title: Vault-poly-ADP-ribose polymerase in the Octopus vulgaris brain: a regulatory factor of actin polymerization dynamic.
abstract: Our previous behavioural, biochemical and immunohistochemical analyses conducted in selected regions (supra/sub oesophageal masses) of the Octopus vulgaris brain detected a cytoplasmic poly-ADP-ribose polymerase (more than 90% of total enzyme activity). The protein was identified as the vault-free form of vault-poly-ADP-ribose polymerase. The present research extends and integrates the biochemical characterization of poly-ADP-ribosylation system, namely, reaction product, i.e., poly-ADP-ribose, and acceptor proteins, in the O. vulgaris brain. Immunochemical analyses evidenced that the sole poly-ADP-ribose acceptor was the octopus cytoskeleton 50-kDa actin. It was present in both free, endogenously poly-ADP-ribosylated form (70kDa) and in complex with V-poly-ADP-ribose polymerase and poly-ADP-ribose (260kDa). The components of this complex, alkali and high salt sensitive, were purified and characterized. The kind and the length of poly-ADP-ribose corresponded to linear chains of 30-35 ADP-ribose units, in accordance with the features of the polymer synthesized by the known vault-poly-ADP-ribose polymerase. In vitro experiments showed that V-poly-ADP-ribose polymerase activity of brain cytoplasmic fraction containing endogenous actin increased upon the addition of commercial actin and was highly reduced by ATP. Anti-actin immunoblot of the mixture in the presence and absence of ATP showed that the poly-ADP-ribosylation of octopus actin is a dynamic process balanced by the ATP-dependent polymerization of the cytoskeleton protein, a fundamental mechanism for synaptic plasticity.
authors.affiliation: Biochemistry, Department of Biology, University of Naples Federico II, 80126, Naples, Italy.
authors.forename: Anna
authors.initials: A
authors.lastname: De Maio
authors.forename: Emiliana
authors.initials: E
authors.lastname: Natale
authors.forename: Sergio
authors.initials: S
authors.lastname: Rotondo
authors.forename: Anna
authors.initials: A
authors.lastname: Di Cosmo
authors.forename: Maria Rosaria
authors.initials: MR
authors.lastname: Faraone-Mennella
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D009473:Neuronal Plasticity / Q000235:genetics; D049831:Octopodiformes / Q000201:enzymology*; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry / Q000378:metabolism*; D058105:Polymerization; D013569:Synapses / Q000378:metabolism / Q000502:physiology; D020394:Vault Ribonucleoprotein Particles / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000199:Actins; D020394:Vault Ribonucleoprotein Particles; D011064:Poly Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases; C449359:vault poly(ADP-ribose) polymerase
keywords: Brain; Oct-actin; Octopus; Poly-ADP-ribose; VPARP