Pharmacokinetically modified human serum albumin based therapeutic design and development
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...
| Main Authors: | , , , |
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| Format: | Book Chapter |
| Published: |
2015
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| Online Access: | http://hdl.handle.net/20.500.11937/46904 |
| _version_ | 1848757688350015488 |
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| author | Taguchi, K. Chuang, Victor Yamasaki, K. Otagiri, M. |
| author_facet | Taguchi, K. Chuang, Victor Yamasaki, K. Otagiri, M. |
| author_sort | Taguchi, K. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T09:32:04Z |
| format | Book Chapter |
| id | curtin-20.500.11937-46904 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:32:04Z |
| publishDate | 2015 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-469042017-01-30T15:29:56Z Pharmacokinetically modified human serum albumin based therapeutic design and development Taguchi, K. Chuang, Victor Yamasaki, K. Otagiri, M. 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. 2015 Book Chapter http://hdl.handle.net/20.500.11937/46904 restricted |
| spellingShingle | Taguchi, K. Chuang, Victor Yamasaki, K. Otagiri, M. Pharmacokinetically modified human serum albumin based therapeutic design and development |
| title | Pharmacokinetically modified human serum albumin based therapeutic design and development |
| title_full | Pharmacokinetically modified human serum albumin based therapeutic design and development |
| title_fullStr | Pharmacokinetically modified human serum albumin based therapeutic design and development |
| title_full_unstemmed | Pharmacokinetically modified human serum albumin based therapeutic design and development |
| title_short | Pharmacokinetically modified human serum albumin based therapeutic design and development |
| title_sort | pharmacokinetically modified human serum albumin based therapeutic design and development |
| url | http://hdl.handle.net/20.500.11937/46904 |