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Institute of Biosciences and Bioresources

National Research Council of Italy

Vincenzo Carginale

Role: Researcher
Section: Researchers and Technologists
Division: Naples
Tel: (39) 081-6132715-081-6132558
E-mail: vincenzo.carginale@ibbr.cnr.it


Address

Dr Vincenzo Carginale, Researcher

CNR Institute of Biosciences and BioResources

Via P. Castellino, 111- 80131 Naples Italy

Phone +39 081 6132715

Email: vincenzo.carginale@cnr.it

Biography

Personal data

Born in Rio de Janeiro (Brasil) 11/13/1960

Education

-Degree in Biology cum laude at University Federico II of Naples in 1987

-post-lauream training at University Federico II of Naples, Department of Evolutionary and Comparative Biology, from 1988 to 1989

-Licenced profession of biologists in 1989

-CNR fellowship at Institute of Protein Biochemistry of Naples from 1989 to 1991

-CNR Project “Biotechnology and Bioinstruments” fellowship at Institute of Protein Biochemistry of Naples from 1992 to 1993

-From 1994 CNR Researcher at Institute of Protein Biochemistry of Naples. Principal investigator of the project “Studies of the effects of heavy metals on gene expression in antarctic marine organisms and plants”.

-Scientific coordinator of the project ”Use of aquatic plants in heavy metal phytoremediation of polluted sites of Campania” funded by Regione Campania in 2000.

- Currently involved in research activities in the framework of Commessa CNR SV.P14.002.001: "Innovative applications of enzymes and Biotransformations".

Research interests

My primary research interests are in the area of protein biochemistry. During my career I performed researches on: regulation of signal transduction in Invertebrates; expression, evolution and functional properties of proteins and enzymes belonging to multigenic families (metallothioneins, aspartic proteinases) in Antarctic marine organisms; study of the effects, at genomic and/or proteomic level, of stress factors, such as heavy metals and pathogens, in Plants. Currently, I am involved in projects concerning the study of innovative biocatalysts from mesophilic and extremophilic organisms catalyzing biochemical transformations occurring at key points in the carbon cycle, in order to utilize them in CO2 sequestration processes and to produce valuable four-carbon compounds.

Publications (complete list at http://scholar.google.it/citations?user=GOwlsnIAAAAJ&hl=it)

Articles on international peer reviewed journals

2014

Migliardini F, De Luca V, Carginale V, Rossi M, Corbo P, Supuran CT, Capasso C. Biomimetic CO(2) capture using a highly thermostable bacterial α-carbonic anhydrase immobilized on a polyurethane foam. J Enzyme Inhib Med Chem, 29:146-150 (2014)

Del Prete S, De Luca V, Scozzafava A, Carginale V, Supuran CT, Capasso C. Biochemical properties of a new α-carbonic anhydrase from the human pathogenic bacterium, Vibrio cholerae. J Enzyme Inhib Med Chem, 29:23-27 (2014)

Pisani A, Sabbatini M, Riccio E, Rossano R, Andreucci M, Capasso C, De Luca V, Carginale V, Bizzarri M, Borrelli A, Schiattarella A, Santangelo M, Mancini A. Effect of a recombinant manganese superoxide dismutase on prevention of contrast-induced acute kidney injury.

Clin Exp Nephrol, 18:424-431 (2014)

Del Prete S, De Luca V, Vullo D, Scozzafava A, Carginale V, Supuran CT, Capasso C. Biochemical characterization of the γ-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis, PgiCA. J Enzyme Inhib Med Chem, 29:532-537 (2014)

2013

Vullo D, Luca VD, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides. Bioorg Med Chem, 21:1534-1538 (2013)

Luca VD, Vullo D, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. An α-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO(2) hydration reaction. Bioorg Med Chem, 21:1465-1469 (2013)

Akdemir A, Vullo D, Luca VD, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The extremo-α-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines. Bioorg Med Chem Lett, 23:1087-1090 (2013)

Del Prete S, Vullo D, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C. A highly catalytically active γ-carbonic anhydrase from the pathogenic anaerobe Porphyromonas gingivalis and its inhibition profile with anions and small molecules. Bioorg Med Chem Lett, 23:4067-4071 (2013)

Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The extremo-α-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides. Bioorg Med Chem, 21:4521-4525 (2013)

Vullo D, Isik S, Del Prete S, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C. Anion inhibition studies of the α-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae. Bioorg Med Chem Lett. 23:1636-1638 (2013)

Di Fiore A, Capasso C, De Luca V, Monti SM, Carginale V, Supuran CT, Scozzafava A, Pedone C, Rossi M, De Simone G. X-ray structure of the first extremo-α-carbonic anhydrase’, a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Acta Crystallogr D Biol Crystallogr. 69:1150-1159 (2013)

2012

A. Basile, S. Sorbo, B. Conte, R. Castaldo Cobianchi, F. Trinchella, C. Capasso, V. Carginale. Toxicity, accumulation, and removal of heavy metals by three aquatic macrophytes. Int J Phytoremediation, 14:374-387 (2012)

Borrelli A, Schiattarella A, Musella A, Mancini R, Capasso C, De Luca V, Carginale V, Sanseverino M, Tornesello A, Gori E, Pica A, Di Santi A, Basile F, Iacobellis F, Colacurci N, Cobellis L, Mancini A. A molecular carrier to transport and deliver cisplatin into endometrial cancer cells. Chem Biol Drug Des, 80:9-16 (2012)

Capasso C, De Luca V, Carginale V, Cannio R, Rossi M. Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1. J Enzyme Inhib Med Chem, 27:892-897 (2012)

Del Prete S, Isik S, Vullo D, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C. DNA cloning, characterization and inhibition studies of an alpha-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae. J Med Chem, 55:10742-10748 (2012)

De Luca V, Vullo D, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. Anion inhibition studies of an α-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Bioorg Med Chem Lett, 22:5630-5634 (2012)

Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. The first activation study of a bacterial carbonic anhydrase (CA). The thermos... Bioorg Med Chem Lett, 22:6324-6327 (2012)

Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C. Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett, 22:7142-7145 (2012)

2011

V. De Luca, C. Capasso, A. Capasso, M. Pastore, V. Carginale. Gene expression profiling of phytoplasma-infected Madagascar periwinkle leaves using differential display. Mol. Biol. Rep. 38:2993-3000 (2011)

Stranges S, Galletti F, Farinaro E, D’Elia L, Russo O, Iacone R, Capasso C, Carginale V, De Luca V, Della Valle E, Cappuccio FP, Strazzullo P. Associations of selenium status with cardiometabolic risk factors: An 8-year follow-up analysis of the Olivetti Heart Study. Atherosclerosis 217:274-278 (2011)

S. Del Prete, V. De Luca, C. Capasso, M. Pastore, M. Del Vaglio, A. Capasso, V. Carginale. Preliminary proteomic analysis of pear leaves in response to pear decline phytoplasma infection. B. Insectol. 64:187-188 (2011)

2009

V. De Luca, G. Maria, G. De Mauro, G. Catara, V. Carginale, G. Ruggiero, A. Capasso, E. Parisi, S. Brier, J. R. Engen, C. Capasso. Aspartic proteinases in Antarctic fish. Mar. Genom. 2:1-10 (2009)

2007

M. Tessitori, G. Maria, C. Capasso, G. Catara, S. Rizza, V. De Luca, A. Catara, A. Capasso, V. Carginale. Differential Display analysis of gene expression in Etrog citron leaves infected by Citrus viroid III. Biochim Biophys Acta, 1769:228-235 (2007).

S. Brier, G. Maria, V. Carginale, A. Capasso, Y. Wu, R.M. Taylor, N.B. Borotto, C. Capasso, J.R. Engen Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii. FEBS J., 274:6152-6166 (2007)

2006

C. Capasso, V. Carginale, M. Riggio, R. Scudiero, P.A. Temussi, F. Trinchella, E. Parisi. Metal detoxification and homeostasis in Antarctic Notothenioids. A comparative survey on evolution, expression and functional properties of fish and mammal metallothioneins. Rev Environ Sci Biotechnol 5, 253-267 (2006)

2005

C. Capasso, V. Carginale, O. Crescenzi, D. Di Maro, R. Spadaccini, P.A. Temussi, E. Parisi. Structural and functional studies of vertebrate metallothioneins: Cross-talk between domains in the absence of physical contact. Biochem J., 391:95-103 (2005)

A. Basile, R. A. di Nuzzo, C. Capasso, S. Sorbo, A. Capasso, V. Carginale. Effect of cadmium on gene expression in the liverwort Lunularia cruciata. Gene, 356:153-159 (2005)

2004

V. Carginale, S. Sorbo, C. Capasso, F. Trinchella, G. Cafiero, A. Basile. Accumulation, localisation and toxic effects of cadmium in the liverwort Lunularia cruciata. Protoplasma, 223:53-61 (2004)

V. Carginale, G. Maria, C. Capasso, E. Ionata, F. La Cara, M, Pastore, A. Bertaccini, A. Capasso. Identification of genes expressed in response to phytoplasma infection in leaves of Prunus armeniaca by messenger RNA differential display. Gene, 332:29-34 (2004)

V. Carginale, F. Trinchella, C. Capasso, R. Scudiero, M. Riggio, E. Parisi. Adaptive evolution and functional divergence of pepsin gene family. Gene, 333:81-90 (2004)

V. Carginale, F. Trinchella, C. Capasso, R. Scudiero, E. Parisi. Gene amplification and cold adaptation of pepsin in Antarctic fish. A possible strategy for food digestion at low temperature. Gene, 336:195-205 (2004)

2003

Capasso C, Carginale V, Crescenzi O, Di Maro D, Parisi E, Spadaccini R, Temussi PA. Solution structure of MT_nc, a novel metallothionein from the Antarctic fish Notothenia coriiceps. Structure (Camb) 11:435-443 (2003)

C. Capasso, V. Carginale, R. Scudiero, O. Crescenzi, R. Spadaccini, P.A. Temussi, E. Parisi. Phylogenetic divergence of fish and mammalian metallothionein. Relationship with structural diversification and organismal temperature. J. Mol. Evol., 57: S250-S257 (2003)

2002

C. Capasso, O. Abugo, F. Tanfani, A. Scire, V. Carginale, R. Scudiero, E. Parisi, S. D’Auria. Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse. Proteins 46: 259-267 (2002)

V. Carginale, C. Capasso, R. Scudiero, E. Parisi. Identification of cadmium-sensitive genes in the Antarctic fish Chionodraco hamatus by messenger RNA differential display. Gene 299:117-124 (2002)

2001

D’auria S, Carginale V, Scudiero R, Crescenzi O, Di Maro D, Temussi PA, Parisi E, Capasso C. Structural characterization and thermal stability of Notothenia coriiceps metallothionein. Biochem J., 354:291-299 (2001)

Scudiero R, Carginale V, Capasso C, Riggio M, Filosa S, Parisi E. Structural and functional analysis of metal regulatory elements in the promoter region of genes encoding metallothionein isoforms in the Antarctic fish Chionodraco hamatus (icefish). Gene 274:199-208 (2001)

2000

R. Scudiero, C. Verde, V. Carginale, P. Kille, C. Capasso, G. di Prisco, E. Parisi. Tissue-specific regulation of metallothionein and metallothionein mRNA accumulation in the Antarctic notothenioid, Notothenia coriiceps. Polar Biol., 23: 17-23 (2000)

V. Carginale, R. Scudiero, C. Capasso, E. Parisi. Metallothionein in Antarctic notothenioids: genetic polymorphism and differential gene expression. Ital. J. Zool., 67:13-20 (2000)

C. Capasso, V. Carginale, R. Scudiero, M. Riggio, J. Kay, E. Parisi. Aspartic proteinases from Antarctic fish. A biochemical and molecular approach. Ital. J. Zool., 67:21-26 (2000)

1999

C. Capasso, W. E. Lees, A. Capasso, R. Scudiero, V. Carginale, P. Kille, J. Kay, E. Parisi. Cathepsin D from the liver of the Antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures. Biochim. Biophys. Acta, 1431:64-73 (1999)

L. Bargelloni, R. Scudiero, E. Parisi, V. Carginale, C. Capasso, T. Patarnello. Metallothioneins in Antarctic Fish: Evidence for Independent Duplication and Gene Conversion. Mol. Biol. Evol., 16:885-897 (1999)

1998

V. Carginale, R. Scudiero, C. Capasso, A. Capasso, P. Kille, G. di Prisco, E. Parisi. Cadmium-induced differential accumulation of metallothionein isoforms in the Antarctic icefish which exhibits no basal protein but high endogenous mRNA levels. Biochem. J., 332:475-481 (1998)

C. Capasso, M. Riggio, R. Scudiero, V. Carginale, G. di Prisco, J. Kay, P. Kille, E. Parisi Molecular cloning and sequence determination of a novel aspartic proteinase from Antarctic fish. Biochim. Biophys. Acta, 1387:457-461 (1998)

R. Scudiero, V. Carginale, C. Capasso, P. Kille, E. Parisi. Biochemical and molecular studies on metallothionein in Antarctic aquatic organisms. Trends in Comp. Biochem. & Physiol., 4:153-164 (1998)

1997

Scudiero, R., Carginale, V., Riggio, M., Capasso, C., Capasso, A., Kille, P., di Prisco, G., Parisi, E. Difference in hepatic metallothionein content in red-blooded and haemoglobinless Antarctic fishes. Undetectable metallothionein levels in haemoglobinless fishes is accompanied by accumulation of untranslated metallothionein mRNA Biochem. J., 322:207-211, (1997)

Scudiero, R., Capasso, C., Carginale, V., Riggio, M., Capasso, A., Ciaramella, M., Filosa, S., Parisi, E. PCR amplification and cloning of metallothionein complementary DNAs in temperate and Antarctic sea urchin characterized by a large difference in egg metallothionein content. CMLS, Cell Mol. Life Sci., 53:472-477 (1997)

1996

Scudiero, R., Capasso, C., Carginale, V., Filosa, S., Capasso, A., Parisi, E. Isolation and characterisation of zinc-binding proteins distinct from metallothionein from the eggs of the sea urchin Strongylocentrotus intermedius. Mar. Biol., 126:225-230 (1996)

1995

V. Carginale, L. Borrelli, A. Capasso, E. Parisi. Changes in dopamine uptake and developmental effect of dopamine receptor inactivation in sea urchin. Mol. Repr. Dev., 40:379-385 (1995)

L. Borrelli, V. Carginale, A. Capasso, T. Schneider, T. Leitz, L. De Petrocellis, V. Di Marzo. Phospholipase A2 and Protein Kinase C enzymatic activities and their interactions in Hydra vulgaris. Comp. Biochem. Physiol., 111B: 211-219 (1995)

1993

A. Capasso, V. Carginale, L. Borrelli, E. Parisi. Receptor-mediated inhibition of octopamine-stimulated adenylate cyclase in the optic lobe of Octopus vulgaris. Comp. Biochem. Physiol., 106C: 555-559 (1993)

1992

V. Carginale, A. Capasso, L. Madonna, L. Borrelli, E. Parisi. Adenylate cyclase from sea urchin eggs is positively and negatively regulated by D-1 and D-2 dopamine receptors. Exp. Cell Res., 203:491-494 (1992)

1991

P. De Prisco, R. Scudiero, V. Carginale, A. Capasso, E. Parisi, B. De Petrocellis. Developmental changes of metallothionein content and synthesis in sea urchin Paracentrotus lividus embryos. Cell Biol. Int. Rep., 15:305-317 (1991)

A. Capasso, V. Carginale, L. Madonna, D. Mancaniello, R. Scudiero, P. De Prisco, B. De Petrocellis, E. Parisi. A dopamine- and octopamine-sensitive adenylate cyclase in the nervous system of Octopus vulgaris. Comp. Biochem. Physiol., 100B: 805-808 (1991)

1990

A. Capasso, V. Carginale, B. De Petrocellis, E. Parisi. Guanine nucleotide binding proteins activate adenylate cyclase from sea urchin sperm. Comp. Biochem. Physiol., 97B: 339-342 (1990)

 

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(full list available at CNR People)

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