PED (Phosphoprotein Enriched in Diabetes) is an ubiquitously expressed 15 kDa cytosolic protein with recognized multiple functions. It has been demonstrated that PED has broad anti-apoptotic properties1,2 and, by altering insulin secretion, has a proven implication in diabetes3. In cultured cells and in transgenic mice, PED overexpression induces insulin-resistance and impairs glucose tolerance. Recent evidence indicates that increased interaction of PED with Phospholipase D1 (hPLD1) is a key event leading to these abnormalities in vivo and that this interaction is mediated by a C-terminal domain of PLD1 comprising residues 712–1070, D44. To further study this interaction, we prepared the recombinant proteins/sub-domains and after purification and preliminary characterization by CD, we measured the KDby SPR. Furthermore, following an approach of protein fragmentation and peptide fractionation we have been able to identify regions on PED that are involved in the...
Peptide antagonists of the PED-hPLD1 binding / Viparelli, F; Doti, N; Monti, S M; Marasco, D; Dathan, N; Pedone, C; Miele, C; Formisano, P; Beguinot, F; Ruvo, M. - In: ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY. - 611:(2009), pp. 445-446. [10.1007/978-0-387-73657-0_192]
Peptide antagonists of the PED-hPLD1 binding
Doti, N;Marasco, D;Pedone, C;Miele, C;Formisano, P;Beguinot, F;Ruvo, M
2009
Abstract
PED (Phosphoprotein Enriched in Diabetes) is an ubiquitously expressed 15 kDa cytosolic protein with recognized multiple functions. It has been demonstrated that PED has broad anti-apoptotic properties1,2 and, by altering insulin secretion, has a proven implication in diabetes3. In cultured cells and in transgenic mice, PED overexpression induces insulin-resistance and impairs glucose tolerance. Recent evidence indicates that increased interaction of PED with Phospholipase D1 (hPLD1) is a key event leading to these abnormalities in vivo and that this interaction is mediated by a C-terminal domain of PLD1 comprising residues 712–1070, D44. To further study this interaction, we prepared the recombinant proteins/sub-domains and after purification and preliminary characterization by CD, we measured the KDby SPR. Furthermore, following an approach of protein fragmentation and peptide fractionation we have been able to identify regions on PED that are involved in the...I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
