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Unraveling the mysteries of serum albumin-more than just a serum protein.

Merlot AM, Kalinowski DS, Richardson DR - Front Physiol (2014)

Bottom Line: Considering this, there is renewed interest in isolating and characterizing albumin-binding proteins or receptors on the plasma membrane that are responsible for albumin uptake.Initially, the cellular uptake and intracellular localization of albumin was unknown due to the large confinement of the protein within the vascular and interstitial compartment of the body.Studies have since assessed the intracellular localization of albumin in order to understand the mechanisms and pathways responsible for its uptake, distribution and catabolism in multiple tissues, and this is reviewed herein.

View Article: PubMed Central - PubMed

Affiliation: Molecular Pharmacology and Pathology Program, Department of Pathology, Faculty of Medicine, Bosch Institute, The University of Sydney Sydney, NSW, Australia.

ABSTRACT
Serum albumin is a multi-functional protein that is able to bind and transport numerous endogenous and exogenous compounds. The development of albumin drug carriers is gaining increasing importance in the targeted delivery of cancer therapy, particularly as a result of the market approval of the paclitaxel-loaded albumin nanoparticle, Abraxane®. Considering this, there is renewed interest in isolating and characterizing albumin-binding proteins or receptors on the plasma membrane that are responsible for albumin uptake. Initially, the cellular uptake and intracellular localization of albumin was unknown due to the large confinement of the protein within the vascular and interstitial compartment of the body. Studies have since assessed the intracellular localization of albumin in order to understand the mechanisms and pathways responsible for its uptake, distribution and catabolism in multiple tissues, and this is reviewed herein.

No MeSH data available.


Related in: MedlinePlus

Structure of human serum albumin consisting of three domains, each grouped into subdomains A and B (Subdomain Ia, yellow; Ib, green; IIa, red; IIb, magenta; IIIa, blue; and IIIb, cyan). Sugio et al. (1999) by permission of Oxford University Press.
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Figure 1: Structure of human serum albumin consisting of three domains, each grouped into subdomains A and B (Subdomain Ia, yellow; Ib, green; IIa, red; IIb, magenta; IIIa, blue; and IIIb, cyan). Sugio et al. (1999) by permission of Oxford University Press.

Mentions: Serum albumin is the most abundant protein in the blood plasma of all vertebrates with the concentration in human serum being 35–50 mg/mL (Peters, 1996). Human serum albumin (HSA) has a molecular mass of 66,348 Da and is composed of three homologous domains, numbered I, II, and III (Figure 1) (He and Carter, 1992; Peters, 1996; Sugio et al., 1999). Each domain is grouped into subdomains A and B that possess common structural motifs. The two principal regions responsible for ligand-binding to HSA are known as Sudlow's Site I and II, located in subdomain IIA and IIIA (Figure 1), respectively (Sudlow et al., 1976; Peters, 1996). Albumin is coded by a single gene, which is expressed in a co-dominant manner with both alleles being transcribed and translated (Hawkins and Dugaiczyk, 1982; Peters, 1996). The human albumin gene is located on the long arm of chromosome 4 at position q13.3.


Unraveling the mysteries of serum albumin-more than just a serum protein.

Merlot AM, Kalinowski DS, Richardson DR - Front Physiol (2014)

Structure of human serum albumin consisting of three domains, each grouped into subdomains A and B (Subdomain Ia, yellow; Ib, green; IIa, red; IIb, magenta; IIIa, blue; and IIIb, cyan). Sugio et al. (1999) by permission of Oxford University Press.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4129365&req=5

Figure 1: Structure of human serum albumin consisting of three domains, each grouped into subdomains A and B (Subdomain Ia, yellow; Ib, green; IIa, red; IIb, magenta; IIIa, blue; and IIIb, cyan). Sugio et al. (1999) by permission of Oxford University Press.
Mentions: Serum albumin is the most abundant protein in the blood plasma of all vertebrates with the concentration in human serum being 35–50 mg/mL (Peters, 1996). Human serum albumin (HSA) has a molecular mass of 66,348 Da and is composed of three homologous domains, numbered I, II, and III (Figure 1) (He and Carter, 1992; Peters, 1996; Sugio et al., 1999). Each domain is grouped into subdomains A and B that possess common structural motifs. The two principal regions responsible for ligand-binding to HSA are known as Sudlow's Site I and II, located in subdomain IIA and IIIA (Figure 1), respectively (Sudlow et al., 1976; Peters, 1996). Albumin is coded by a single gene, which is expressed in a co-dominant manner with both alleles being transcribed and translated (Hawkins and Dugaiczyk, 1982; Peters, 1996). The human albumin gene is located on the long arm of chromosome 4 at position q13.3.

Bottom Line: Considering this, there is renewed interest in isolating and characterizing albumin-binding proteins or receptors on the plasma membrane that are responsible for albumin uptake.Initially, the cellular uptake and intracellular localization of albumin was unknown due to the large confinement of the protein within the vascular and interstitial compartment of the body.Studies have since assessed the intracellular localization of albumin in order to understand the mechanisms and pathways responsible for its uptake, distribution and catabolism in multiple tissues, and this is reviewed herein.

View Article: PubMed Central - PubMed

Affiliation: Molecular Pharmacology and Pathology Program, Department of Pathology, Faculty of Medicine, Bosch Institute, The University of Sydney Sydney, NSW, Australia.

ABSTRACT
Serum albumin is a multi-functional protein that is able to bind and transport numerous endogenous and exogenous compounds. The development of albumin drug carriers is gaining increasing importance in the targeted delivery of cancer therapy, particularly as a result of the market approval of the paclitaxel-loaded albumin nanoparticle, Abraxane®. Considering this, there is renewed interest in isolating and characterizing albumin-binding proteins or receptors on the plasma membrane that are responsible for albumin uptake. Initially, the cellular uptake and intracellular localization of albumin was unknown due to the large confinement of the protein within the vascular and interstitial compartment of the body. Studies have since assessed the intracellular localization of albumin in order to understand the mechanisms and pathways responsible for its uptake, distribution and catabolism in multiple tissues, and this is reviewed herein.

No MeSH data available.


Related in: MedlinePlus