Abstract
Human serum albumin (HSA) is synthesized predominantly in the liver, and has an extraordinarily long circulatory half-life (~19 days). Since HSA is responsible for 80% of the colloidal osmotic pressure of plasma, the patients with hypoalbuminemia are typically given a plasma expander to increase the plasma volume. Clinically, using HSA as an extender is preferable to other options, such as dextran, hydroxylethyl starch, due to its long retention in plasma. However, the circulatory half-life of HSA is significantly- impacted by structural changes of HSA and pathological conditions. Recent scientific advances have revealed new information regarding the factors that influence the pharmacokinetic properties of HSA. In this chapter, we provide an overview of the impact of HSA structure and biotransformation upon the pharmacokinetic properties of HSA, and discuss new possibilities for the therapeutic potential of HSA based on its pharmacokinetic properties.
| Original language | English |
|---|---|
| Title of host publication | Human Serum Albumin (HSA) |
| Subtitle of host publication | Functional Structure, Synthesis and Therapeutic Uses |
| Publisher | Nova Science Publishers, Inc. |
| Pages | 69-89 |
| Number of pages | 21 |
| ISBN (Electronic) | 9781634830157 |
| ISBN (Print) | 9781634829632 |
| Publication status | Published - 2015 Jul 1 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Pharmacokinetically modified human serum albumin based therapeutic design and development. / Taguchi, Kazuaki; Chuang, Victor Tuan Giam; Yamasaki, Keishi; Otagiri, Masaki.
Human Serum Albumin (HSA): Functional Structure, Synthesis and Therapeutic Uses. Nova Science Publishers, Inc., 2015. p. 69-89.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Pharmacokinetically modified human serum albumin based therapeutic design and development
AU - Taguchi, Kazuaki
AU - Chuang, Victor Tuan Giam
AU - Yamasaki, Keishi
AU - Otagiri, Masaki
PY - 2015/7/1
Y1 - 2015/7/1
N2 - Human serum albumin (HSA) is synthesized predominantly in the liver, and has an extraordinarily long circulatory half-life (~19 days). Since HSA is responsible for 80% of the colloidal osmotic pressure of plasma, the patients with hypoalbuminemia are typically given a plasma expander to increase the plasma volume. Clinically, using HSA as an extender is preferable to other options, such as dextran, hydroxylethyl starch, due to its long retention in plasma. However, the circulatory half-life of HSA is significantly- impacted by structural changes of HSA and pathological conditions. Recent scientific advances have revealed new information regarding the factors that influence the pharmacokinetic properties of HSA. In this chapter, we provide an overview of the impact of HSA structure and biotransformation upon the pharmacokinetic properties of HSA, and discuss new possibilities for the therapeutic potential of HSA based on its pharmacokinetic properties.
AB - Human serum albumin (HSA) is synthesized predominantly in the liver, and has an extraordinarily long circulatory half-life (~19 days). Since HSA is responsible for 80% of the colloidal osmotic pressure of plasma, the patients with hypoalbuminemia are typically given a plasma expander to increase the plasma volume. Clinically, using HSA as an extender is preferable to other options, such as dextran, hydroxylethyl starch, due to its long retention in plasma. However, the circulatory half-life of HSA is significantly- impacted by structural changes of HSA and pathological conditions. Recent scientific advances have revealed new information regarding the factors that influence the pharmacokinetic properties of HSA. In this chapter, we provide an overview of the impact of HSA structure and biotransformation upon the pharmacokinetic properties of HSA, and discuss new possibilities for the therapeutic potential of HSA based on its pharmacokinetic properties.
UR - http://www.scopus.com/inward/record.url?scp=84957035515&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84957035515&partnerID=8YFLogxK
M3 - Chapter
AN - SCOPUS:84957035515
SN - 9781634829632
SP - 69
EP - 89
BT - Human Serum Albumin (HSA)
PB - Nova Science Publishers, Inc.
ER -