Function: RCSB PDB Pdbe PDBJ Structure Summary

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PDB RCSB PDB ; PDBe ;

PDBj

PDBsum structure summary

A number of blood transport proteins are


evolutionarily related, including serum
albumin, alpha-fetoprotein, vitamin D-
binding protein and afamin.[4][5][6]

Albumin binds to the cell surface receptor


albondin.

Function
Serum albumin is the main protein of
human blood plasma.[7] 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.

Structure
The 3D structure of human serum albumin
has been determined by X-ray
┌───┐
┌────┐
┌─────┐
│ │
│ │
│ │
○○C○○○○○○○○○○○○○○○
○CC○○C○○○○C○○○○○CC○○
○C○○○○○○○○○C○○○○○○
○○○○○○○○CC○○○○C○○
│ │
│ │ │

└────────────────
─┘ └──────┘
└───────────────┘
C: cysteine, ○: any amino
acid

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 50% of human plasma
protein.[7]
Serum albumins are important in
regulating blood volume by maintaining
the oncotic pressure (also known as
colloid osmotic pressure) of the blood
compartment.[7] 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:

human serum albumin


bovine serum albumin (cattle serum
albumin) or BSA, often used in medical
and molecular biology labs.

Serum albumin levels

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.[9]
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).[10] 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.[11]

Other albumin types

Other albumin types include the storage


protein ovalbumin in egg white, and
different storage albumins in the seeds of
some plants, including hemp.[12]

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.

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.[13]

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