Big angiotensin-25: A novel glycosylated angiotensin-related peptide isolated from human urine |
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Authors: | Sayaka Nagata Kinta Hatakeyama Maki Asami Mariko Tokashiki Hajime Hibino Yuji Nishiuchi Kenji Kuwasako Johji Kato Yujiro Asada Kazuo Kitamura |
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Institution: | 1. Circulatory and Body Fluid Regulation, Faculty of Medicine, University of Miyazaki, Kiyotake, Miyazaki 889-1692, Japan;2. Pathology, Faculty of Medicine, University of Miyazaki, Kiyotake, Miyazaki 889-1692, Japan;3. SAITO Research Center, Peptide Institute, Inc., Ibaraki, Osaka 567-0085, Japan;4. Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan;5. Frontier Science Research Center, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki, Miyazaki 889-1692, Japan |
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Abstract: | 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. |
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Keywords: | Bigangiotensin-25 Renin&ndash angiotensin system Glycosyl chain Angiotensinogen |
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