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ヒト血清アルブミンの体内動態に及ぼす表面電荷とα-へリックス含量の影響(発表論文抄録(2008))
https://fukuyama-u.repo.nii.ac.jp/records/8574
https://fukuyama-u.repo.nii.ac.jp/records/8574479c57aa-574c-4e7f-b66e-567cd7197d7f
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
ヒト血清アルブミンの体内動態に及ぼす表面電荷とα-へリックス含量の影響 (54.1 kB)
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Copyright (c) 2009 by Fukuyama University
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-01-26 | |||||
| タイトル | ||||||
| タイトル | ヒト血清アルブミンの体内動態に及ぼす表面電荷とα-へリックス含量の影響(発表論文抄録(2008)) | |||||
| タイトル | ||||||
| タイトル | Changes of net charge and alpha-helical content affect the pharmacokinetic properties of human serum albumin. | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Half-Life | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Humans | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Ions | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Models, Molecular | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Mutant Proteins | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Point Mutation | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Protein Denaturation | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Protein Folding | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Protein Structure, Secondary | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Protein Structure, Tertiary | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Serum Albumin | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Structure-Activity Relationship | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Temperature | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | departmental bulletin paper | |||||
| 著者 |
岩尾, 康範
× 岩尾, 康範× 平池, 美香子× Kragh-Hansen, Ulrich× 米良, 克美× 野口, 大志× 安楽, 誠× 川井, 恵一× 丸山, 徹× 小田切, 優樹 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The pharmacokinetics of 17 genetic variants of human serum albumin with single-residue mutations and their corresponding normal albumin were studied in mice. In all cases, the plasma half-life was affected, but only variants with +2 changes in charge prolonged it, whereas changes in hydrophobicity decreased it. Good positive and negative correlations were found between changes in alpha-helical content taking place in domains I+III and domain II, respectively, and changes in half-lives. No correlation was found to type of mutation or to changes in heat stability as represented by DeltaH(v). Liver and kidney uptake clearances were also modified: alpha-helical changes of domains I+III showed good negative correlations to both types of clearances, whereas changes in domain II only had a good positive correlation to kidney uptake clearance. No correlation between the other molecular changes and organ uptakes was observed. The relatively few correlations between changes in molecular characteristics and the organ uptakes of the variants are most probably due to different handling by plasma enzyme(s) and the various types of cell endocytosis. Of the latter, most lead to destruction of albumin, but at least one results in recycling of the protein. The present information should be useful when designing recombinant, therapeutical albumins or albumin products with a modified plasma half-life. | |||||
| 内容記述 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | The pharmacokinetics of 17 genetic variants of human serum albumin with single-residue mutations and their corresponding normal albumin were studied in mice. In all cases, the plasma half-life was affected, but only variants with +2 changes in charge prolonged it, whereas changes in hydrophobicity decreased it. Good positive and negative correlations were found between changes in alpha-helical content taking place in domains I+III and domain II, respectively, and changes in half-lives. No correlation was found to type of mutation or to changes in heat stability as represented by DeltaH(v). Liver and kidney uptake clearances were also modified: alpha-helical changes of domains I+III showed good negative correlations to both types of clearances, whereas changes in domain II only had a good positive correlation to kidney uptake clearance. No correlation between the other molecular changes and organ uptakes was observed. The relatively few correlations between changes in molecular characteristics and the organ uptakes of the variants are most probably due to different handling by plasma enzyme(s) and the various types of cell endocytosis. Of the latter, most lead to destruction of albumin, but at least one results in recycling of the protein. The present information should be useful when designing recombinant, therapeutical albumins or albumin products with a modified plasma half-life. | |||||
| 書誌情報 |
福山大学薬学部研究年報 en : Annual report of the Faculty of Pharmacy & Pharmaceutical Sciences, Fukuyama University 号 27, p. 44-44, 発行日 2009-12-25 |
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| 出版者 | ||||||
| 出版者 | 福山大学薬学部 | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0288-724X | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN10064550 | |||||
