Big angiotensin-25 : A novel glycosylated angiotensin-related peptide isolated from human urine
Big angiotensin-25 : A novel glycosylated angiotensin-related peptide isolated from human urine
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Big angiotensin-25:从人尿中分离出的一种新型糖基化血管紧张素相关肽
DOI:
10.1016/j.bbrc.2013.10.124
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发表时间:
2013
期刊:
影响因子:
--
通讯作者:
Kitamura K
中科院分区:
文献类型:
--
作者:
Nagata S;Hatakeyama K;Asami M;Tokashiki M;Hibino H;Nishiuchi Y;Kuwasako K;Kato J;Asada Y;Kitamura K
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.