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- 須藤 純一
- 東京大学医学部薬理学教室
書誌事項
- タイトル別名
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- Distributions of peptidases in the metabolization of peptide hormones, particularly angiotensin II, along the isolated single nephron of rat
- ラット ジン ネフロン ニ オケル ペプチド ホルモン ノ ブンカイ コウソ
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説明
The present study was undertaken to investigate the peptidases which degrade peptide hormones, particularly angiotensin II (AII), in the isolated rat nephron segments. These peptidases include leucine aminopeptidase, aminopeptidase A, cystine aminopeptidase, “trypsin-like enzyme(s)”, “chymotrypsin-like enzyme(s)”, postproline cleaving enzyme, and converting enzyme. The metabolic ability of [3H]-AII in each nephron segment, was also studied. The activities of these peptidases were exclusively higher in proximal tubules than in other segments. In the proximal tubule, only “trypsin-like enzyme(s)” showed the highest activity in pars convoluta, however, the other peptidases showed the highest activities in pars recta. The activities of aminopeptidase A, “trypsin-like enzyme(s)”, and post-proline cleaving enzyme, were also high in the glomerulus. The activities of these peptidases were hardly detectable in distal nephron segments. From the investigation of the metabolic ability of [3H]-AII in each nephron segment, AII was found to be highly metabolized both in the glomerulus and in the proximal tubule, especially in the pars recta. AII was converted to angiotensin III (AIII) mainly in the glomerulus. All these findings suggest that peptide hormones including AII filtrated through the glomerulus are metabolized in the proximal tubule and that the conversion from AII to AIII occurs mainly in the glomerulus.
収録刊行物
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- 日本薬理学雑誌
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日本薬理学雑誌 78 (1), 27-44, 1981
公益社団法人 日本薬理学会
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詳細情報 詳細情報について
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- CRID
- 1390282679249026560
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- NII論文ID
- 130000759414
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- NII書誌ID
- AN00198335
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- COI
- 1:CAS:528:DyaL3MXkslOnurs%3D
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- ISSN
- 13478397
- 00155691
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- NDL書誌ID
- 2356242
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- PubMed
- 7308897
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可