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117 results on '"MacCarrone M"'

10. Amine oxidase from Euphorbia characias: Kinetic and structural characterization

Author

Pintus, F, Sabatucci, A, Maccarrone, M, Dainese, E, and Medda, R

Subjects
Euphorbia characias, Kinetics, Molecular Structure, latex, Euphorbia, small-angle X-ray scattering, 2,4,5-trihydroxyphenyl alanine quinone, copper amine oxidases, human vascular adhesion protein-1, Amine Oxidase (Copper-Containing), 5-trihydroxyphenyl alanine quinone
Abstract

This minireview focuses on a plant copper/2,4,5-trihydroxyphenyl alanine quinone amine oxidase isolated from the latex of the shrub Euphorbia characias (ELAO). This enzyme has been investigated in terms of both molecular structure and kinetic mechanism. The characterization of this enzyme allowed us to identify specific amino acids and domains that play a key role in modulating substrate access into the active site not only for ELAO but also for other plant and mammalian amine oxidases. As mammalian amine oxidases are implicated in several physiological and pathological conditions, the deep structural characterization of their active site accession mechanisms could be the starting point for the development of enzyme modulators with high therapeutic potential. Thus, this paper gives structural/functional insights that open new perspectives in the research about the whole amine oxidase family.

Published
2017

11. In silico mapping of allosteric ligand binding sites in type-1 cannabinoid receptor

Author

Sabatucci, A, Tortolani, D, Dainese, E, and Maccarrone, M

Subjects
Allosteric modulators, CB1 binding, in silico mapping, Molecular Docking Simulation, Binding Sites, Receptor, Cannabinoid, CB1, Humans, Computer Simulation, Ligands, Hydrophobic and Hydrophilic Interactions, Allosteric Site
Abstract

The recent resolution of the crystal structure of type-1 cannabinoid receptor (CB

Published
2017

19. Subventricular zone neural progenitors protect striatal neurons from glutamatergic excitotoxicity

Author

Butti, E., Bacigaluppi, M., Rossi, S., Cambiaghi, M., Bari, M., Silla, A.C., Brambilla, E., Musella, A., Teneud, L., De Chiara, Garcia Verdugo, J.M. , Comi, LEOCANI , ANNUNZIATA MARIA LETIZIA, Maccarrone, M., Centonze, D., Martino, G., Butti, E., Bacigaluppi, M., Rossi, S., Cambiaghi, M., Bari, M., Silla, A. C., Brambilla, E., Musella, A., Teneud, L., De, Chiara, Garcia, Verdugo, J. M., Comi, Leocani, ANNUNZIATA MARIA LETIZIA, Maccarrone, M., Centonze, D., and Martino, G.

Published
2012

20. LETTER TO THE EDITOR

Author

Gironi M, Pasquariello N, Franchi S, Pucci M, Martinelli Boneschi F, Solaro C, Centonze D, Sacerdote P, Maccarrone M., MARTINO , GIANVITO, Gironi, M, Pasquariello, N, Franchi, S, Pucci, M, Martinelli Boneschi, F, Solaro, C, Centonze, D, Martino, Gianvito, Sacerdote, P, and Maccarrone, M.

Subjects
Male, Multiple Sclerosis, Gene Expression Regulation, Receptors, Brain, Female, Humans, Phospholipase D, Receptors, Cannabinoid, Cannabinoid
Published
2012

27. BIOCHIMICA 5° edizione

Author

Ascenzi, P, Battistoni, A, Carrì, Mt, Ciriolo, Mr, Contestabile, R, di Masi, A, di Salvo ML, Di Venere, A, Eufemi, M, Giacometti, Gm, Maccarrone, M, Mordente, A, Palestini, P, Pascarella, S, Polticelli, F, Rosato, N, Scatena, R, and Tavazzi, B

Published
2014

36. Epigenetic control of skin differentiation genes by phytocannabinoids

Author

Pucci, Mariangela, Rapino, Cinzia, DI FRANCESCO, Andrea, Dainese, Enrico, D'Addario, Claudio, and Maccarrone, M.

Subjects
Keratinocytes, Transglutaminases, Dose-Response Relationship, Drug, Transcription, Genetic, Cannabinoids, Phytochemicals, Down-Regulation, Cell Differentiation, DNA Methylation, Keratin-10, Research Papers, Cell Line, DNA Methyltransferase 3A, Epigenesis, Genetic, Cannabidiol, Humans, RNA, Messenger, Protein Precursors, Keratin-1, DNA Modification Methylases, Skin
Abstract

Endocannabinoid signalling has been shown to have a role in the control of epidermal physiology, whereby anandamide is able to regulate the expression of skin differentiation genes through DNA methylation. Here, we investigated the possible epigenetic regulation of these genes by several phytocannabinoids, plant-derived cannabinoids that have the potential to be novel therapeutics for various human diseases.The effects of cannabidiol, cannabigerol and cannabidivarin on the expression of skin differentiation genes keratins 1 and 10, involucrin and transglutaminase 5, as well as on DNA methylation of keratin 10 gene, were investigated in human keratinocytes (HaCaT cells). The effects of these phytocannabinoids on global DNA methylation and the activity and expression of four major DNA methyltransferases (DNMT1, 3a, 3b and 3L) were also examined.Cannabidiol and cannabigerol significantly reduced the expression of all the genes tested in differentiated HaCaT cells, by increasing DNA methylation of keratin 10 gene, but cannabidivarin was ineffective. Remarkably, cannabidiol reduced keratin 10 mRNA through a type-1 cannabinoid (CB1 ) receptor-dependent mechanism, whereas cannabigerol did not affect either CB1 or CB2 receptors of HaCaT cells. In addition, cannabidiol, but not cannabigerol, increased global DNA methylation levels by selectively enhancing DNMT1 expression, without affecting DNMT 3a, 3b or 3L.These findings show that the phytocannabinoids cannabidiol and cannabigerol are transcriptional repressors that can control cell proliferation and differentiation. This indicates that they (especially cannabidiol) have the potential to be lead compounds for the development of novel therapeutics for skin diseases.

Published
2013

41. Rat and human fatty acid amide hydrolases: overt similarities and hidden differences

Author

DI VENERE, A, Dainese, Fezza, F, F, Angelucci, B, Rosato, N, Cravatt, B, Finazzi Agrò, A, Mei, G, and Maccarrone, M

Subjects
Oleamide, Organophosphonates, Arachidonic Acids, Biology, Protein Structure, Secondary, Amidohydrolases, Substrate Specificity, chemistry.chemical_compound, Protein structure, Fatty acid amide hydrolase, Animals, Humans, Settore BIO/10, Enzyme Inhibitors, Molecular Biology, chemistry.chemical_classification, Fatty acid amide, Protein Stability, Fatty Acids, Fatty acid, Cell Biology, Anandamide, Rats, Kinetics, Enzyme, chemistry, Membrane protein, Biochemistry, lipids (amino acids, peptides, and proteins)
Abstract

Fatty acid amide hydrolase (FAAH) is a membrane protein that plays a relevant role in the metabolism of fatty acid amides and esters. It degrades important neurotransmitters such as oleamide and anandamide, and it has been involved in a number of human pathological conditions, representing therefore a valuable target for biochemical and pharmacological research. In this study, we have investigated in vitro the structure-function relationship of rat and human FAAHs. In particular circular dichroism, fluorescence spectroscopy and light scattering measurements have been performed, in order to characterize the structural features of the two proteins, both in the presence and absence of the irreversible inhibitor methoxyarachidonyl-fluorophosphonate. The results demonstrate that the structural dynamics of the two FAAHs are different, despite their high sequence homology and overall similarity in temperature-dependence. Additionally, membrane binding and kinetic assays of both FAAHs indicate that also the functional properties of the two enzymes are different in their interaction with lipid bilayers and with exogenous inhibitors. These findings suggest that pre-clinical studies of FAAH-dependent human diseases based only on animal models should be interpreted with caution, and that the efficacy of new drugs targeted to FAAH should be tested in vitro, on both rat and human enzymes.

Published
2012

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