Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer
Peptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of th...
| Autores: | , , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2017 |
| País: | Ecuador |
| Institución: | Universidad Regional Amazónica |
| Repositorio: | Repositorio Universidad Regional Amazónica |
| OAI Identifier: | oai:repositorio.ikiam.edu.ec:RD_IKIAM/130 |
| Acceso en línea: | https://doi.org/10.1016/j.euprot.2017.02.001 http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/130 |
| Access Level: | acceso abierto |
| Palabra clave: | Kazal-type proteinase inhibitors Frog skin secretion Peptidomic Molecular cloning Tandem mass spectrometry Cruziohyla calcarifer |
| Sumario: | Peptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern C-X(7)-C-X(6,7)-C-X(6,7)-Y-X(3)-C-X(2)-C-X(15-21)-C and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These peptidase inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions. |
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