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Dive into the research topics where Michela Festa is active.

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Featured researches published by Michela Festa.


Journal of Biological Chemistry | 2000

Overexpression of H Ferritin and Up-regulation of Iron Regulatory Protein Genes during Differentiation of 3T3-L1 Pre-adipocytes

Michela Festa; Gaetano Ricciardelli; Guido Mele; Concetta Pietropaolo; Alfredo Ruffo; Alfredo Colonna

The role of iron-dependent oxidative metabolism in protecting the oxidable substrates contained in mature adipocytes is still unclear. Because differentiation increases ferritin formation in several cell types, thereby leading to an accumulation of H-rich isoferritins, we investigated whether differentiation affects iron metabolism in 3T3-L1 pre-adipocytes. To this aim, we evaluated the expression of the genes coding for the H and L ferritin subunits and for cytoplasmic iron regulatory protein (IRP) during the differentiation of 3T3-L1 cells in adipocytes induced by the addition of isobutylmethylxanthine, insulin, and dexamethasone. Differentiation enhanced ferritin formation and caused overexpression of the H subunit, thus altering the H/L subunit ratio. Northern blot analysis showed increased levels of H subunit mRNA. A gel retardation assay of cytoplasmic extract from differentiated cells, using an iron-responsive element as a probe, revealed enhanced an RNA binding capacity of IRP1, which correlated with the increase of IRP1 mRNA. The observed correlation between differentiation and iron metabolism in adipocytes suggests that an accumulation of H-rich isoferritin may limit the toxicity of iron in adipose tissue, thus exerting an antioxidant function.


Rendiconti Lincei-scienze Fisiche E Naturali | 1997

Modulation of gene expression in differentiating 3T3-L1 preadipocytes

Michela Festa; Alfredo Colonna; Alfredo Ruffo; Gaetano Ricciardelli; Concetta Pietropaolo

Abstract3T3-L1 cells can be induced to differentiate by exposing cell culture to a medium containing 3-isobutyl-l-methyl-xanthine together with insulin and dexamethasone. We have previously observed that oxalomalate which inhibits aconitase thus blocking the citric cycle, also favours differentiation to adipocytes leading to fatty acids accumulation and increased synthesis of specific proteins. We compared the effects of 3-isobutyl-l-methyl-xanthme-insulin-dexamethasone and on the steady-state levels of mRNA of c/EBP, H-ferritin and aconitase/IRE-BP. does not affect the steady-state mRNA amount of c/EBP, H-ferritin and aconitase/IRE-BP, but the 3-isobutyl-l-methyl-xanthine-insulin-dexamethasone mixture is able to induce a five-fold increase of mRNA levels for aconitase/IRE-BP. This is the first finding correlating iron metabolism to adipocyte differentiation. Further studies will clarify a possible role for the aconitase inhibitor.RiassuntoLe cellule 3T3-L1 possono essere indotte a differenziarsi dall’aggiunta al mezzo di coltura di 3-isobutil-l-metil-xantina-insulina-desametasone. Noi abbiamo precedentemente osservato che anche l’ossalomalato noto inibitorc della aconitasi, put) indurre 1a differenziazione di 3T3-L1 con accumulo di acidi grassi e aumento della sintesi di proteine specifiche. Nel presente lavoro sono stati paragonati i livelli di mRNA per c/EBP, H-ierritina e aconitasi/IRE-BP in 3T3-L1 differenziate in seguito a trattamento con mezzi contenenti 3-isobutil-1-metil-xantina-insulina-desametasone owero ON1A. L’OMA non altera i livelli degli mRNA analizzati, ma l’aggiunta di 3-isobutil-l-metil-xantina-insulina-desametasone al mezzo di coltura fa aumentare di circa cinque volte il livello di mRNA per aconitasi/IRE-BP. Questi sono i primi dati che mostrano una correlazione tra il metabolismo del ferro e la differenziazione degli adipociti. Ricerche in corso chiariranno se l’OMA svolga un ruolo in tale correlazione.


Rendiconti Lincei-scienze Fisiche E Naturali | 2000

Oxalomalate: an inhibitor for two functions

Michela Festa; Alfredo Ruffo

It has been investigated whether oxalomalate (OMA) the competitive inhibitor of cytosolic aconitase might extend its effect also on IRP-1, an iron regulatory protein, probably present in a commercial preparation of purified aconitase. The results showed that IRP-1 is contained in the purified preparation and was strongly inhibited during the incubation with OMA. The effect produced by OMA on the bi-functional protein IRP-1/aconitase was discussed.RiassuntoÈ stato indagato l’effetto dell’OMA, ben noto inibitore competitivo della forma citosolica di aconitasi, sulla eventuale presenza di IRP-1 in una preparazione commerciale di aconitasi purificata. I risultati hanno dimostrato che IRP-1 è presente nella preparazione purificata e viene fortemente inibita nel corso di una breve incubazione con OMA 5 mM, a temperatura ambiente. Viene messa in evidenza l’inibizione prodotta da OMA su entrambe le forme della proteina bifunzionale IRP-1/Aconitasi.


Rendiconti Lincei-scienze Fisiche E Naturali | 1999

Regulation of iron metabolism by oxalomalate

Michela Festa; Alfredo Colonna; Concetta Pietropaolo; Alfredo Ruffo

It has been investigatedin vitro the effect of oxalomalate (OMA) on the ferritin mRNA binding capacity of the bifunctional protein aconitase/IRP-1 contained in lysates of confluent cultures of 3T3-L1 fibroblasts. After short time of incubation with OMA at 37 °C, the gel mobility-shift analysis showed that the binding capacity of IRP-1 diminished and after 1 hour practically disappeared, indicating that the interaction of OMA with the aconitase counterpart reduced the aliquot of IRP-1 available to mRNA binding.RiassuntoL’effetto dell’acido ossalomalico (OMA) sul potere legante l’mRNA della ferritina da parte di una proteina bifunzionale regolatrice il metabolismo del ferro, l’aconitasi/IRP-1, presente nei lisati di colture di 3T3-L1, è stato determinato con il metodo dettomobility-shift assay. I risultati ottenuti dopo incubazione dei lisati con OMA 5 mM hanno mostrato notevole diminuzione della capacità legante di IRP-1 che dopo 1 ora a 37 °C scompare, mettendo in evidenza la possibilità che l’OMA possa partecipare al complesso meccanismo della regolazione intracellulare del metabolismo del ferro.


Rendiconti Lincei-scienze Fisiche E Naturali | 1997

Regulation of ferritin expression by oxalomalate in differentiating preadipocytes 3T3-L1

Alfredo Colonna; Michela Festa; Concetta Pietropaolo; Gaetano Ricciardelli; Alfredo Ruffo

Ferritin content and the specific RNA binding capacity of IRP1/aconitase were determined in lysates of 3T3-L1 adipocytes during their differentiation promoted by the addition to the culture of isobutyl-methylxantine, insulin and dexamethasone (DXM) or by a solution of oxalomalate well known inhibitor of aconitase. The results obtained show that ferritin is present in mature adipocytes and that during differentiation a consistent increase of its formation was observed. Moreover a high extent of RNA-IRPl binding activity was demonstrated only in the DXM differentiated cells, while those treated by presented a binding capacity similar to the control.RiassuntoII contenuto in rerritina e la capacità di legarsi da parte di una proteina regolatrice nota come IRP1/aconitasi ad un sito ferro-sensibile dell’mRNA della ferritina, sono stati determinati in lisati di cellule 3T3-L1 nel corso della loro differenziazione, indotta dall’aggiunta alle colture sia di una miscela di isobutil-metilxantina, insulina e desametasone (DXM), sia di una soluzione di ossalomalato (OMA), noto inibitore dell’aconitasi. I risultati ottenuti mostrano che 1a ferritina è presente negli adipociti maturi ed il suo contenuto aumenta sensibilmente nel corso della loro differenziazione. Inoltrc, è stato dimostrato che la capacità dell’IRP1/aconitasi di legarsi all’mRNA della ferritina è elevata solo nelle cellule trattate con DXM, mentre in quelle diiferenziate da è simile a quelle di controllo.


Rendiconti Lincei-scienze Fisiche E Naturali | 2002

Effect of oxalomalate on the development and differentiation of 3T3-L1 pre-adipocytes

Michela Festa; Concetta Pietropaolo; Alfredo Ruffo

We investigated on cultured 3T3-L1 pre-adipocytes incubated with and withoutα-hydroxy-β-oxalosuccinic acid, shortly named oxalomalate (OMA), the rate of growth and differentiation together with fatty acids and protein synthesis and the variation of ferritin mRNA level. The main results showed that OMA inhibited cellular growth, accelerated the differentiation into adipocytes, increased the synthesis of fatty acids and proteins and enhanced the translation of ferritin mRNA. The presented results were briefly discussed.RiassuntoÈ stata determinata in colture di 3T3-L1 pre-adipociti incubati con e senza OMA, la crescita e la differenziazione in adipociti, insieme al dosaggio di acidi grassi, proteine e mRNA della ferritina. I risultati ottenuti hanno dimostrato che in presenza di OMA viene inibita la crescita, stimolata la differenziazione, aumentata la sintesi di acidi grassi e proteine ed incrementata l’espressione di mRNA della ferritina. Le ragioni di tali risultati sono state brevemente discusse.


Biochemical Journal | 2000

Oxalomalate, a competitive inhibitor of aconitase, modulates the RNA-binding activity of iron-regulatory proteins

Michela Festa; Alfredo Colonna; Concetta Pietropaolo; Alfredo Ruffo


Biochimica et Biophysica Acta | 2004

Induction of ferritin expression by oxalomalate

Rita Santamaria; Carlo Irace; Michela Festa; Carmen Maffettone; Alfredo Colonna


Life Sciences | 2007

Oxalomalate affects the inducible nitric oxide synthase expression and activity.

Carlo Irace; Giuseppe Esposito; Carmen Maffettone; Antonietta Rossi; Michela Festa; Teresa Iuvone; Rita Santamaria; Lidia Sautebin; Rosa Carnuccio; Alfredo Colonna


Rendiconti Lincei-scienze Fisiche E Naturali | 2002

Effetto dellossalomalato sullo sviluppo e sulla differenziazione di pre-adipociti 3T3-L1

Michela Festa; Concetta Pietropaolo; Alfredo Ruffo

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Alfredo Colonna

University of Naples Federico II

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Concetta Pietropaolo

Children's Hospital of Philadelphia

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Carlo Irace

University of Naples Federico II

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Carmen Maffettone

University of Naples Federico II

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Rita Santamaria

University of Naples Federico II

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Antonietta Rossi

University of Naples Federico II

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Giuseppe Esposito

Sapienza University of Rome

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Lidia Sautebin

University of Naples Federico II

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Rosa Carnuccio

University of Naples Federico II

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