Structure-function studies on the biosynthesis and bioactivity of the precursor convertase PC2 and the formation of the PC2/7B2 complex
| Autor: | N. G. Seidah, M. Chrétien, J. Lusson, Diane Savaria, Suzanne Benjannet, Josée Hamelin |
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| Rok vydání: | 1995 |
| Předmět: |
endocrine system
Pro-Opiomelanocortin Mutant Biophysics Prohormone convertase Nerve Tissue Proteins Chaperone Biology Biosynthesis Transfection Biochemistry Cell Line Neuroendocrine Protein 7B2 Mice Neuroendocrine Secretory Protein 7B2 Structure-Activity Relationship PC2 Structural Biology Genetics Biomarkers Tumor Animals 7B2 Subtilisins Protein Precursors Site-directed mutagenesis Molecular Biology Immunosorbent Techniques RGD motif Furin Serine Endopeptidases Wild type Cell Biology Neoplasm Proteins Pituitary Hormones Proprotein Convertase 2 Oxyanion hole Mutagenesis Zymogen activation Mutagenesis Site-Directed Proprotein Convertases hormones hormone substitutes and hormone antagonists |
| Zdroj: | FEBS letters. 362(2) |
| ISSN: | 0014-5793 |
| Popis: | Site directed mutagenesis of the prohormone convertase PC2 was used to define the effect of certain residues on the zymogen activation of proPC2 and on its binding to the neuroendocrine protein 7B2. These included the oxyanion hole Asp309 (D309N), the N-terminal Glu25 (E25Q and E25K) of proPC2 and the Asp519 (D519E) of the RGD motif within the P-domain of PC2. Heterologous vaccinia virus expression of the wild type and mutant PC2's in endocrine pituitary cells such as AtT20 and GH3 cells demonstrated that the most dramatic effect was observed with the D309N mutant which no longer bound pro7B2 and which exhibited a significant reduction in its capacity to produce β-endorphin from pro-opiomelanocortin (POMC). |
| Databáze: | OpenAIRE |
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