transferrin saturation.

This protein is essential for delivering iron to cells while preventing the harmful effects of free iron, which can catalyze the formation of reactive oxygen species through Fenton reactions. Transferrin interacts with specific transferrin receptors on the surface of cells, particularly in erythroid precursors and brain endothelial cells, to facilitate iron uptake via receptor-mediated endocytosis.

In addition to its role in iron transport, transferrin also has antimicrobial properties due to its ability to sequester free iron, making it less available for bacterial growth and survival. Transferrin levels can be used as a clinical marker of iron status, with decreased levels indicating iron deficiency anemia and increased levels potentially signaling inflammation or liver disease.

Lymphangiectasis is a medical condition characterized by the dilation and abnormal expansion of lymphatic vessels, which are responsible for transporting lymph fluid throughout the body. These dilated lymphatic vessels can be found in various tissues and organs, including the intestines, lungs, or other parts of the body.

In the case of intestinal lymphangiectasis (also known as Waldmann's disease), the lymphatic vessels in the small intestine become enlarged, leading to impaired absorption of nutrients and lymph fluid. This can result in protein-losing enteropathy, malnutrition, diarrhea, and edema (swelling) due to the loss of proteins and lymphatic fluids into the gastrointestinal tract.

Pulmonary lymphangiectasis is a rare congenital disorder where the lymphatic vessels in the lungs are abnormally developed and dilated, causing respiratory distress, recurrent lung infections, and chylous effusions (accumulation of milky lymph fluid in the pleural space surrounding the lungs).

Treatment for lymphangiectasis depends on the underlying cause and severity of the condition. It may involve dietary modifications, medications to manage symptoms, or surgical interventions in some cases.

Deficiency diseases are a group of medical conditions that occur when an individual's diet lacks essential nutrients, such as vitamins and minerals. These diseases develop because the body needs these nutrients to function correctly, and without them, various bodily functions can become impaired, leading to disease.

Deficiency diseases can manifest in many different ways, depending on which nutrient is lacking. For example:

* Vitamin A deficiency can lead to night blindness and increased susceptibility to infectious diseases.
* Vitamin C deficiency can result in scurvy, a condition characterized by fatigue, swollen gums, joint pain, and anemia.
* Vitamin D deficiency can cause rickets in children, a disease that leads to weakened bones and skeletal deformities.
* Iron deficiency can result in anemia, a condition in which the blood lacks adequate healthy red blood cells.

Preventing deficiency diseases involves eating a balanced diet that includes a variety of foods from all the major food groups. In some cases, supplements may be necessary to ensure adequate nutrient intake, especially for individuals who have restricted diets or medical conditions that affect nutrient absorption.

Turpentine, also known as oil of turpentine, is not a medical term itself but a substance that has been used in some traditional medical preparations. It is a volatile essential oil obtained by the distillation of resin from live trees, mainly pines.

Medically, it has been used as a counterirritant and rubefacient (a substance that causes redness of the skin and increases blood flow) in liniments and plasters. However, its use in modern medicine is not very common due to potential toxicity and irritation. It's important to note that turpentine should not be ingested or used topically without proper medical supervision.

Anserine is a type of protein that belongs to the family of muscle proteins called myofibrillar proteins. It is found in high concentrations in the muscles of birds, especially in the breast muscle, and is also present in the muscles of some mammals, including humans. Anserine is composed of three peptide chains: two actin molecules and one tropomyosin molecule. It plays a role in the contraction and relaxation of muscles, and has been studied for its potential role in muscle function and disease. In humans, anserine is found primarily in type II (fast-twitch) muscle fibers, which are responsible for powerful, quick movements.

Haptoglobins are proteins found in the blood that bind to free hemoglobin, which is released when red blood cells break down. The resulting complex is then removed from the bloodstream by the liver, preventing the loss of iron and potential kidney damage caused by the breakdown products of hemoglobin. Haptoglobins are produced in the liver and their levels can be measured to help diagnose various medical conditions such as hemolytic anemia, liver disease, and inflammation.

Cation transport proteins are a type of membrane protein that facilitate the movement of cations (positively charged ions) across biological membranes. These proteins play a crucial role in maintaining ion balance and electrical excitability within cells, as well as in various physiological processes such as nutrient uptake, waste elimination, and signal transduction.

There are several types of cation transport proteins, including:

1. Ion channels: These are specialized protein structures that form a pore or channel through the membrane, allowing ions to pass through rapidly and selectively. They can be either voltage-gated or ligand-gated, meaning they open in response to changes in electrical potential or binding of specific molecules, respectively.

2. Ion pumps: These are active transport proteins that use energy from ATP hydrolysis to move ions against their electrochemical gradient, effectively pumping them from one side of the membrane to the other. Examples include the sodium-potassium pump (Na+/K+-ATPase) and calcium pumps (Ca2+ ATPase).

3. Ion exchangers: These are antiporter proteins that facilitate the exchange of one ion for another across the membrane, maintaining electroneutrality. For example, the sodium-proton exchanger (NHE) moves a proton into the cell in exchange for a sodium ion being moved out.

4. Symporters: These are cotransporter proteins that move two or more ions together in the same direction, often coupled with the transport of a solute molecule. An example is the sodium-glucose cotransporter (SGLT), which facilitates glucose uptake into cells by coupling its movement with that of sodium ions.

Collectively, cation transport proteins help maintain ion homeostasis and contribute to various cellular functions, including electrical signaling, enzyme regulation, and metabolic processes. Dysfunction in these proteins can lead to a range of diseases, such as neurological disorders, cardiovascular disease, and kidney dysfunction.

Apoproteins are the protein components of lipoprotein complexes, which are responsible for transporting fat molecules, such as cholesterol and triglycerides, throughout the body. Apoproteins play a crucial role in the metabolism of lipids by acting as recognition signals that allow lipoproteins to interact with specific receptors on cell surfaces.

There are several different types of apoproteins, each with distinct functions. For example, apolipoprotein A-1 (apoA-1) is the major protein component of high-density lipoproteins (HDL), which are responsible for transporting excess cholesterol from tissues to the liver for excretion. Apolipoprotein B (apoB) is a large apoprotein found in low-density lipoproteins (LDL), very low-density lipoproteins (VLDL), and lipoprotein(a). ApoB plays a critical role in the assembly and secretion of VLDL from the liver, and it also mediates the uptake of LDL by cells.

Abnormalities in apoprotein levels or function can contribute to the development of various diseases, including cardiovascular disease, diabetes, and Alzheimer's disease. Therefore, measuring apoprotein levels in the blood can provide valuable information for diagnosing and monitoring these conditions.

Copper sulfate is an inorganic compound with the chemical formula CuSO₄. It is a common salt of copper and is often found as a blue crystalline powder. Copper sulfate is used in various applications, including as a fungicide, algicide, and in some industrial processes.

In medical terms, copper sulfate has been historically used as an emetic (a substance that causes vomiting) to treat poisoning. However, its use for this purpose is not common in modern medicine due to the availability of safer and more effective emetics. Copper sulfate can be harmful or fatal if swallowed, and it can cause burns and irritation to the skin and eyes. Therefore, it should be handled with care and kept out of reach of children and pets.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Macroglobulins are high molecular weight immunoglobulins, specifically, IgM antibodies. They are called "macro" because of their large size, which is approximately 10 times larger than other types of immunoglobulins (IgG, IgA, and IgD). Macroglobulins are normally present in low concentrations in the blood, but their levels can increase in certain medical conditions such as macroglobulinemia, lymphoma, multiple myeloma, and other chronic inflammatory diseases.

Elevated levels of macroglobulins can cause various symptoms, including fatigue, weakness, bleeding, and neurological problems due to the increased viscosity of the blood. Macroglobulins can also interfere with laboratory tests, leading to false positive results for certain conditions. Treatment for elevated macroglobulins depends on the underlying cause and may include chemotherapy, radiation therapy, or other targeted therapies.

... (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene. Ceruloplasmin is the major ... Ceruloplasmin can be measured by means of a blood test; this can be done using immunoassays . The sample is spun and separated ... Ceruloplasmin is a relatively large enzyme (~10nm); the larger size prevents the bound copper from being lost in a person's ... Ceruloplasmin (CP) is an enzyme (EC 1.16.3.1) synthesized in the liver containing 6 atoms of copper in its structure. ...
Ceruloplasmin metabolism and function. Annual review of nutrition, 22(1), pp.439-458. Løvstad, R.A., 2004. A kinetic study on ...
No totally reliable test for Wilson's disease is known, but levels of ceruloplasmin and copper in the blood, as well of the ... Copper accumulates in the liver tissue; ceruloplasmin is still secreted, but in a form that lacks copper (termed apo- ... The liver also releases copper into the bloodstream that is not bound to ceruloplasmin. This free copper precipitates ... ceruloplasmin) and is rapidly degraded in the bloodstream. When the amount of copper in the liver overwhelms the proteins that ...
Hickman J, Ashwell G, Morell AG, van den Hamer CJ, Scheinberg IH (1970). "Physical and chemical studies on ceruloplasmin. 8. ... Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin". J. Biol. Chem. 245 (4): 759-66. PMID 4313609. Paulson JC, ...
Ceruloplasmin also oxidizes iron from its ferrous state to the ferric form that is required for iron binding. Impairment in ... Low levels of copper and ceruloplasmin in the serum are consistent with the diagnosis as is a low 24 hour urine copper level. ... Another iron transporting enzyme is ceruloplasmin. This enzyme is required to mobilize iron from the reticuloendothelial cell ... ceruloplasmin, Cu/Zn superoxide dismutase, and in amine oxidases. These enzyme catalyze reactions for oxidative phosphorylation ...
α2 - haptoglobin, α2-macroglobulin, α2-antiplasmin, ceruloplasmin. The beta (β) band - transferrin, LDL, complement The gamma ( ...
... s include: Ceruloplasmin EC 1.16.3.1 (ferroxidase), a 6-domain enzyme found in the serum of mammals and ... Messerschmidt A, Huber R (January 1990). "The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and ...
The effects of estradiol undecylate on serum lipids and ceruloplasmin levels have been studied as well. Additionally, the ... Götz H, Ehrmeier H (June 1971). "[Estrogens and ceruloplasmine level]" [Estrogens and ceruloplasmin levels]. Archiv für ...
Martin, G. M.; Derr, M. A.; Benditt, E. P. (March 1964). "Ceruloplasmins of Several Animal Species. Comparison of ...
Green color can be due to ceruloplasmin or sulfhemoglobin. The latter may form due to medicines that are able to form ...
Wolf T. L.; Kotun J.; Meador-Woodruff J. H. (2006). "Plasma copper, iron, ceruloplasmin and ferroxidase activity in ...
Ceruloplasmin is also an acute-phase protein produced by monocytes, and its plasma concentration can double during multiple ... Mazumder B, Sampath P, Fox PL (2005). "Regulation of macrophage ceruloplasmin gene expression: one paradigm of 3'-UTR-mediated ... Mazumder B, Sampath P, Fox PL (2006). "Translational control of ceruloplasmin gene expression: beyond the IRE". Biol Res. 39 (1 ... UTR of the ceruloplasmin (Cp) mRNA. The GAIT element forms a stem-loop secondary structure. The GAIT element is involved in ...
While deficiency in hephaestin or ceruloplasmin alone do not seem to cause iron buildup in the retina, studies done on murine ... Human iron metabolism Ceruloplasmin GRCh38: Ensembl release 89: ENSG00000089472 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... While the structure and kinetic activity of ceruloplasmin have been studied extensively, hephaestin has yet to be investigated ... While hephaestin shares 50% amino acid sequence identity with its serum homologue ceruloplasmin, the hephaestin protein ...
... a ceruloplasmin-like protein which is immunologically similar to serum ceruloplasmin. The occluding junctions of Sertoli cells ... Skinner MK, Griswold MD (June 1983). "Sertoli cells synthesize and secrete a ceruloplasmin-like protein". Biology of ... a blood plasma protein for iron ion delivery testicular ceruloplasmin, ...
... which involves the protein ceruloplasmin, carrying the majority of copper in blood. Ceruloplasmin also carries the copper that ... Severe deficiency can be found by testing for low plasma or serum copper levels, low ceruloplasmin, and low red blood cell ... S.S. Percival; Harris, E.D. (1 January 1990). "Copper transport from ceruloplasmin: Characterization of the cellular uptake ... Frieden, E.; Hsieh, H.S. (1976). Ceruloplasmin: The copper transport protein with essential oxidase activity. Advances in ...
Ceruloplasmin is an acute phase protein synthesized in the liver. It is the carrier of the copper ion. Its level is increased ... In Wilson disease, the ceruloplasmin level is depressed which lead to copper accumulation in body tissues. Alpha-fetoprotein ( ...
Ceruloplasmin is the major copper-carrying protein in the blood. Ceruloplasmin exhibits oxidase activity, which is associated ...
Osaki S (November 1966). "Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin)". J. Biol ... Ceruloplasmin FTH1 - Ferritin heavy chain FTMT - Ferritin, mitochondrial HEPH - Hephaestin Cox JC, Boxer DH (1986). "The role ...
The α2 region is mostly haptoglobin, α2-macroglobulin, α2-antiplasmin, and ceruloplasmin. The β band consists of transferrin, ...
The majority of blood copper (or serum copper) is bound to ceruloplasmin. The proportion of ceruloplasmin-bound copper can ... Most of the copper (70 - 95%) excreted by the liver is incorporated into ceruloplasmin, the main copper carrier in blood. ... Copper is transported to extra-hepatic tissues by ceruloplasmin, albumin and amino acids, or excreted into the bile. By ... Fortunately, copper deficiency can be confirmed by very low serum metal and ceruloplasmin concentrations in the blood. Other ...
Ceruloplasmin helps move iron from the organs and tissues of the body and prepares it for incorporation into a molecule called ... When ceruloplasmin is unavailable, transport of iron out of the body's tissues is impaired. The resulting iron accumulation ... The CP gene mutation results in the production of ceruloplasmin protein that is unstable or nonfunctional by altering the open ... Diagnosis of this disorder depends on blood tests demonstrating the absence of serum ceruloplasmin, combined with low serum ...
"Considerations about the possible function of ceruloplasmin in influenza and parainfluenza virus infection". www. ...
"Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somatic Cell and Molecular ...
"Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somatic Cell and Molecular ...
Special reference to metallothionein and ceruloplasmin". Physiological Reviews. 65 (2): 238-309. doi:10.1152/physrev.1985.65. ...
... ceruloplasmin, serum amyloid A and haptoglobin. Others give negative feedback on the inflammatory response, e.g. serpins. Alpha ...
ClC-4 promotes copper incorporation into ceruloplasmin". Gastroenterology. 126 (4): 1157-66. doi:10.1053/j.gastro.2004.01.015. ...
... ceruloplasmin), optimal functions of the erythrocyte membrane. Ceruloplasmin (copper containing protein) is required for normal ...
... ceruloplasmin, transferrin, complement, and glycoproteins. Hepatocytes manufacture their own structural proteins and ...
"Physical and Chemical Studies on Ceruloplasmin: V. METABOLIC STUDIES ON SIALIC ACID-FREE CERULOPLASMIN IN VIVO". Journal of ... The researchers transferred radioactively-labeled ceruloplasmin that had undergone a reaction via the enzyme neuraminidase to ...
Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene. Ceruloplasmin is the major ... Ceruloplasmin can be measured by means of a blood test; this can be done using immunoassays . The sample is spun and separated ... Ceruloplasmin is a relatively large enzyme (~10nm); the larger size prevents the bound copper from being lost in a persons ... Ceruloplasmin (CP) is an enzyme (EC 1.16.3.1) synthesized in the liver containing 6 atoms of copper in its structure. ...
The ceruloplasmin test measures the level of the copper-containing protein ceruloplasmin in the blood. ... The ceruloplasmin test measures the level of the copper-containing protein ceruloplasmin in the blood. ... Ceruloplasmin is made in the liver. Ceruloplasmin stores and transports copper in the blood to parts of the body that need it. ... The ceruloplasmin test measures the level of the copper-containing protein ceruloplasmin in the blood. ...
Ceruloplasmin is an α2-globulin containing copper. About 70% or more of total serum copper is associated with ceruloplasmin, 7 ... Ceruloplasmin is high in a variety of neoplastic and inflammatory states, since it behaves as an acute phase reactant, although ... Ceruloplasmin is low in Menkes kinky hair syndrome (In Menkes syndrome the defect is secondary to poor absorption and ... A normal ceruloplasmin does not rule out Wilsons disease. Serum copper should be measured in addition. ...
ceruloplasmin. Names. cuproxidase ceruloplasmin. ferroxidase. ferroxidase ceruloplasmin. NP_001263177.1. *EC 1.16.3.1 ... CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin. cd04225. Location:726 → 896. CuRO_5_ceruloplasmin; The ... CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin. cd11022. Location:569 → 712. CuRO_4_ceruloplasmin; The ... CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin. cd04225. Location:726 → 896. CuRO_5_ceruloplasmin; The ...
Serum Ceruloplasmin or Slit-Lamp Examination. Serum ceruloplasmin or slit lamp examination for Kayser-Fleischer rings might be ...
Labshub completely concentrates on constant progress and monitoring ensures that we can deliver all assistance at a consistently high-quality level, via our disciplined and automated processes, which is why we are here 24/7 and 365 days for your services. ...
Confusing the word Copper with the word Ceruloplasmin... What do I mean by that? Ok...So...Ceruloplasmin & Copper are OPPOSITES ... They oppose each other... High ceruloplasmin means low Copper, & ... If we were to use serum Ceruloplasmin as a diagnostic marker ... Copper is LOW during Cancer, Ceruloplasmin is HIGH!!! (Watch your step!!!). *Copper is low in cancer, ceruloplasmin is high in ... When you do a search for foods containing Copper, you may see the word Liver…UHUH…NOOoooo…Liver is high in Ceruloplasmin, not ...
2143 QUANTITATIVE PROTEOMICS IDENTIFIES CERULOPLASMIN AS A POTENTIAL PROMOTER OF UROLITHIASIS Wright C., Howles S., Trudgian D ...
Serum Ceruloplasmin. Serum ceruloplasmin levels are low in newborns and gradually rise within the first 2 years of life. ... Ceruloplasmin levels may also be decreased in 10-20% of Wilson Disease gene heterozygotes, who do not develop Wilson disease ... The presence of Kayser-Fleischer rings and ceruloplasmin levels of less than 20 mg/dL in a patient with neurologic signs or ... Falsely low ceruloplasmin levels may be observed in any protein deficiency state, including nephrotic syndrome, malabsorption, ...
Ceruloplasmin • Ferritin alpha 1 antitrypsin ...
Ceruloplasmin and cardiovascular disease. Fox PL, Mazumder B, Ehrenwald E, Mukhopadhyay CK. Fox PL, et al. Among authors: ...
indirect copper assay, ceruloplasmin. Regulation Description. Ceruloplasmin immunological test system.. Regulation Medical ...
Ceruloplasmin, mg/dL. 32.5 (20.0-60.0). Creatine kinase, U/L. 39-257 (0.6-1.3). ...
ceruloplasmin 2.0245 5.12E-06 4582 MUC1 mucin 1, cell surface associated 1.8852 1.33E-05 ...
The membrane protein hephaestin and the plasma protein ceruloplasmin (Cp) oxidize cellular Fe2+ into Fe3+ [2]. Ceruloplasmin is ... known as ceruloplasmin, to allow loading onto the Tf. Ceruloplasmin is a copper-dependent ferroxidase, a major protein of ... known as ceruloplasmin, to allow loading onto the Tf. Ceruloplasmin is a copper-dependent ferroxidase, a major protein of ... Linder, M.C. Ceruloplasmin and other copper binding components of blood plasma and their functions: An update. Metallomics 2016 ...
Age and Serum Creatinine Can Differentiate Wilson Disease Patients with Pseudonormal Ceruloplasmin. March 02, 2023 ...
2008). Ceruloplasmin/hephaestin knockout mice model morphologic and molecular features of AMD. Invest. Ophthalmol. Vis. Sci. 49 ... 2016). Hephaestin and ceruloplasmin facilitate iron metabolism in the mouse kidney. Sci. Rep. 6:39470. doi: 10.1038/srep39470 ... 1999). Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet ... 2013). Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease. Ann. Neurol. 73, 554-559. doi: 10.1002/ana. ...
Ceruloplasmin. 5.57e-4. VAT1. Vesicle amine transport 1. 8.63e-4. ...
Ceruloplasmin. polyclonal. Rabbit. human. unconjugated. 100ug. n/a. AMPERSAND BIOSCIENCES More Info ...
... such as ceruloplasmin and haptoglobin, increases during such reactions. Moderate and isolated increases occur when glomerular ...
Serum ceruloplasmin concentrations were also depressed by cadmium. Serum amylase concentrations were not significantly affected ... Cadmium feeding had a similar effect on serum copper and ceruloplasmin concentrations in male and female rats. ... and ceruloplasmin was studied in male rats fed a semipurified diet. Drinking water was supplemented with 2.5, 5, or 10 parts ...
The ceruloplasmin and hydrogen peroxide system induces alpha-synuclein aggregation in vitro. Biochimie. 2002;84(7):625-31. ... Carnosine and related dipeptides protect human ceruloplasmin against peroxyl radical-mediated modification. Mol Cells. 2002;13( ... Protection by carnosine-related dipeptides against hydrogen peroxidemediated ceruloplasmin modification. Mol Cells. 2002 a.;13( ...
Other plasma proteins may be increased (angiotensinogen/renin substrate, alpha-1-antitrypsin, ceruloplasmin). ...
Memisogullari, R. and Bakan, E. (2004). Levels of Ceruloplasmin, Transferrin, and Lipid Peroxidation in the Serum of Patients ...
V. Metabolic studies on sialic acid-free ceruloplasmin in vivo. J Biol Chem 243: 155-159, 1968. 2. Ashwell G, Morell AG. The ... REFERENCES 1. Morell AG, Irvine RA, Sternlieb I, Scheunberg IH, Ashwell G. Physical and chemical studies on ceruloplasmin. ...
... ceruloplasmin, complement C3, kininogen-1 (KNG1) isoform 2, myeloperoxidase (MPO), and inter-α-trypsin inhibitor heavy chain H4 ... ceruloplasmin, complement C3, KNG1 isoform 2, MPO, and ITIH4 was observed [83]. The overexpression of TFF2 was associated with ...
The BN ProSpec® System uses our proven nephelometric technology for the determination of a large variety of assays which support the management of disease states such as iron and anemia assessment, gammopathies / immune system, kidney disease, and many others. The BN ProSpec System is a fully automated benchtop analyzer which combines efficient workflow with cost-effective determinations for plasma protein testing needs:. ...
  • Serum ceruloplasmin or slit lamp examination for Kayser-Fleischer rings might be considered. (medscape.com)
  • If a patient is asymptomatic, exhibits isolated liver disease, and lacks corneal rings, the coexistence of a hepatic copper concentration of more than 250 mg/g of dry weight and a low serum ceruloplasmin level is sufficient to establish a diagnosis. (grovecanada.ca)
  • Serum ceruloplasmin levels are low in newborns and gradually rise within the first 2 years of life. (medscape.com)
  • Ceruloplasmin exhibits a copper-dependent oxidase activity, which is associated with possible oxidation of Fe2+ (ferrous iron) into Fe3+ (ferric iron), therefore assisting in its transport in the plasma in association with transferrin, which can carry iron only in the ferric state. (wikipedia.org)
  • All horses at the beginning of the competition (day 0) and on the last day of competition were subjected to collection of blood and SDS-polyacrylamide gel (SDS-PAGE) electrophoresis was used to measure APPs concentrations (albumin, ceruloplasmin, transferrin, haptoglobin, acid glycoprotein, immunoglobulin G, immunoglobulin A and a protein with molecular weight of 23 kDa). (scielo.br)
  • whereas, the serum level of other positive reactants, such as ceruloplasmin and haptoglobin, increases during such reactions. (cdc.gov)
  • 0.0001) in the serum concentrations of the ceruloplasmin, haptoglobin, acid glycoprotein, immunoglobulin A and protein with molecular weight of 23kDa. (scielo.br)
  • Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene. (wikipedia.org)
  • As a ferroxidase, ceruloplasmin (Cp) plays a key role in iron homeostasis and its abnormal activity leads to iron accumulation. (isogem.org)
  • Copper and ceruloplasmin, as acute phase reactants, are sensitive to inflammation. (stillmanwellness.com)
  • A cis-regulatory element called the GAIT element is involved in the selective translational silencing of the Ceruloplasmin transcript. (wikipedia.org)
  • WTX101 is an oral "first-in-class copper-protein-binding molecule that targets hepatic intracellular copper and reduces plasma non-ceruloplasmin-bound copper (NCC) by forming tripartite complexes with albumin and increasing biliary copper excretion," Dr. Karl Heinz Weiss from University Hospital Heidelberg in Germany and colleagues explain in their article. (medscape.com)
  • Menkes disease (Menkes kinky hair syndrome) (rare - UK incidence 1/100,000) Copper deficiency Aceruloplasminemia Zinc toxicity Greater-than-normal ceruloplasmin levels may indicate or be noticed in: copper toxicity / zinc deficiency pregnancy oral contraceptive pill use lymphoma acute and chronic inflammation (it is an acute-phase reactant) rheumatoid arthritis Angina Alzheimer's disease Schizophrenia Obsessive-compulsive disorder Normal blood concentration of ceruloplasmin in humans is 20-50 mg/dL. (wikipedia.org)
  • Cadmium feeding had a similar effect on serum copper and ceruloplasmin concentrations in male and female rats. (cdc.gov)
  • Ceruloplasmin (CP) is an enzyme (EC 1.16.3.1) synthesized in the liver containing 6 atoms of copper in its structure. (wikipedia.org)
  • Ceruloplasmin is made in the liver. (medlineplus.gov)
  • When you do a search for foods containing Copper, you may see the word Liver…UHUH…NOOoooo…Liver is high in Ceruloplasmin, not copper! (grovecanada.ca)
  • Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. (wikipedia.org)
  • Another protein, hephaestin, is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism. (wikipedia.org)
  • The ceruloplasmin test measures the level of the copper-containing protein ceruloplasmin in the blood. (medlineplus.gov)
  • Falsely low ceruloplasmin levels may be observed in any protein deficiency state, including nephrotic syndrome, malabsorption, protein-losing enteropathy, and malnutrition. (medscape.com)
  • Ceruloplasmin is an acute phase reactant and may be increased in response to hepatic inflammation, pregnancy, estrogen use, or infection. (medscape.com)
  • The effect of low concentration dietary cadmium (7440439) on hemoglobin, hematocrit and serum amylase, zinc (7440666), copper (7440508), and ceruloplasmin was studied in male rats fed a semipurified diet. (cdc.gov)
  • The molecular weight of human ceruloplasmin is reported to be 151kDa. (wikipedia.org)
  • Ceruloplasmin carries more than 95% of the total copper in healthy human plasma. (wikipedia.org)
  • Plasma ceruloplasmin was slightly elevated. (who.int)
  • Ceruloplasmin immunological test system. (fda.gov)
  • Mutations in the ceruloplasmin gene (CP), which are very rare, can lead to the genetic disease aceruloplasminemia, characterized by hyperferritinemia with iron overload. (wikipedia.org)
  • Ceruloplasmin stores and transports copper in the blood to parts of the body that need it. (medlineplus.gov)
  • Lower-than-normal ceruloplasmin levels may indicate the following: Wilson disease (a rare [UK incidence 2/100,000] copper storage disease). (wikipedia.org)
  • Normally, most of the copper in your blood is part of ceruloplasmin. (medlineplus.gov)
  • Blood antioxidant enzymes (superoxide dismutase, catalase, ceruloplasmin) were investigated in gestational ages and diseases. (msk.ru)
  • Concentration of metals, ceruloplasmin, metallothionein and the activity of N-acetyl-beta-D-glucosaminidase and gamma-glutamyltransferase in pregnant women who smoke and in those environmentally exposed to tobacco smoke and in their infants. (nih.gov)
  • The effect of low concentration dietary cadmium (7440439) on hemoglobin, hematocrit and serum amylase, zinc (7440666), copper (7440508), and ceruloplasmin was studied in male rats fed a semipurified diet. (cdc.gov)
  • whereas, the serum level of other positive reactants, such as ceruloplasmin and haptoglobin, increases during such reactions. (cdc.gov)
  • The presence of Kayser-Fleischer rings and ceruloplasmin levels of less than 20 mg/dL in a patient with neurologic signs or symptoms suggest a diagnosis of Wilson disease. (medscape.com)
  • A ceruloplasmin test measures the amount of ceruloplasmin in a sample of your blood. (medlineplus.gov)
  • Ceruloplasmin tests may also be used to help diagnose conditions that cause low levels of copper. (medlineplus.gov)
  • Ceruloplasmin tests are mostly used with tests that measure copper levels in blood and/or urine (pee). (medlineplus.gov)
  • Ceruloplasmin levels may also be decreased in 10%-20% of Wilson Disease gene heterozygotes, who do not develop Wilson disease and do not require treatment. (medscape.com)
  • Copper and ceruloplasmin levels may be normal in the milder variants and in the neonatal period. (medscape.com)
  • Ceruloplasmin levels are 6-12 mg/dL initially and only later are considered pathologically low. (medscape.com)
  • I have succeeded in lowering my ceruloplasmin from 37 to 10 mg/dL (normal is 18-36) during this time. (cancer.org)
  • So, ceruloplasmin testing can help diagnose conditions that involve having too much or too little copper in your body. (medlineplus.gov)
  • You need a prescription for TM to get from a reputable source, but I get mine from Bellevue Pharmacy in Missouri (1-800-728-0288) and it definitely works in getting your ceruloplasmin (measure of copper in body) down. (cancer.org)

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