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|Serum albumin family|
The albumins (//) (formed from Latin: albumen "(egg) white; dried egg white") are a family of globular proteins, the most common of which are the serum albumins. All the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not glycosylated. Substances containing albumins, such as egg white, are called albuminoids.
Albumin binds to the cell surface receptor albondin.
Serum albumin is the main protein of human blood plasma. It binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin, thyroxine (T4) and pharmaceuticals (including barbiturates): its main function is to regulate the Oncotic pressure of blood. Alpha-fetoprotein (alpha-fetoglobulin) is a fetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids. The isoelectric point of albumin is 4.9.
Albumin comprises three homologous domains that assemble to form a heart-shaped protein. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds, as shown schematically below:
+---+ +----+ +-----+ | | | | | | xxCxxxxxxxxxxxxxxxxCCxxCxxxxCxxxxxCCxxxCxxxxxxxxxCxxxxxxxxxxxxxxCCxxxxCxxxx | | | | | | +-----------------+ +------+ +---------------+ C = cysteine, x = any amino acid
Serum albumin is the most abundant blood plasma protein and is produced in the liver and forms a large proportion of all plasma protein. The human version is human serum albumin, and it normally constitutes about 50% of human plasma protein.
Serum albumins are important in regulating blood volume by maintaining the oncotic pressure (also known as colloid osmotic pressure) of the blood compartment. They also serve as carriers for molecules of low water solubility this way isolating their hydrophobic nature, including lipid-soluble hormones, bile salts, unconjugated bilirubin, free fatty acids (apoprotein), calcium, ions (transferrin), and some drugs like warfarin, phenobutazone, clofibrate & phenytoin. For this reason, it is sometimes referred as a molecular "taxi". Competition between drugs for albumin binding sites may cause drug interaction by increasing the free fraction of one of the drugs, thereby affecting potency.
Specific types include:
The normal range of human serum albumin in adults (> 3 y.o.) is 3.5 to 5 g/dL. For children less than three years of age, the normal range is broader, 2.9–5.5 g/dL.
Low albumin (hypoalbuminemia) may be caused by liver disease, nephrotic syndrome, burns, protein-losing enteropathy, malabsorption, malnutrition, late pregnancy, artefact, genetic variations and malignancy.
High albumin (hyperalbuminemia) is almost always caused by dehydration. In some cases of retinol (Vitamin A) deficiency, the albumin level can be elevated to high-normal values (e.g., 4.9 g/dL). This is because retinol causes cells to swell with water (this is also the reason too much Vitamin A is toxic). This swelling also likely occurs during treatment with 13-cis retinoic acid (isotretnoin), a pharmaceutical for treating severe acne, amongst other conditions. In lab experiments it has been shown that all-trans retinoic acid down regulates human albumin production.
For patients with low blood volume, there is no evidence that albumin reduces mortality when compared with cheaper alternatives such as normal saline, or that albumin reduces mortality in patients with burns and low albumin levels. Therefore, the Cochrane Collaboration recommends that it not be used, except in clinical trials.[needs update]
Human serum albumin may be used to potentially reverse drug/chemical toxicity by binding to free drug/agent. (Tatlow, D, Poothencheri,S, Bhangal, R and Tatlow C. Novel method for rapid reversal of drug toxicity: A case report. doi|10.1111/1440-1681.12358). Ascentzi, P, Leboffe, L, Toti, D, Polticelli, F, and Trezza, V. Fipronil recognition by the FA1 site of human serum albumin. doi|10.1002/jmr.2713.
Worldwide, certain traditional Chinese medicines contain wild bear bile, banned under CITES legislation. Dip sticks, similar to common pregnancy tests, have been developed to detect the presence of bear albumin in traditional medicine products, indicating that bear bile had been used in their creation.
|Wikisource has the text of the 1911 Encyclopædia Britannica article Albumin.|