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EnglishAngiogenin is a member of the ribonuclease family and a normal constituent of human plasma. It is one of the most potent angiogenic factors known and is overexpressed in different types of cancers. Copper is also an essential cofactor in angiogenesis and, during this process, it is mobilized from inside to outside of the cell. To date, contrasting results have been reported about copper(II) influencing angiogenin activity. However, in these studies, the recombinant form of the protein was used. Unlike recombinant angiogenin, that contains an extra methionine with a free terminal amino group, the naturally occurring protein present in human plasma starts with a glutamine residue that spontaneously cyclizes to pyroglutamate, a lactam derivative. Herein, we report spectroscopic evidence indicating that copper(II) experiences different coordination environments in the two protein isoforms, and affects their RNase and angiogenic activity differently. These results show how relatively small differences between recombinant and wild type proteins can result in markedly different behaviours.
| Autori interni: | |
| Autori: | LA MENDOLA, DIEGO; Arnesano, Fabio; Hansson, Örjan; GIACOMELLI, CHIARA; Calò, Vincenza; Mangini, Vincenzo; Magrì, Antonio; Bellia, Francesco; TRINCAVELLI, MARIA LETIZIA; MARTINI, CLAUDIA; Natile, Giovanni; Rizzarelli, Enrico |
| Titolo: | Copper binding to naturally occurring, lactam form of angiogenin differs from that to recombinant protein, affecting their activity |
| Anno del prodotto: | 2016 |
| Abstract: | Angiogenin is a member of the ribonuclease family and a normal constituent of human plasma. It is one of the most potent angiogenic factors known and is overexpressed in different types of cancers. Copper is also an essential cofactor in angiogenesis and, during this process, it is mobilized from inside to outside of the cell. To date, contrasting results have been reported about copper(II) influencing angiogenin activity. However, in these studies, the recombinant form of the protein was used. Unlike recombinant angiogenin, that contains an extra methionine with a free terminal amino group, the naturally occurring protein present in human plasma starts with a glutamine residue that spontaneously cyclizes to pyroglutamate, a lactam derivative. Herein, we report spectroscopic evidence indicating that copper(II) experiences different coordination environments in the two protein isoforms, and affects their RNase and angiogenic activity differently. These results show how relatively small differences between recombinant and wild type proteins can result in markedly different behaviours. |
| Digital Object Identifier (DOI): | 10.1039/C5MT00216H |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
File in questo prodotto:
| File | Descrizione | Tipologia | Licenza | |
|---|---|---|---|---|
| La Mendola_798363.pdf | Versione finale editoriale | NON PUBBLICO - Accesso privato/ristretto | Utenti riconosciuti Richiedi una copia | |
| Post-print Metallomics La Mendola 2016.pdf | Post-prints | Documento in Post-print | Tutti i diritti riservati (All rights reserved) | Open AccessVisualizza/Apri |
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