Irene Messana

Prof. Irene Messana

Istituto di Scienze e Tecnologie Chimiche “Giulio Natta”, Consiglio Nazionale delle Ricerche, Roma, Italy.
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Research Focus & Metrics

Academic Career Length

48Years (1979-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 January 1995 in Critical Reviews in Biochemistry and Molecular Biology
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Journal Article
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BGBruno Giardina
Bruno Giardina
IMIrene Messana
Irene Messana
RSRoberto Scatena
Roberto Scatena
MCMassimo Castagnola
Massimo Castagnola
The aim of this review is to focus and discuss several parallel biological functions of hemoglobin besides its basic function of oxygen transport. In light of the information present in the literature the following possible physiological roles of hemoglobin are discussed: (1) hemoglobin as molecular heat transducer through its oxygenation-deoxygenation cycle, (2) hemoglobin as modulator of erythrocyte metabolism, (3) hemoglobin oxidation as an onset of erythrocyte senescence, (4) hemoglobin and its implication in genetic resistance to malaria, (5) enzymatic activities of hemoglobin and interactions with drugs, and (6) hemoglobin as source of physiological active catabolites.

1 April 2017 in Acta Otorhinolaryngologica Italica
Verified
Journal Article
Open access
MCMassimo Castagnola
Massimo Castagnola
ESE. Scarano
E. Scarano
Giulio Cesare PassaliGiulio Cesare Passali
Giulio Cesare Passali
IMIrene Messana
Irene Messana
TCTiziana Cabras
Tiziana Cabras
GPG. Paludetti
G. Paludetti
Lo studio della proteomica salivare, test economico e non invasivo, rappresenta una fonte di numerose informazioni, ed è utile per la diagnosi di svariate malattie. Da quando siamo entrati nell’era della tecnologia genomica e delle scienze “omiche”, la raccolta di campioni salivari è aumentata esponenzialmente. Recenti piattaforme proteomiche hanno analizzato il proteoma salivare umano, caratterizzando circa 3000 peptidi e proteine, espressi in maniera differente: più del 90% in peso deriva dalla secrezione delle tre ghiandole salivari maggiori, mentre la restante parte proviene dalle ghiandole salivari minori, dal fluido crevicolare gengivale, da essudati mucosi e dalla microflora orale. L’obiettivo principale dell’analisi proteomica è discriminare tra condizioni fisiologiche e patologiche. Ad oggi, tuttavia, non esiste un preciso protocollo che permetta di analizzare l’intero proteoma salivare, pertanto sono state realizzate svariate strategie. Innanzitutto, è possibile distinguere due tipologie di piattaforme proteomiche: l’approccio “top-down” prevede l’analisi delle proteine sotto esame come entità intatte; nell’approccio “bottom-up” la caratterizzazione della proteina avviene mediante lo studio dei peptidi ottenuti dopo digestione enzimatica (con tripsina tipicamente). A causa di questa eterogeneità, per una stessa patologia sono stati proposti differenti biomarkers. Il proteoma salivare è stato caratterizzato in numerose malattie: carcinoma squamoso e leucoplachie orali, malattia del trapianto contro l’ospite (GVHD) cronica, sindrome di Sjögren e altri disordini autoimmuni come la sindrome SAPHO (sinovite, acne, pustolosi, iperostosi e osteite), schizofrenia e disordine bipolare, malattie genetiche come la sindrome di Down o la malattia di Wilson. In conclusione, i risultati delle ricerche riportate in questa review suggeriscono che nel prossimo futuro la saliva diverrà un fluido di indubbia rilevanza diagnostica utile per fini clinici, sia diagnostici, sia prognostici.

1 June 2008 in Journal of Separation Science
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Journal Article
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IMIrene Messana
Irene Messana
RIRosanna Inzitari
Rosanna Inzitari
CFChiara Fanali
Chiara Fanali
TCTiziana Cabras
Tiziana Cabras
MCMassimo Castagnola
Massimo Castagnola

1 January 2012 in Fertility and Sterility
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Journal Article
Closed access
DMDomenico Milardi
Domenico Milardi
GGGiuseppe Grande
Giuseppe Grande
FVFederica Vincenzoni
Federica Vincenzoni
IMIrene Messana
Irene Messana
APAlfredo Pontecorvi
Alfredo Pontecorvi
RMRiccardo Marana
Riccardo Marana

1 May 2008 in Molecular & Cellular Proteomics
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Journal Article
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IMIrene Messana
Irene Messana
TCTiziana Cabras
Tiziana Cabras
EPElisabetta Pisano
Elisabetta Pisano
MSMaria Teresa Sanna
Maria Teresa Sanna
AOAlessandra Olianas
Alessandra Olianas
MCMassimo Castagnola
Massimo Castagnola
To elucidate the localization of post-translational modifications of different classes of human salivary proteins and peptides (acidic and basic proline-rich proteins (PRPs), Histatins, Statherin, P-B peptide, and “S type” Cystatins) a comparative reversed phase HPLC-ESI-MS analysis on intact proteins of enriched granule preparations from parotid and submandibular glands as well as parotid, submandibular/sublingual (Sm/Sl), and whole saliva was performed. The main results of this study indicate the following. (i) Phosphorylation of all salivary peptides, sulfation of Histatin 1, proteolytic cleavages of acidic and precursor basic PRPs occur before granule storage. (ii) In agreement with previous studies, basic PRPs are secreted by the parotid gland only, whereas all isoforms of acidic PRPs (aPRPs) are secreted by both parotid and Sm/Sl glands. (iii) Phosphorylation levels of aPRPs, Histatin 1, and Statherin are higher in the parotid gland, whereas the extent of cleavage of aPRP is higher in Sm/Sl glands. (iv) O-Sulfation of tyrosines of Histatin 1 is a post-translational modification specific for the submandibular gland. (v) The concentration of Histatin 3, Histatin 5, and Histatin 6, but not Histatin 1, is higher in parotid saliva. (vi) Histatin 3 is submitted to the first proteolytic cleavage (generating Histatins 6 and 5) during granule maturation, and it occurs to the same relative extent in both glands. (vii) The proteolytic cleavages of Histatin 5 and 6, generating a cascade of Histatin 3 fragments, take place after granule secretion and are more extensive in parotid secretion. (viii) Basic PRPs are cleaved in the oral cavity by unknown peptidases, generating various small proline-rich peptides. (ix) C-terminal removal from Statherin is more extensive in parotid saliva. (x) P-B peptide is secreted by both glands, and its relative quantity is higher in submandibular/sublingual secretion. (xi) In agreement with previous studies, S type Cystatins are mainly the product of Sm/Sl glands.

1 September 1997 in Clinica Chimica Acta
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Journal Article
Closed access
CZCecilia Zuppi
Cecilia Zuppi
IMIrene Messana
Irene Messana
FFFranca Forni
Franca Forni
CRCristina Rossi
Cristina Rossi
LPLucia Pennacchietti
Lucia Pennacchietti
BGBruno Giardina
Bruno Giardina