Biological activity of FGF-23 fragments
| Autor: | Stephen J. O'Brien, Theresa J. Berndt, Marlon Pragnell, Beate Lanske, Rajiv Kumar, Theodore A. Craig, Mohammed S. Razzaque, Despina Sitara, Ann E. Bowe, Susan C. Schiavi, Daniel J. McCormick |
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| Rok vydání: | 2007 |
| Předmět: |
Male
Fibroblast growth factor 23 medicine.medical_specialty Physiology Molecular Sequence Data Clinical Biochemistry Peptide Kidney Article Cell Line Phosphates Rats Sprague-Dawley Excretion Mice Physiology (medical) Internal medicine medicine Animals Humans Amino Acid Sequence Vitamin D Receptor Fibroblast Mice Knockout chemistry.chemical_classification Chemistry Biological activity Opossums Peptide Fragments Rats Amino acid Fibroblast Growth Factors Fibroblast Growth Factor-23 medicine.anatomical_structure Endocrinology Potassium |
| Zdroj: | Pflügers Archiv - European Journal of Physiology. 454:615-623 |
| ISSN: | 1432-2013 0031-6768 |
| Popis: | The phosphaturic activity of intact, full-length, fibroblast growth factor-23 (FGF-23) is well documented. FGF-23 circulates as the intact protein, and as fragments generated as the result of proteolysis of the full-length protein. To assess whether short fragments of FGF-23 are phosphaturic, we compared the effect of acute, equimolar infusions of full-length FGF-23 and various FGF-23 fragments carboxyl-terminal to amino acid 176. In rats, intravenous infusions of full-length FGF-23, and FGF-23 176-251, significantly and equivalently increased fractional phosphate excretion (FE Pi)) from 14±3 to 32±5% and 15±2 to 33±2% (p |
| Databáze: | OpenAIRE |
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