Romani R

References (14)

Title : Anandamide and its congeners inhibit human plasma butyrylcholinesterase. Possible new roles for these endocannabinoids? - Romani_2011_Biochimie_93_1584
Author(s) : Romani R , Galeazzi R , Rosi G , Fiorini R , Pirisinu I , Ambrosini A , Zolese G
Ref : Biochimie , 93 :1584 , 2011
Abstract : Butyrylcholinesterase (BChE), a serine hydrolase biochemically related to the cholinergic enzyme Acetylcholinesterase (AChE), is found in many mammalian tissues, such as serum and central nervous system, but its physiological role is still unclear. BChE is an important human plasma esterase, where it has detoxifying roles. Furthermore, recent studies suggest that brain BChE can have a role in Alzheimer's disease (AD). The endocannabinoid arachidonoylethanolamide (anandamide) and other acylethanolamides (NAEs) are almost ubiquitary molecules and are physiologically present in many tissues, including blood and brain, where they show neuroprotective and anti-inflammatory properties. This paper demonstrates that they are uncompetitive (oleoylethanolamide and palmitoylethanolamide) or non competitive (anandamide) inhibitors of BChE (Ki in the range 1.32-7.48 nM). On the contrary, NAEs are ineffective on AChE kinetic features. On the basis of the X-ray crystallographic structure of human BChE, and by using flexible docking procedures, an hypothesis on the NAE-BChE interaction is formulated by molecular modeling studies. Our results suggest that anandamide and the other acylethanolamides studied could have a role in the modulation of the physiological actions of BChE.
ESTHER : Romani_2011_Biochimie_93_1584
PubMedSearch : Romani_2011_Biochimie_93_1584
PubMedID: 21664223

Title : Organophosphate-resistant forms of acetylcholinesterases in two scallops--the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus - Romani_2006_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_145_188
Author(s) : Romani R , Corsi I , Bonacci S , Focardi S , De Medio GE , De Santis A , Incarnato F , Giovannini E , Rosi G
Ref : Comparative Biochemistry & Physiology B Biochem Mol Biol , 145 :188 , 2006
Abstract : We describe the acetylcholinesterase polymorphisms of two bivalve molluscs, Adamussium colbecki and Pecten jacobaeus. The research was aimed to point out differences in the expression of pesticide-resistant acetylcholinesterase forms in organisms living in different ecosystems such as the Ross Sea (Antarctica) and the Mediterranean Sea. In A. colbecki, distinct acetylcholinesterase molecular forms were purified and characterized from spontaneously soluble, low-salt-soluble and low-salt-Triton extracts from adductor muscle and gills. They consist of two non-amphiphilic acetylcholinesterases (G(2), G(4)) and an amphiphilic-phosphatidylinositol-membrane-anchored form (G(2)); a further amphiphilic-low-salt-soluble G(2) acetylcholinesterase was found only in adductor muscle. In the corresponding tissues of P. jacobaeus, we found a non-amphiphilic G(4) and an amphiphilic G(2) acetylcholinesterase; amphiphilic-low-salt-soluble acetylcholinesterases (G(2)) are completely lacking. Such results are related with differences in cell membrane lipid compositions. In both scallops, all non-amphiphilic AChEs are resistant to used pesticides. Differently, the adductor muscle amphiphilic forms are resistant to carbamate eserine and organophosphate diisopropylfluorophosphate, but sensitive to organophoshate azamethiphos. In the gills of P. jacobaeus, amphiphilic G(2) forms are sensitive to all three pesticides, while the corresponding forms of A. colbecki are sensitive to eserine and diisopropylfluorophosphate, but resistant to azamethiphos. Results indicate that organophosphate and/or carbamate resistant AChE forms are present in species living in far different and far away environments. The possibility that these AChE forms could have ensued from a common origin and have been spread globally by migration is discussed.
ESTHER : Romani_2006_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_145_188
PubMedSearch : Romani_2006_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_145_188
PubMedID: 16931084

Title : Effects of chlorpyrifos on the catalytic efficiency and expression level of acetylcholinesterases in the bivalve mollusk Scapharca inaequivalvis - Romani_2005_Environ.Toxicol.Chem_24_2879
Author(s) : Romani R , Isani G , De Santis A , Giovannini E , Rosi G
Ref : Environ Toxicol Chem , 24 :2879 , 2005
Abstract : Three acetylcholinesterase (AChE) forms were detected and recovered from foot or gill tissues of the benthonic bivalve mollusk Scapharca inaequivalvis. A study was performed to investigate changes in catalytic and hydrodynamic features of these enzymes, as well as in their expression levels, after a 4-d or a 15-d exposure to a sublethal concentration (0.1 microl/L) of the pesticide chlorpyrifos (CPF). Both considered organs hold, in either CPF-exposed or untreated animals, two nonamphiphilic AChE forms, G2 and G4, which copurified on a procainamide-containing affinity gel and were separated by density gradient centrifugation. A third AChE form, an amphiphilic membrane-anchored G2, was also purified on the same affinity matrix from both organs. All enzymatic forms are true AChEs and are poorly inhibited by CPE They show different increases in the maximum velocity (Vmax) and in the Michaelis constant (Km) values after CPF exposure. Consequently, catalytic efficiency of AChEs, as defined by the ratio Vmax:Km, rises in the gills and drops in the foot. This would produce an overexpression of AChE-specific mRNAs. The effect was longer lasting in the foot. The combined results indicate that overexpression of enzymes in the presence of organophosphate (OP) may be a consequence of OP resistance itself. Again, the resistance of the organism to CPF seem to depend mainly on the resulting increase in AChE content.
ESTHER : Romani_2005_Environ.Toxicol.Chem_24_2879
PubMedSearch : Romani_2005_Environ.Toxicol.Chem_24_2879
PubMedID: 16398125

Title : Increased acetylcholinesterase activities in specimens of Sparus auratus exposed to sublethal copper concentrations - Romani_2003_Chem.Biol.Interact_145_321
Author(s) : Romani R , Antognelli C , Baldracchini F , De Santis A , Isani G , Giovannini E , Rosi G
Ref : Chemico-Biological Interactions , 145 :321 , 2003
Abstract : The present study looks at possible changes in the activity of acetylcholinesterase (AChE) in tissues (brain and white muscle) of the Mediterranean bony fish Sparus auratus after a 20 days exposure to sublethal concentrations (0.1 or 0.5 ppm) of copper in the marine water and on control untreated animals. The trials also included measurements of Cu concentration in the tissues to evaluate possible metal accumulation. Moreover, sedimentation analysis as well as V(max) and K(m) determination were carried out in tissue extracts of Cu-exposed or control animals. V(max) and K(m) were also determined with or without addition of Cu(2+) in the assay. No Cu accumulation occurred in brain and muscle after Cu exposure. AChE showed in both tissues a molecular polymorphism with putative globular (G) and asymmetric (A) forms. Cu exposition led to an increased specific activity and improved catalytic efficiency of AChE in brain and muscle, seemingly regarding G forms. The increase in catalytic efficiency also resulted from the in vitro assay with tissue extracts and Cu(2+) addition. The higher AChE activity and catalytic efficiency in both tissues after Cu exposition and without metal accumulation, suggests an increase of free Cu aliquot into the cells, likely due to mechanisms of metal homeostasis.
ESTHER : Romani_2003_Chem.Biol.Interact_145_321
PubMedSearch : Romani_2003_Chem.Biol.Interact_145_321
PubMedID: 12732458

Title : Different expressions of organophosphate-resistant acetylcholinesterases in the bivalve mollusk Scapharca inaequivalvis living in three different habitats - Talesa_2002_Environ.Toxicol.Chem_21_102
Author(s) : Talesa V , Romani R , Antognelli C , Giovannini E , Rosi G
Ref : Environ Toxicol Chem , 21 :102 , 2002
Abstract : The benthic mollusk Scapharca inaequivalvis was collected in spring 1999 from three areas of the northern Adriatic Sea From the mollusk molecular forms of acetylcholinesterase AChE consisting of two prevailing spontaneously soluble SS forms present in the blood were obtained These forms are a globular tetramer SSG4 a dimer SSG2 of catalytic subunits and a minor amphiphilic globular dimer low-salt Triton LST G2 phosphatidylinositol tailed All SS and LST forms partially purified by affinity chromatography are AChEs with a marked substrate specificity for acetylthiocholine and poor hydrolysis with butyrylthiocholine They are poorly inhibited by carbamate eserine and show a different pattern of inhibition by organophosphate diisopropylfluorophosphate DFP with totally resistant SS forms from clams collected from the two stations nearest the Po River Acetylcholinesterase SS and LST forms are expressed at highest lowest and middle levels in clams collected from the northern station closer to the Po delta and from the two more southern ones respectively The possibility that the expression pattern of AChE forms is due to effects of single or mixed classes of chemical pollutants is discussed
ESTHER : Talesa_2002_Environ.Toxicol.Chem_21_102
PubMedSearch : Talesa_2002_Environ.Toxicol.Chem_21_102
PubMedID: 11804042

Title : Cerebrospinal fluid acetylcholinesterase activity after long-term treatment with donepezil and rivastigmina - Amici_2001_Mech.Ageing.Dev_122_2057
Author(s) : Amici S , Lanari A , Romani R , Antognelli C , Gallai V , Parnetti L
Ref : Mech Ageing Dev , 122 :2057 , 2001
Abstract : At present acetylcholinesterase (AChE) inhibitors (AChEIs) represent the only reliable therapeutic resource for symptomatic treatment of Alzheimer Disease (AD). This study was designed to assess the effects of 6-12 month treatment with AChEIs donepezil and rivastigmine on cerebrospinal fluid (CSF) AChE and butyrylcholinesterase (BuChE) activity in AD patients. The pattern of AChE isoforms (G4, G1, G2) before and after treatment was investigated as well. In AD patients treated with donepezil a significant increase of CFS AChE activity was observed, whereas treatment with rivastigmine induced a significant decrease of AChE activity. Both drugs did not change BuChE activity and tended to restore the physiological pattern of AChE isoform. The possible significance of the influence of AChEIs on CSF AChE activity and isoforms is discussed.
ESTHER : Amici_2001_Mech.Ageing.Dev_122_2057
PubMedSearch : Amici_2001_Mech.Ageing.Dev_122_2057
PubMedID: 11589922

Title : Soluble and membrane-bound acetylcholinesterases in Mytilus galloprovincialis (Pelecypoda: Filibranchia) from the northern Adriatic sea - Talesa_2001_Chem.Biol.Interact_134_151
Author(s) : Talesa V , Romani R , Antognelli C , Giovannini E , Rosi G
Ref : Chemico-Biological Interactions , 134 :151 , 2001
Abstract : Three forms of acetylcholinesterase (AChE) were detected in samples of the bivalve mollusc Mytilus galloprovincialis collected in sites of the Adriatic sea. Apart from the origin of the mussels, two spontaneously soluble (SS) AChE occur in the hemolymph and represent about 80% of total activity, perhaps hydrolyzing metabolism-borne choline esters. These hydrophilic enzymes (forms A and B) copurified by affinity chromatography (procainamide-Sepharose gel) and were separated by sucrose gradient centrifugation. They are, respectively, a globular tetramer (11.0-12.0 S) and a dimer (6.0-7.0 S) of catalytic subunits. The third form, also purified from tissue extracts by the same affinity matrix, proved to be an amphiphilic globular dimer (7.0 S) with a phosphatidylinositol tail giving cell membrane insertion, detergent (Triton X-100, Brij 96) interaction and self-aggregation. Such an AChE is likely functional in cholinergic synapses. All three AChE forms show a good substrate specificity and are inactive on butyrylthiocholine. Studies with inhibitors showed low inhibition by eserine and paraoxon, especially on SS forms, high sensitivity to 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide (BW284c51) and no inhibition with propoxur and diisopropylfluorophosphate (DFP). The ChE forms in M. galloprovincialis are possibly encoded by different genes. Some kinetic features of these enzymes suggest a genetic polymorphism.
ESTHER : Talesa_2001_Chem.Biol.Interact_134_151
PubMedSearch : Talesa_2001_Chem.Biol.Interact_134_151
PubMedID: 11311211

Title : Molecular cloning and expression of a full-length cDNA encoding acetylcholinesterase in optic lobes of the squid Loligo opalescens: a new member of the cholinesterase family resistant to diisopropyl fluorophosphate - Talesa_1999_J.Neurochem_72_1250
Author(s) : Talesa V , Grauso M , Arpagaus M , Giovannini E , Romani R , Rosi G
Ref : Journal of Neurochemistry , 72 :1250 , 1999
Abstract : Acetylcholinesterase cDNA was cloned by screening a library from Loligo opalescens optic lobes; cDNA sequence analysis revealed an open reading frame coding for a protein of 610 amino acids that showed 20-41% amino acid identity with the acetylcholinesterases studied so far. The characteristic structure of cholinesterase (the choline binding site, the catalytic triad, and six cysteines that form three intrachain disulfide bonds) was conserved in the protein. The heterologous expression of acetylcholinesterase in COS cells gave a recovery of acetylcholinesterase activity 20-fold higher than in controls. The enzyme, partially purified by affinity chromatography, showed molecular and kinetic features indistinguishable from those of acetylcholinesterase expressed in vivo, which displays a high catalytic efficiency. Both enzymes are true acetylcholinesterase corresponding to phosphatidylinositol-anchored G2a dimers of class I, with a marked substrate specificity for acetylthiocholine. The deduced amino acid sequence may explain some particular kinetic characteristics of Loligo acetylcholinesterase, because the presence of a polar amino acid residue (S313) instead of a nonpolar one [F(288) in Torpedo] in the acyl pocket of the active site could justify the high substrate specificity of the enzyme, the absence of hydrolysis with butyrylthiocholine, and the poor inhibition by the organophosphate diisopropyl fluorophosphate.
ESTHER : Talesa_1999_J.Neurochem_72_1250
PubMedSearch : Talesa_1999_J.Neurochem_72_1250
PubMedID: 10037498
Gene_locus related to this paper: lolop-ACHE1

Title : Four Acetylcholinesterase Genes in the Nematodes caenorhabditis Elegans and Caenorhabditis Briggsae -
Author(s) : Culetto E , Grauso M , Combes D , Fedon Y , Romani R , Toutant JP , Arpagaus M
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :87 , 1998
PubMedID:

Title : Four acetylcholinesterase genes in the nematode Caenorhabditis elegans - Arpagaus_1998_J.Physiol.Paris_92_363
Author(s) : Arpagaus M , Combes D , Culetto E , Grauso M , Fedon Y , Romani R , Toutant JP
Ref : Journal de Physiologie (Paris) , 92 :363 , 1998
Abstract : Whereas a single gene encodes acetylcholinesterase (AChE) in vertebrates and most insect species, four distinct genes have been cloned and characterized in the nematode Caenorhabditis elegans. We found that ace-1 (mapped to chromosome X) is prominently expressed in muscle cells whereas ace-2 (located on chromosome I) is mainly expressed in neurons. Ace-x and ace-y genes are located in close proximity on chromosome II where they are separated by only a few hundred base pairs. The role of these two genes is still unknown.
ESTHER : Arpagaus_1998_J.Physiol.Paris_92_363
PubMedSearch : Arpagaus_1998_J.Physiol.Paris_92_363
PubMedID: 9789838

Title : Four Acetylcholinesterase Genes in the Nematode Caenorhabditis Elegans - 1 -
Author(s) : Combes D , Culetto E , Grauso M , Romani R , Fedon Y , Toutant JP , Arpagaus M
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :136 , 1998
PubMedID:

Title : Acetylcholinesterase at high catalytic efficiency and substrate specificity in the optic lobe of Eledone moschata (Cephalopoda: Octopoda): biochemical characterization and histochemical localization - Talesa_1998_Neurochem.Int_33_131
Author(s) : Talesa V , Romani R , Calvitti M , Rosi G , Giovannini E
Ref : Neurochem Int , 33 :131 , 1998
Abstract : In the optic lobe of the cephalopod mollusc Eledone moschata, two acetylcholinesterase forms I and II were detected, both showing a marked active site specificity with differently sized substrates. Catalytic efficiency (kcat/Km) of the prevailing form II is similar to that of acetylcholinesterases from vertebrate nervous system. Enzyme forms I and II were co-purified from a high-salt-Triton X-100 soluble extract of optic lobe by consecutive affinity chromatographies on procainamide- and concanavalin A-Sepharose columns and then separately obtained by preparative density gradient centrifugation. According to gel-filtration chromatography, sedimentation analysis and SDS-PAGE, the major form II is an amphiphilic globular dimer (135-136 kDa, 6.3-7.4 S) of monomers (66 kDa) S-S linked between terminal segments. Phosphatidylinositol anchors give cell membrane insertion, self-aggregation and detergent (Triton X-100, Brij 97) interaction. Form I, characterized only in part owing to its small amount, showed molecular size (129 kDa) and sedimentation coefficient (7.5 S) similar to those of form II; it is likely to be attached to the cell membrane by electrostatic interactions. Both forms behaved similarly with various inhibitors and underwent excess-substrate inhibition. The results obtained suggest a common origin of both form I and II from a single gene. The former could be a degradation product of the prevailing one (II), which is likely to be functional in cholinergic synapses.
ESTHER : Talesa_1998_Neurochem.Int_33_131
PubMedSearch : Talesa_1998_Neurochem.Int_33_131
PubMedID: 9761457

Title : Expression of a single dimeric membrane-bound acetylcholinesterase in Parascaris equorum - Talesa_1997_Parasitology_115_653
Author(s) : Talesa V , Romani R , Grauso M , Rosi G , Giovannini E
Ref : Parasitology , 115 :653 , 1997
Abstract : A single form of cholinesterase was detected in the parasitic nematode Parascaris equorum and purified from a low-salt Triton X-100 extract of whole animals by affinity chromatography on an edrophonium-Sepharose matrix. Based on gel-filtration chromatography, sedimentation analysis and SDS-PAGE, such a cholinesterase is an amphiphilic globular (G2) dimer (125-129 kDa, 6.1 S). It includes some hydrophobic domain other than phosphatidylinositol, which gives autoaggregation, detergent interaction and also anchors the molecule to the cell membrane. The enzyme, probably functional in cholinergic neurotransmission, is an acetylcholinesterase showing a fairly low substrate specificity with thiocholine esters. Electrostatic interactions seem to play a major role in the catalytic activity. Studies with inhibitors gave complete inhibition with 1 mM eserine, low sensitivity for procainamide and for tetra(monoisopropyl)pyrophosphortetramide as well as higher inhibition with edrophonium chloride and 1,5-bis(4allyldimethylammoniumphenyl)-pentan-3-one dibromide. The enzyme also showed excess-substrate inhibition with acetylthiocholine. No cross-hybridization occurred between the gene(s) encoding acetylcholinesterase in P. equorum and ace-1 from the free-living nematode Caenorhabditis elegans. The expression of a single cholinesterase form in P. equorum, unusual in free-living nematodes, could be due to parasitic life adaptation with resulting reduction of locomotor activity.
ESTHER : Talesa_1997_Parasitology_115_653
PubMedSearch : Talesa_1997_Parasitology_115_653
PubMedID: 9488877

Title : Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is present with forms sensitive and insensitive to phosphatidylinositol phospholipase C. Biochemical characterization and histochemical localization in the nervous system - Talesa_1996_Eur.J.Biochem_238_538
Author(s) : Talesa V , Romani R , Rosi G , Giovannini E
Ref : European Journal of Biochemistry , 238 :538 , 1996
Abstract : Three distinct acetylcholinesterases were detected in the annelid oligochaete Dendrobaena veneta. Two enzymes (alpha, beta), copurified from a Triton-X-100-soluble extract of whole animals by affinity (edrophonium-Sepharose) chromatography, were separately eluted from a Sephadex G-200 column. Gel-filtration chromatography, sedimentation analysis and SDS/PAGE showed the alpha and beta forms to be a globular dimer (110 kDa, 7.0 S) and a hydrophilic monomer (58 kDa, 5.0 S) respectively, both weakly linked to the cell membrane. The third form (gamma), also purified to homogeneity by slower filtration through an edrophonium-Sepharose matrix, proved to be an amphiphilic globular dimer (133 kDa, 7.0 S) with a phosphatidylinositol anchor giving cell membrane insertion, detergent (Triton X-100, Brij 96) interaction and self-aggregation. The alpha acetylcholinesterase showed a fairly low substrate specificity: the beta form hydrolyzed propionylthiocholine at the highest rate and was inactive on butyrylthiocholine; the gamma acetylcholinesterase, showing a marked active-site specificity with differently sized substrates, was likely functional in cholinergic synapses. Studies with inhibitors showed incomplete inhibition of all three acetylcholinesterase by 1 mM eserine and different sensitivity for edrophonium or procainamide. The alpha and beta forms, sensitive to 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide, were unaffected by tetra(monoisopropyl)-pyrophosphortetramide, while both these agents inhibited the gamma enzyme. All three forms showed excess-substrate inhibition by acetylthiocholine. Enzyme activity was histochemically localized in the nerve ring and its minor branches. Monomeric acetylcholinesterase (beta) is likely the only form present in the ganglionic glial framework.
ESTHER : Talesa_1996_Eur.J.Biochem_238_538
PubMedSearch : Talesa_1996_Eur.J.Biochem_238_538
PubMedID: 8681969