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Monoclonal Gammopathy
Monoclonal gammopathy, also known as paraproteinemia, is the presence of excessive amounts of myeloma protein or monoclonal gamma globulin in the blood. It is usually due to an underlying immunoproliferative disorder or hematologic neoplasms, especially multiple myeloma. It is sometimes considered equivalent to plasma cell dyscrasia. The most common form of the disease is monoclonal gammopathy of undetermined significance. Causes Causes of paraproteinemia include the following: * Leukemias and lymphomas of various types, but usually B-cell non-Hodgkin lymphomas with a plasma cell component. ** Myeloma ** Plasmacytoma ** Lymphoplasmacytic lymphoma * Idiopathic (no discernible cause): some of these will be revealed as leukemias or lymphomas over the years. ** AL amyloidosis Diagnosis These are characterized by the presence of any abnormal protein that is involved in the immune system, which are most often immunoglobulins and are associated with the clonal proliferation of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serum Protein Electrophoresis
Serum protein electrophoresis (SPEP or SPE) is a laboratory test that examines specific proteins in the blood called globulins. The most common indications for a serum protein electrophoresis test are to diagnose or monitor multiple myeloma, a monoclonal gammopathy of uncertain significance (MGUS), or further investigate a discrepancy between a low albumin and a relatively high total protein. Unexplained bone pain, anemia, proteinuria, chronic kidney disease, and hypercalcemia are also signs of multiple myeloma, and indications for SPE. Blood must first be collected, usually into an airtight vial or syringe. Electrophoresis is a laboratory technique in which the blood serum (the fluid portion of the blood after the blood has clotted) is applied to either an acetate membrane soaked in a liquid buffer, or to a buffered agarose gel matrix, or into liquid in a capillary tube, and exposed to an electric current to separate the serum protein components into five major fract ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AL Amyloidosis
Amyloid light-chain (AL) amyloidosis, also known as primary amyloidosis, is the most common form of systemic amyloidosis. The disease is caused when a person's antibody-producing cells do not function properly and produce abnormal protein fibers made of components of antibodies called light chains. These light chains come together to form amyloid deposits which can cause serious damage to different organs. An abnormal light chain in urine is known as Bence Jones protein. Signs and symptoms AL amyloidosis can affect a wide range of organs, and consequently present with a range of symptoms. Non-specific symptoms may include fatigue and weight loss. The kidneys are commonly affected in systemic AL amyloidosis with 60–70% of people having kidney involvement. Symptoms of kidney disease and kidney failure can include fluid retention, swelling, and shortness of breath. Other manifestations of kidney involvement may include protein loss in the urine, low albumin levels in the blood an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bence Jones Protein
Bence Jones protein is a monoclonal globulin protein or immunoglobulin light chain found in the urine, with a molecular weight of 22–24 kDa. Detection of Bence Jones protein may be suggestive of multiple myeloma, or Waldenström's macroglobulinemia. Bence Jones proteins are particularly diagnostic of multiple myeloma in the context of target organ manifestations such as kidney failure, lytic (or "punched out") bone lesions, anemia, or large numbers of plasma cells in the bone marrow. Bence Jones proteins are present in 2/3 of multiple myeloma cases. The proteins are immunoglobulin light chains (paraproteins) and are produced by neoplastic plasma cells. They can be kappa (most of the time) or lambda. The light chains can be immunoglobulin fragments or single homogeneous immunoglobulins. They are found in urine as a result of decreased kidney filtration capabilities due to kidney failure, sometimes induced by hypercalcemia from the calcium released as the bones are destroyed ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Immunoglobulin Light Chain
] The immunoglobulin light chain is the small Peptide, polypeptide subunit of an antibody (immunoglobulin). A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains. In humans There are two types of light chain in humans: * kappa (κ) chain, encoded by the immunoglobulin kappa locus (IGK@) on chromosome 2 (locus: 2p11.2) * lambda (λ) chain, encoded by the immunoglobulin lambda locus (IGL@) on chromosome 22 (locus: 22q11.2) Antibodies are produced by B lymphocytes, each expressing only one class of light chain. Once set, light chain class remains fixed for the life of the B lymphocyte. In a healthy individual, the total kappa-to-lambda ratio is roughly 2:1 in serum (measuring intact whole antibodies) or 1:1.5 if measuring free light chains, with a highly divergent ratio indicative of neoplasm. The free light chain ratio ranges from 0.26 to 1.65. Both the kappa and the lambda chains can increase proportionately, maintaining a normal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Complement System
The complement system, also known as complement cascade, is a part of the humoral, innate immune system and enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promote inflammation, and attack the pathogen's cell membrane. Despite being part of the innate immune system, the complement system can be recruited and brought into action by antibodies generated by the adaptive immune system. The complement system consists of a number of small, inactive, liver synthesized protein precursors circulating in the blood. When stimulated by one of several triggers, proteases in the system cleave specific proteins to release cytokines and initiate an amplifying cascade of further cleavages. The end result of this ''complement activation'' or ''complement fixation'' cascade is stimulation of phagocytes to clear foreign and damaged material, inflammation to attract additional phagocytes, and activation of the cell-killi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Low-density Lipoproteins
Low-density lipoprotein (LDL) is one of the five major groups of lipoprotein that transport all fat molecules around the body in extracellular water. These groups, from least dense to most dense, are chylomicrons (aka ULDL by the overall density naming convention), very low-density lipoprotein (VLDL), intermediate-density lipoprotein (IDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL). LDL delivers fat molecules to cells. LDL has been associated with the progression of atherosclerosis. Overview Lipoproteins transfer lipids (fats) around the body in the extracellular fluid, making fats available to body cells for receptor-mediated endocytosis. Lipoproteins are complex particles composed of multiple proteins, typically 80–100 proteins per particle (organized by a single apolipoprotein B for LDL and the larger particles). A single LDL particle is about 22–27.5 nanometers in diameter, typically transporting 3,000 to 6,000 fat molecules per particle and varyin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transferrin
Transferrins are glycoproteins found in vertebrates which bind and consequently mediate the transport of iron (Fe) through blood plasma. They are produced in the liver and contain binding sites for two Iron(III), Fe3+ ions. Human transferrin is encoded by the ''TF'' gene and produced as a 76 Dalton (unit), kDa glycoprotein. Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h). Transferrin has a molecular weight of around 80 atomic mass unit, kDa and contains two specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (association constant is 1020 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality. Transferrins are not limited to only binding to iron but also to different metal ions. These glycoproteins are located in various b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ceruloplasmin
Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the ''CP'' gene. Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. It was first described in 1948. Another protein, hephaestin, is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism. Function Ceruloplasmin (CP) is an enzyme () synthesized in the liver containing 6 atoms of copper in its structure. Ceruloplasmin carries more than 95% of the total copper in healthy human plasma. The rest is accounted for by macroglobulins. 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. The molecular weight of human ceruloplasmin is reported to be 151kDa. Despit ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antiplasmin
Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin. Plasmin is an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the ''SERPINF2'' gene. Structure Alpha 2-antiplasmin (α2AP) is a member of the serine protease inhibitor (serpin) superfamily and is structurally characterized by a central serpin domain flanked by unique N- and C-terminal extensions. The mature human α2AP protein consists of 452 amino acids, with a 12-residue N-terminus, a central serpin domain, and a C-terminal tail of approximately 55 residues. The reactive center loop, which is crucial for its inhibitory function, protrudes from the central serpin domain and contains the Arg364-Met365 peptide bond that is specifically targeted and cleaved by plasmin. There are two main circulating forms: Met-α2A ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Macroglobulin
Macroglobulins are large globular proteins and are found in the blood and other body fluids. Various physiological processes, including immunity, coagulation, and chemical transport, rely on these proteins. A macroglobulin is a plasma globulin of high molecular weight. Elevated levels of macroglobulins ( macroglobulinemia) may cause manifestations of excess blood viscosity (as is the case for IgM antibodies in Waldenström macroglobulinemia) and/or precipitate within blood vessels when temperature drops (as in cryoglobulinaemia). Other macroglobulins include α2-macroglobulin, which is elevated in nephrotic syndrome, diabetes, severe burns, and other conditions, while a deficiency is associated with chronic obstructive pulmonary disease. Structure Macroglobulins range in molecular weight from 400,000 to 720,000 daltons. They are made up of four distinguishing subunits that each possess multiple domains. Disulfide bonds and non-covalent interactions allow the subunits to sta ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Haptoglobin
Haptoglobin (abbreviated as Hp) is the protein that in humans is encoded by the ''HP'' gene. In blood plasma, haptoglobin binds with high affinity to ''free'' hemoglobin released from erythrocytes, and thereby inhibits its deleterious oxidative activity. Compared to Hp, hemopexin binds to ''free'' heme. The haptoglobin-hemoglobin complex will then be removed by the reticuloendothelial system (mostly the spleen). In clinical settings, the haptoglobin assay is used to screen for and monitor intravascular hemolytic anemia. In intravascular hemolysis, free hemoglobin will be released into circulation and hence haptoglobin will bind the hemoglobin. This causes a decline in haptoglobin levels. The protein was discovered as a "plasma substance" in 1938 by French biochemists Max-Fernand Jayle and Michel Polonovski. Function Hemoglobin that has been released into the blood plasma by damaged red blood cells has harmful effects. The ''HP'' gene encodes a preproprotein that is proc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-1-acid Glycoprotein
Introduction Orosomucoid (ORM) or alpha-1-acid glycoprotein (''α1AGp'', ''AGP'' or ''AAG'') is an acute phase protein found in plasma. Orosomucoid was discovered over 70 years ago and belongs to the lipocalin protein family. There are two isoforms of AGP, referred to as AGP1 and AGP2. It is an alpha-globulin glycoprotein and is modulated by two polymorphic genes. It is synthesized primarily in hepatocytes and has a normal plasma concentration between 0.6–1.2 mg/mL (1–3% plasma protein). Recent research has shown that under certain physiological conditions, brain and adipose tissue can also synthesize this protein. Plasma levels of AGP are affected by pregnancy, burns, certain drugs, and certain diseases, particularly HIV. APG also plays an important role in inflammation and pharmacokinetics, acting as a major transport protein in the blood stream. Structure Orosomucoid is a highly glycosylated protein having a molecular weight of 34–54 kDa, with nearly 45% of i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
