2013年11月
Big angiotensin-25: A novel glycosylated angiotensin-related peptide isolated from human urine
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- 巻
- 441
- 号
- 4
- 開始ページ
- 757
- 終了ページ
- 762
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2013.10.124
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
The renin-angiotensin system (RAS), including angiotensin II (Ang II), plays an important role in the regulation of blood pressure and body fluid balance. Consequently, the RAS has emerged as a key target for treatment of kidney and cardiovascular disease. In a search for bioactive peptides using an antibody against the N-terminal portion of Ang II, we identified and characterized a novel angiotensin-related peptide from human urine as a major molecular form. We named the peptide Big angiotensin-25 (Bang-25) because it consists of 25 amino acids with a glycosyl chain and added cysteine. Bang-25 is rapidly cleaved by chymase to Ang II, but is resistant to cleavage by renin. The peptide is abundant in human urine and is present in a wide range of organs and tissues. In particular, immunostaining of Bang-25 in the kidney is specifically localized to podocytes. Although the physiological function of Bang-25 remains uncertain, our findings suggest it is processed from angiotensinogen and may represent an alternative, renin-independent path for Ang II synthesis in tissue. (C) 2013 Published by Elsevier Inc.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbrc.2013.10.124
- ISSN : 0006-291X
- eISSN : 1090-2104
- Web of Science ID : WOS:000328434800011