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Alpha-globulin
Alpha globulins are a group of globular proteins in blood plasma, plasma that are highly mobile in alkaline or electrically charged solutions. They inhibit certain blood proteases and show significant inhibitor activity. The alpha globulins typically have molecular weights of around 93 kDa. Examples Alpha globulins include certain hormones, proteins that transport hormones, and other compounds, including prothrombin and High-density lipoprotein, HDL. Alpha 1 globulins *Alpha 1-antitrypsin, α1-antitrypsin *Alpha 1-antichymotrypsin *Orosomucoid (acid glycoprotein) *Serum amyloid A *Alpha 1-lipoprotein Alpha 2 globulins *Haptoglobin *Alpha-2u globulin *Alpha 2-macroglobulin, α2-macroglobulin *Ceruloplasmin *Thyroxine-binding globulin *Alpha 2-antiplasmin *Protein C *Alpha 2-lipoprotein *Angiotensinogen * Cortisol-binding globulin, Cortisol binding globulin *Vitamin D-binding protein References Blood proteins {{protein-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cortisol-binding Globulin
Transcortin, also known as corticosteroid-binding globulin (CBG) or serpin A6, is a protein produced in the liver in animals. In humans it is encoded by the SERPINA6 gene. It is an alpha-globulin. Function This gene encodes an alpha-globulin protein with corticosteroid-binding properties. This is the major transport protein for glucocorticoids and progestins in the blood of most vertebrates. The gene localizes to a chromosomal region containing several closely related serine protease inhibitors (serpins). Binding Transcortin binds several steroid hormones at high rates: * Cortisol - Approximately 90% of the cortisol in circulation is bound to transcortin. (The rest is bound to serum albumin.) Cortisol is thought to be biologically active only when it is not bound to transcortin. * Cortisone * Deoxycorticosterone (DOC) * Corticosterone - About 78% of serum corticosterone is bound to transcortin. * Aldosterone - Approximately 17% of serum aldosterone is bound to transcortin, while ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vitamin D-binding Protein
Vitamin D-binding protein (DBP), also/originally known as gc-globulin (group-specific component), is a protein that in humans is encoded by the ''GC'' gene. DBP is genetically the oldest member of the albuminoid family and appeared early in the evolution of vertebrates. Structure Human GC is a glycosylated alpha-globulin, ~58 kDa in size. Its 458 amino acids are coded for by 1690 nucleotides on chromosome 4 (4q11–q13). The primary structure contains 28 cysteine residues forming multiple disulfide bonds. GC contains 3 domains. Domain 1 is composed of 10 alpha helices, domain 2 of 9, and domain 3 of 4. Function Vitamin D-binding protein belongs to the albumin gene family, together with human serum albumin and alpha-fetoprotein. It is a multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid and on the surface of many cell types. It is able to bind the various forms of vitamin D including ergocalciferol (vitamin D2) and cholecalciferol (vitamin D3), the 2 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 1-antitrypsin
Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded in humans by the ''SERPINA1'' gene. A protease inhibitor, it is also known as alpha1–proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it inhibits various proteases (not just trypsin). In older biomedical literature it was sometimes called serum trypsin inhibitor (STI, dated terminology), because its capability as a trypsin inhibitor was a salient feature of its early study. As a type of enzyme inhibitor, it protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 0.9–2.3 g/L (in the US the reference range is expressed as mg/dL or micromoles), but the concentration can rise manyfold upon acute inflammation. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Orosomucoid
Orosomucoid (ORM) or alpha-1-acid glycoprotein (''α1AGp'', ''AGP'' or ''AAG'') is an acute phase protein found in plasma. 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). Plasma levels are affected by pregnancy, burns, certain drugs, and certain diseases, particularly HIV. The only established function of ORM is to act as a carrier of basic and neutrally charged lipophilic compounds. In medicine, it is known as the primary carrier of basic (negatively charged) drugs (whereas albumin carries acidic (positively charged) and neutral drugs), steroids, and protease inhibitors. Aging causes a small decrease in plasma albumin levels; if anything, there is a small increase in alpha-1-acid glycoprotein. The effect of these changes on drug protein binding and drug delivery, however, appear to be minimal. AGP shows a comple ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-2u Globulin
Major urinary proteins (Mups), also known as α2u-globulins, are a subfamily of proteins found in abundance in the urine and other secretions of many animals. Mups provide a small range of identifying information about the donor animal, when detected by the vomeronasal organ of the receiving animal. They belong to a larger family of proteins known as lipocalins. Mups are encoded by a cluster of genes, located adjacent to each other on a single stretch of DNA, that varies greatly in number between species: from at least 21 functional genes in mice to none in humans. Mup proteins form a characteristic glove shape, encompassing a ligand-binding pocket that accommodates specific small organic chemicals. Urinary proteins were first reported in rodents in 1932, during studies by Thomas Addis into the cause of proteinuria. They are potent human allergens and are largely responsible for a number of animal allergies, including to cats, horses and rodents. Their endogenous function withi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Angiotensinogen
Angiotensin is a peptide hormone that causes vasoconstriction and an increase in blood pressure. It is part of the renin–angiotensin system, which regulates blood pressure. Angiotensin also stimulates the release of aldosterone from the adrenal cortex to promote sodium retention by the kidneys. An oligopeptide, angiotensin is a hormone and a dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. Angiotensin was isolated in the late 1930s (first named 'angiotonin' or 'hypertensin') and subsequently characterized and synthesized by groups at the Cleveland Clinic and Ciba laboratories. Precursor and types Angiotensinogen Angiotensinogen is an α-2-globulin synthesized in the liver and is a precursor for angiotensin, but has also been indicated as having many other roles not related to angiotensin peptides. It is a member of the serpin family of proteins, leading to another name: Serpin A8, although it is not known t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 2-lipoprotein
A lipoprotein is a biochemical assembly whose primary function is to transport hydrophobic lipid (also known as fat) molecules in water, as in blood plasma or other extracellular fluids. They consist of a triglyceride and cholesterol center, surrounded by a phospholipid outer shell, with the hydrophilic portions oriented outward toward the surrounding water and lipophilic portions oriented inward toward the lipid center. A special kind of protein, called apolipoprotein, is embedded in the outer shell, both stabilising the complex and giving it a functional identity that determines its role. Many enzymes, transporters, structural proteins, antigens, adhesins, and toxins are lipoproteins. Examples include plasma lipoprotein particles ( HDL, LDL, IDL, VLDL and chylomicrons). Subgroups of these plasma particles are primary drivers or modulators of atherosclerosis. Scope Transmembrane lipoproteins Some transmembrane proteolipids, especially those found in bacteria, are referred t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein C
Protein C, also known as autoprothrombin IIA and blood coagulation factor XIX, is a zymogen, that is, an inactive enzyme. The activated form plays an important role in regulating anticoagulation, inflammation, and apoptosis, cell death and maintaining the vascular permeability, permeability of blood vessel walls in humans and other animals. Activated protein C (APC) performs these operations primarily by proteolysis, proteolytically inactivating proteins Factor V, Factor Va and Factor VIII, Factor VIIIa. APC is classified as a serine protease since it contains a residue (chemistry), residue of serine in its active site. In humans, protein C is encoded by the ''PROC'' gene, which is found on chromosome 2 (human), chromosome 2. The zymogenic form of protein C is a vitamin K-dependent glycoprotein that circulates in blood plasma. Its structure is that of a two-chain polypeptide consisting of a light chain and a heavy chain connected by a disulfide bond. The protein C zymog ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 2-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. Role in disease Very few cases (<20) of A2AP deficiency have been described. As plasmin degrades blood clots, impaired inhibition of plasmin leads to a bleeding tendency, which was severe in the cases reported. In liver , there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of and an increase in |
Thyroxine-binding Globulin
Thyroxine-binding globulin (TBG) is a globulin protein that in humans is encoded by the ''SERPINA7'' gene. TBG binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T4) and triiodothyronine (T3) in the bloodstream. Of these three proteins, TBG has the highest affinity for T4 and T3 but is present in the lowest concentration relative to transthyretin and albumin, which also bind T3 and T4 in circulation. Despite its low concentration, TBG carries the majority of T4 in the blood plasma. Due to the very low concentration of T4 and T3 in the blood, TBG is rarely more than 25% saturated with its ligand. Unlike transthyretin and albumin, TBG has a single binding site for T4/T3. TBG is synthesized primarily in the liver as a 54-kDa protein. In terms of genomics, TBG is a serpin Serpins are a Protein superfamily, superfamily of proteins with similar struct ... [...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. Despite ext ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha 2-macroglobulin
α2-Macroglobulin (α2M), or alpha-2-macroglobulin, is a large (720 KDa) plasma protein found in the blood. It is mainly produced by the liver, and also locally synthesized by macrophages, fibroblasts, and adrenocortical cells. In humans it is encoded by the ''A2M'' gene. α2-Macroglobulin acts as an antiprotease and is able to inactivate an enormous variety of proteinases. It functions as an inhibitor of fibrinolysis by inhibiting plasmin and kallikrein. It functions as an inhibitor of coagulation by inhibiting thrombin. α2-macroglobulin may act as a carrier protein because it also binds to numerous growth factors and cytokines, such as platelet-derived growth factor, basic fibroblast growth factor, TGF-β, insulin, and IL-1β. No specific deficiency with associated disease has been recognized, and no disease state is attributed to low concentrations of α2-macroglobulin. The concentration of α2-macroglobulin rises 10-fold or more in the nephrotic syndrome when other lower mo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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