کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10757555 | 1050396 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Big angiotensin-25: A novel glycosylated angiotensin-related peptide isolated from human urine
ترجمه فارسی عنوان
آنژیوتانسین 25 بزرگ: پپتید مرتبط با آنژیوتانسین گلیکوزیل شده جدا شده از ادرار انسان
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 441, Issue 4, 29 November 2013, Pages 757-762
Journal: Biochemical and Biophysical Research Communications - Volume 441, Issue 4, 29 November 2013, Pages 757-762
نویسندگان
Sayaka Nagata, Kinta Hatakeyama, Maki Asami, Mariko Tokashiki, Hajime Hibino, Yuji Nishiuchi, Kenji Kuwasako, Johji Kato, Yujiro Asada, Kazuo Kitamura,