The excision of N terminal two amino acids of a novel human parathyroid hormone analog with dipeptidylpeptidase
- DOI
- 10.2991/ifeesd-16.2016.98How to use a DOI?
- Keywords
- human Parathyroid hormone, analog, dipeptidyl peptidase, enzymatic reaction, prodrug.
- Abstract
Pro-Pro-[Arg11]hPTH(1-34)-Pro-Pro-Asp (hPTH') is more effective than hPTH(1-34) in the treatment of osteoporosis in our previous studies. The hypothesis that the active form of hPTH' was introduced by the excision with dipeptidyl peptidase IV (DPPIV) in vivo was validated in the present study. Following the determinations of DPPIV activities in rats tissues and serum, the N-terminus dipeptides of hPTH' were excised by DPPIV in rats tissues and serum and the excision production was determined by Tris-Tricine-SDS-PAGE. The results indicated that the N-terminus dipeptides of hPTH' could be excised with DPPIV in rats tissues and serum. The molecular weight of excision production was greater than that of hPTH (1-34) and less than that of hPTH'. In addition, the excision production was injected to mice for detecting its effect on serum calcium of mice. The results suggested that the serum calcium levels of mice treated with hPTH' were similar with those of mice treated with hPTH (1-34). In conclusion, appearing to function as a prodrug, the active form of hPTH' was introduced by the excision with DPPIV in vivo.
- Copyright
- © 2016, the Authors. Published by Atlantis Press.
- Open Access
- This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).
Cite this article
TY - CONF AU - Jiao Feng AU - Yan Zhu AU - Shuang Gao AU - Lihua Sun AU - Shuyan Ren AU - Tian Hong PY - 2016/05 DA - 2016/05 TI - The excision of N terminal two amino acids of a novel human parathyroid hormone analog with dipeptidylpeptidase BT - Proceedings of the 2016 International Forum on Energy, Environment and Sustainable Development PB - Atlantis Press SP - 545 EP - 549 SN - 2352-5401 UR - https://doi.org/10.2991/ifeesd-16.2016.98 DO - 10.2991/ifeesd-16.2016.98 ID - Feng2016/05 ER -