Albumin
 | This article needs additional citations for verification. (March 2009) |
| Serum albumin family | |||||||||||
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| Identifiers | |||||||||||
| Symbol | Serum_albumin | ||||||||||
| Pfam | PF00273 | ||||||||||
| Pfam clan | CL0282 | ||||||||||
| InterPro | IPR014760 | ||||||||||
| SMART | SM00103 | ||||||||||
| PROSITE | PS51438 | ||||||||||
| SCOP2 | 1ao6 / SCOPe / SUPFAM | ||||||||||
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Albumin (Latin: albus, white) refers generally to any protein that is water soluble, is moderately soluble in concentrated salt solutions, and experiences heat denaturation. Albumins are commonly found in blood plasma, and are unique from other blood proteins in that they are not glycosylated. Substances containing albumin, such as egg white, are called albuminoids.
A number of blood transport proteins are known to be evolutionarily related, including serum albumin, alpha-fetoprotein, vitamin D-binding protein and afamin.[3][4][5]
Medical uses
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.[6]
Function
Albumin is the main protein of plasma; it binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin, thyroxine (T4) and drugs (including barbiturates) - its main function is to regulate the colloidal osmotic 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 biological role of afamin (alpha-albumin) has not yet been characterised.[citation needed]
Structure
The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 Å.[7]
Albumin comprises three homologous domains that assemble to form a heart-shaped molecule.[2] Each domain is a product of two subdomains that possess common structural motifs.[2] 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
Types
Serum albumin
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 60% 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's 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:
- human serum albumin
- bovine serum albumin (cattle serum albumin) or BSA, often used in medical and molecular biology labs.
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).[8] In lab experiments it has been shown that All-trans retinoic acid down regulates human albumin production[9]
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.[10]
Albumin binds to the cell surface receptor Albondin.
Other types
Other types include the storage protein ovalbumin in egg white, and different storage albumins in the seeds of some plants.
- Note that the protein 'albumin' is spelled with an "i", while "albumen" with an "e", is the white of an egg which contains (among other things) several dozen types of albumin (with an 'i'), mostly ovalbumin.
See also
- Cohn process (human serum albumin purification method)
- Serum albumin
References
- ^ Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K (1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Eng. 12 (6): 439–46. doi:10.1093/protein/12.6.439. PMID 10388840.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b c He XM, Carter DC (1992). "Atomic structure and chemistry of human serum albumin". Nature. 358 (6383): 209–15. doi:10.1038/358209a0. PMID 1630489.
- ^ Haefliger DN, Moskaitis JE, Schoenberg DR, Wahli W (1989). "Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family". J. Mol. Evol. 29 (4): 344–54. doi:10.1007/BF02103621. PMID 2481749.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Schoentgen F, Metz-Boutigue MH, Jollès J, Constans J, Jollès P (1986). "Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein". Biochim. Biophys. Acta. 871 (2): 189–98. doi:10.1016/0167-4838(86)90173-1. PMID 2423133.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Lichenstein HS, Lyons DE, Wurfel MM, Johnson DA, McGinley MD, Leidli JC, Trollinger DB, Mayer JP, Wright SD, Zukowski MM (1994). "Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family". J. Biol. Chem. 269 (27): 18149–54. PMID 7517938.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ "Human albumin solution for resuscitation and volume expansion in critically ill patients". Cochrane Database Syst Rev (10): CD001208. 2011. doi:10.1002/14651858.CD001208.pub3. PMID 21975732.
- ^ Sugio S , Kashima A , Mochizuki S , Noda M , Kobayashi K (1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Engineering. 12 (6): 439–446. doi:10.1093/protein/12.6.439. PMID 10388840.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^
Gaull, H; Wright, CE; Gaull, GE (1984). "Protective effect of taurine, zinc and tocopherol on retinol-induced damage in human lymphoblastoid cells". J Nutr. 114 (12): 2256–61. PMID 6502269.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ Suzuki, T; Matsuura, T; Ohkawa, K; Miyamura, T; Okazaki, I; Watanabe, T; Suzuki, T (2006). "All-trans retinoic acid down-regulates human albumin gene expression through the induction of C/EBPbeta-LIP". Biochem J. 397 (2): 345–53. doi:10.1042/BJ20051863. PMC 1513275. PMID 16608438.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ "Normal Ranges for Common Laboratory Tests." Rush University
External links
- Albumins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- The Albumin website
- Albumin binding prediction