VPARPVault Poly (ADP-Ribose) Polymerase (protein)
References in periodicals archive ?
(2004) Cryoelectron microscopy imaging of recombinant and tissue derived vaults: Localization of the MVP N termini and VPARP. J.
(1999) The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase.
Abbreviations: CFTR: cystic fibrosis transmembrane conductance regulator; EGF: epidermal growth factor; MVP: major vault protein, NCS: noncrystallographic symmetry; NMR: nuclear magnetic resonance; VPARP: vault poly(ADP-ribose) polymerase; SPFH: stomatin-prohibitin-flotillin-HflK-C; PEG: polyethylene glycol; vRNA: Vault RNA; SH2: Src homology 2; TEP1: telomerase-associated protein 1; IFN-[gamma]: interferon [gamma].
residues weight or bases (kDa) MVP rat 861 95,798 11 human 893 99,327 12 vPARP human 1,724 192,595 5 TEP1 rat 2,629 291,708 6, 13 human 2,627 290,490 6, 14 vRNA rat 141 47,686 15 human 8 hvg1 98 32,994 hvg2 88 29,612 hvg3 88 29,544 Table 2.
To investigate the relationship between Octopus actin (Oct-actin) and VPARP, we performed a turbidometric assay.
When considering that our understanding of vertebrate physiology greatly benefited from the subcellular analysis of the cephalopod nervous system, as shown by the discovery of the ionic bases of action potentials and of the [Ca.sup.2+] requirement for neurotransmitter release (18), it will be important to investigate whether VPARP may regulate the state of actin polymerization in other cell systems.
Since learning requires a period of consolidation and we detected the VPARP hyper-activation in trained octopuses in both OL and VSF, we suggest that VPARP might work in the neural circuitry responsible for memory consolidation.