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{{About|the family of mammalian albumin proteins|the human variant|human serum albumin|the cow variant|bovine serum albumin|the chicken variant|conalbumin}}
|authorTag={{AP}}
{{Infobox_gene}}
|genericName=Serum albumin
|aOrAn=a
|drugClass=volume expander
|indicationType=treatment
|indication=burn therapy, [[Cardiopulmonary bypass]], [[hypovolemic shock]], [[acute liver failure]] and sequestration of protein rich fluids
|blackBoxWarningTitle=<b><span style="color:#FF0000;">TITLE</span></b>
|blackBoxWarningBody=<i><span style="color:#FF0000;">Condition Name:</span></i> (Content)
|fdaLIADAdult======Emergency Treatment of Hypovolemic Shock=====
Albuked 5 is iso-oncotic with normal plasma and on intravenous infusion will expand the circulating blood volume by an amount approximately equal to the volume infused. In conditions associated mainly with a volume deficit, albumin is best administered as a 5% solution (Albuked 5); but where there is an oncotic deficit, Albumin (Human) 25%, USP (Albuked™ 25) may be preferred. This is also an important consideration where the treatment of the shock state has been delayed. If Albuked 25 is used, appropriate additional crystalloid should be administered.


[[Crystalloid solutions]] in volumes several times greater than that of Albuked 5 may be effective in treating [[shock]] in younger individuals who have no preexisting illness at the time of the incident. Older patients, especially those with preexisting debilitating conditions, or those in whom the [[shock]] is caused by a medical disorder, or where the state of shock has existed for some time before active therapy could be instituted, may not tolerate [[hypoalbuminemia]] as well.(1)
'''Serum albumin''', often referred to simply as '''blood albumin''', is an [[albumin]] (a type of globular [[protein]]) found in vertebrate [[blood]]. [[Human serum albumin]] is encoded by the ''ALB'' [[gene]].<ref name="pmid6292049">{{cite journal | vauthors = Hawkins JW, Dugaiczyk A | title = The human serum albumin gene: structure of a unique locus | journal = Gene | volume = 19 | issue = 1 | pages = 55–8 | year = 1982 | pmid = 6292049 | doi = 10.1016/0378-1119(82)90188-3 }}</ref><ref name="pmid6192711">{{cite journal | vauthors = Harper ME, Dugaiczyk A | title = Linkage of the evolutionarily-related serum albumin and alpha-fetoprotein genes within q11-22 of human chromosome 4 | journal = American Journal of Human Genetics | volume = 35 | issue = 4 | pages = 565–72 | date = July 1983 | pmid = 6192711 | pmc = 1685723 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: albumin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=213| accessdate = }}</ref> Other [[mammal]]ian forms, such as [[bovine serum albumin]], are chemically similar.


Removal of [[ascitic fluid]] from a patient with [[cirrhosis]] may cause changes in cardiovascular function and even result in [[hypovolemic shock]]. In such circumstances, the use of albumin infusion may be required to support the [[blood volume]].
Serum albumin is produced by the [[liver]], occurs dissolved in [[blood plasma]] and is the most abundant [[blood protein]] in [[mammal]]s. Albumin is essential for maintaining the [[oncotic pressure]] needed for proper distribution of [[body fluid]]s between blood vessels and body tissues; without albumin, the high pressure in the blood vessels would force more fluids out into the tissues. It also acts as a plasma carrier by non-specifically binding several [[hydrophobic]] [[steroid hormones]] and as a transport protein for [[hemin]] and [[fatty acid]]s. Too much or too little circulating serum albumin may be harmful. Albumin in the urine usually denotes the presence of kidney disease. Occasionally albumin appears in the urine of normal persons following long standing ([[postural albuminuria]]).


=====Burn Therapy=====
== Function ==
An optimal therapeutic regimen with respect to the administration of [[colloids]], [[crystalloids]], and water following extensive burns has not been established. During the first 24 hours after sustaining thermal injury, large volumes of crystalloids are infused to restore the depleted extracellular fluid volume. Beyond 24 hours, albumin can be used to maintain plasma [[colloid osmotic pressure]]. Albuked 25 may be preferred for this purpose.
Albumin functions primarily as a carrier protein for [[steroid]]s, [[fatty acid]]s, and [[thyroid hormone]]s in the blood and plays a major role in stabilizing extracellular fluid volume by contributing to [[oncotic pressure]] (known also as colloid osmotic pressure) of plasma.


=====Cardiopulmonary Bypass=====
Because smaller animals (for example [[rat]]s) function at a lower [[blood pressure]], they need less oncotic pressure to balance this{{Citation needed|date=May 2016}}, and thus need less albumin to maintain proper fluid distribution.
With the relatively small priming volume required with modern pumps, preoperative dilution of the blood using [[albumin]] and [[crystalloid]] has been shown to be safe and well-tolerated. Although the limit to which the [[hematocrit]] and plasma protein concentration can be safely lowered has not been defined, it is common practice to adjust the [[albumin]] and [[crystalloid]] pump prime to achieve a [[hematocrit]] of 20% and a plasma albumin concentration of 2.5 g per 100 mL in the patient.


=====Acute Liver Failure=====
==Synthesis==
In the uncommon situation of rapid loss of [[liver function[[, with or without [[coma]], administration of albumin may serve the double purpose of supporting the [[colloid osmotic pressure]] of the [[plasma]] as well as binding excess [[plasma bilirubin]].
Albumin is synthesized in the [[liver]] as preproalbumin which has an [[N-terminus|N-terminal]] peptide that is removed before the nascent protein is released from the rough [[endoplasmic reticulum]]. The product, proalbumin, is in turn cleaved in the [[Golgi apparatus|Golgi vesicle]]s to produce the secreted albumin.<ref name="entrez"/>


=====Sequestration of Protein Rich Fluids=====
== Properties ==
This occurs in such conditions as acute [[peritonitis]], [[pancreatitis]], [[mediastinitis]], and extensive [[cellulitis]]. The magnitude of loss into the third space may require treatment of reduced volume or [[oncotic]] activity with an infusion of albumin.
Albumin is a globular, water-soluble, un-[[glycosylation|glycosylated]] serum protein of approximate molecular weight of 65,000 [[Unified_atomic_mass_unit|Daltons]].
|offLabelAdultGuideSupport=There is limited information regarding <i>Off-Label Guideline-Supported Use</i> of Serum albumin in adult patients.
 
|offLabelAdultNoGuideSupport=There is limited information regarding <i>Off-Label Non–Guideline-Supported Use</i> of Serum albumin in adult patients.
Albumin (when ionized in water at pH 7.4, as found in the body) is negatively charged. The [[glomerular basement membrane]] is also negatively charged in the body; some studies suggest that this prevents the filtration of albumin in the urine. According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate. A defect in this property results in [[nephrotic syndrome]] leading to albumin loss in the urine. Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin.
|offLabelPedGuideSupport=There is limited information regarding <i>Off-Label Guideline-Supported Use</i> of Serum albumin in pediatric patients.
|offLabelPedNoGuideSupport=There is limited information regarding <i>Off-Label Non–Guideline-Supported Use</i> of Serum albumin in pediatric patients.
|alcohol=Alcohol-Serum albumin interaction has not been established. Talk to your doctor about the effects of taking alcohol with this medication.
}}
{{SI}}
{{CMG}}


==Overview==
== Structure ==
[[Serum albumin]], often referred to simply as '''albumin''', is the most abundant [[plasma protein]] in humans and other [[mammal]]s. Albumin is essential for maintaining the [[osmotic pressure]] needed for proper distribution of [[body fluid]]s between intravascular compartments and body tissues. It also acts as a plasma carrier by non-specifically binding several [[hydrophobic]] [[steroid hormones]] and as a transport protein for [[hemin]] and [[fatty acid]]s.
{{main|Albumin}}
The general structure of albumin is characterized by several long [[alpha helix|α helices]] allowing it to maintain a relatively static shape, which is essential for regulating blood pressure.


==Classification==
Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One [[hemin]] and six long-chain [[fatty acid]]s can bind to serum albumin at the same time.<ref name="pmid12846933">{{cite journal | vauthors = Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S | title = Crystal structural analysis of human serum albumin complexed with hemin and fatty acid | journal = BMC Structural Biology | volume = 3 | issue =  | pages = 6 | date = July 2003 | pmid = 12846933 | pmc = 166163 | doi = 10.1186/1472-6807-3-6 }}</ref>
{|
|{{Infobox protein family
| Symbol = Serum_albumin
| Name = Serum albumin family
| image = PDB 1ao6 EBI.jpg
| width =
| caption = Structure of human serum albumin.<ref>{{cite journal | vauthors = Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K | title = Crystal structure of human serum albumin at 2.5 A resolution | journal = Protein Engineering | volume = 12 | issue = 6 | pages = 439–46 | date = June 1999 | pmid = 10388840 | doi = 10.1093/protein/12.6.439 }}</ref>
| Pfam = PF00273
| Pfam_clan = CL0282
| InterPro = IPR014760
| SMART = SM00103
| PROSITE = PS51438
| SCOP = 1ao6
| TCDB =
| OPM family =
| OPM protein =
| PDB = {{PDB2|1ao6}}, {{PDB2|1bj5}}, {{PDB2|1bke}}, {{PDB2|1bm0}}, {{PDB2|1e78}}, {{PDB2|1e7a}}, {{PDB2|1e7b}}, {{PDB2|1e7c}}, {{PDB2|1e7e}}, {{PDB2|1e7f}}, {{PDB2|1e7g}}, {{PDB2|1e7h}}, {{PDB2|1e7i}}, {{PDB2|1gni}}, {{PDB2|1gnj}}, {{PDB2|1h9z}}, {{PDB2|1ha2}}, {{PDB2|1hk1}}, {{PDB2|1hk2}}, {{PDB2|1hk3}}, {{PDB2|1hk4}}, {{PDB2|1hk5}}, {{PDB2|1j78}}, {{PDB2|1j7e}}, {{PDB2|1kw2}}, {{PDB2|1kxp}}, {{PDB2|1lot}}, {{PDB2|1ma9}}, {{PDB2|1n5u}}, {{PDB2|1o9x}}, {{PDB2|1tf0}}, {{PDB2|1uor}}, {{PDB2|1ysx}}, {{PDB2|2bx8}}, {{PDB2|2bxa}}, {{PDB2|2bxb}}, {{PDB2|2bxc}}, {{PDB2|2bxd}}, {{PDB2|2bxe}}, {{PDB2|2bxf}}, {{PDB2|2bxg}}, {{PDB2|2bxh}}, {{PDB2|2bxi}}, {{PDB2|2bxk}}, {{PDB2|2bxl}}, {{PDB2|2bxm}}, {{PDB2|2bxn}}, {{PDB2|2bxo}}, {{PDB2|2bxp}}, {{PDB2|2bxq}}, {{PDB2|2i2z}}, {{PDB2|2i30}}, {{PDB2|2vdb}}, {{PDB2|2vue}}, {{PDB2|2vuf}}, {{PDB2|3b9l}}, {{PDB2|3b9m}}
}}
|}


== Types ==
Serum albumin is widely distributed in mammals. 
* The human version is [[human serum albumin]].  
* The human version is [[human serum albumin]].  
* [[Bovine serum albumin]], or BSA, is commonly used in immunodiagnostic procedures, clinical chemistry reagents, cell culture media, protein chemistry research and [[molecular biology]] laboratories.
* [[Bovine serum albumin]], or BSA, is commonly used in immunodiagnostic procedures, clinical chemistry reagents, cell culture media, protein chemistry research (including venom toxicity), and [[molecular biology]] laboratories (usually to leverage its non-specific protein binding properties).


==Pathophysiology==
== See also ==
 
* [[Human serum albumin]]
Albumin is negatively charged. The [[glomerular basement membrane]] is also negatively charged; some studies suggest that this prevents the filtration of albumin in the urine. According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate, a defect in this property results in [[nephrotic syndrome]].  Thus, there is more albumin loss in the urine. Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin.
* [[Bovine serum albumin]]
 
* [[Blood plasma fractionation]]
Because smaller animals (for example rats) function at a lower [[blood pressure]], they need less [[oncotic pressure]] to balance this, and thus need less albumin to maintain proper fluid distribution.
* [[Chromatography in blood processing]]
 
* [[Lactalbumin]]
Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One [[hemin]] and six long-chain [[fatty acid]]s can bind to serum albumin at the same time <ref name="">
* [[Ovalbumin]]
BMC Structural Biology 2003, 3(1):6 2003. ''Crystal structural analysis of human serum albumin complexed with hemin and fatty acid''. Zunszain, Patricia A Ghuman, Jamie Komatsu, Teruyuki Tsuchida, Eishun Curry, Stephen doi: 10.1186/1472-6807-3-6 PMID 12846933 [http://www.biomedcentral.com/1472-6807/3/6 online]</ref>.


== References ==
== References ==
{{Reflist|2}}
{{Reflist}}


== External links ==
* [http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb37_1.html RCSB Protein Data Bank : Molecule of the Month – Serum Albumin]
* [http://albumin.althotas.com/ Albumin binding prediction]


{{PDB Gallery|geneid=213}}
{{Albumins}}
{{Albumins}}
{{Nuclear receptor modulators}}


[[Category:Proteins]]
[[Category:Blood proteins]]
[[Category:Blood]]
[[Category:Gastroenterology]]
 
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Latest revision as of 12:10, 10 January 2019

This article is about the family of mammalian albumin proteins. For the human variant, see human serum albumin. For the cow variant, see bovine serum albumin. For the chicken variant, see conalbumin.
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Serum albumin, often referred to simply as blood albumin, is an albumin (a type of globular protein) found in vertebrate blood. Human serum albumin is encoded by the ALB gene.[1][2][3] Other mammalian forms, such as bovine serum albumin, are chemically similar.

Serum albumin is produced by the liver, occurs dissolved in blood plasma and is the most abundant blood protein in mammals. Albumin is essential for maintaining the oncotic pressure needed for proper distribution of body fluids between blood vessels and body tissues; without albumin, the high pressure in the blood vessels would force more fluids out into the tissues. It also acts as a plasma carrier by non-specifically binding several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids. Too much or too little circulating serum albumin may be harmful. Albumin in the urine usually denotes the presence of kidney disease. Occasionally albumin appears in the urine of normal persons following long standing (postural albuminuria).

Function

Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones in the blood and plays a major role in stabilizing extracellular fluid volume by contributing to oncotic pressure (known also as colloid osmotic pressure) of plasma.

Because smaller animals (for example rats) function at a lower blood pressure, they need less oncotic pressure to balance this[citation needed], and thus need less albumin to maintain proper fluid distribution.

Synthesis

Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin.[3]

Properties

Albumin is a globular, water-soluble, un-glycosylated serum protein of approximate molecular weight of 65,000 Daltons.

Albumin (when ionized in water at pH 7.4, as found in the body) is negatively charged. The glomerular basement membrane is also negatively charged in the body; some studies suggest that this prevents the filtration of albumin in the urine. According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate. A defect in this property results in nephrotic syndrome leading to albumin loss in the urine. Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin.

Structure

Main article: Albumin

The general structure of albumin is characterized by several long α helices allowing it to maintain a relatively static shape, which is essential for regulating blood pressure.

Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time.[4]

Serum albumin family
File:PDB 1ao6 EBI.jpg
Structure of human serum albumin.[5]
Identifiers
SymbolSerum_albumin
PfamPF00273
Pfam clanCL0282
InterProIPR014760
SMARTSM00103
PROSITEPS51438
SCOP1ao6
SUPERFAMILY1ao6

Types

Serum albumin is widely distributed in mammals.

  • The human version is human serum albumin.
  • Bovine serum albumin, or BSA, is commonly used in immunodiagnostic procedures, clinical chemistry reagents, cell culture media, protein chemistry research (including venom toxicity), and molecular biology laboratories (usually to leverage its non-specific protein binding properties).

See also

References

  1. ↑ Hawkins JW, Dugaiczyk A (1982). "The human serum albumin gene: structure of a unique locus". Gene. 19 (1): 55–8. doi:10.1016/0378-1119(82)90188-3. PMID 6292049.
  2. ↑ Harper ME, Dugaiczyk A (July 1983). "Linkage of the evolutionarily-related serum albumin and alpha-fetoprotein genes within q11-22 of human chromosome 4". American Journal of Human Genetics. 35 (4): 565–72. PMC 1685723. PMID 6192711.
  3. ↑ 3.0 3.1 "Entrez Gene: albumin".
  4. ↑ Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S (July 2003). "Crystal structural analysis of human serum albumin complexed with hemin and fatty acid". BMC Structural Biology. 3: 6. doi:10.1186/1472-6807-3-6. PMC 166163. PMID 12846933.
  5. ↑ Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K (June 1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Engineering. 12 (6): 439–46. doi:10.1093/protein/12.6.439. PMID 10388840.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Serum_albumin&oldid=1526501"