Articolo in rivista, 2009, ENG

Derangement of erythrocytic AE1 in beta-thalassemia by caspase 3: pathogenic mechanisms and implications in red blood cell senescence.

Ficarra S., Tellone E., Giardina B., Scatena R., Russo A., Misiti F., Clementi M.E., Colucci D., Bellocco E., Laganà G., Barreca D., Galtieri A.

1) Department of Organic and Biological Chemistry, University of Messina, Salita Sperone 31, 98166 Messina, Italy (2) Institute of Biochemistry and Clinical Biochemistry, Catholic University, School of Medicine, L.go F. Vito n.1, 00168 Rome, Italy (3) C.N.R. Institute of Chemistry of Molecular Recognition, L.go F. Vito n.1, 00168 Rome, Italy (4) Department of Health and Motor Sciences, University of Cassino, V.le Bonomi, 03043 Cassino, FR, Italy

Considering its complex molecular pathophysiology, beta-thalassemia could be a good in vivo model to study some aspects related to erythrocyte functions with potential therapeutic implications not only within the frame of this particular hemoglobinopathy but also with respect to conditions in which the cellular milieu, altered by a deranged anion exchanger, could display a significant pathogenetic role (i.e., erythrocyte senescence, complications of red cell storage, renal tubular acidosis and some abnormal protein thesaurismosis). This work evaluates the anionic influx across band 3 protein in normal and beta-thalassemic red blood cells (RBCs) and ghosts. Since redox-mediated injury is an important pathway in the destruction of beta-thalassemic RBCs, we studied the anion transport and the activity of caspase 3 in the absence and presence of t-butylhydroperoxide in order to evaluate the effect of an increase of cellular oxidative stress. Interestingly, beta-thalassemic erythrocytes show a faster rate of anion exchange than normal RBCs and absence of any modulation mechanism of anion influx. These findings led us to formulate a hypothesis about the metabolic characteristics of beta-thalassemic erythrocytes, outlining that one of the main targets of caspase 3 in RBCs is the cytoplasmic domain of band 3 protein.

The journal of membrane biology (Print) 228 , pp. 43–49

Keywords

CNR authors

Giardina Bruno, Clementi Maria Elisabetta

CNR institutes

ICRM – Istituto di chimica del riconoscimento molecolare

ID: 17646

Year: 2009

Type: Articolo in rivista

Creation: 2009-06-16 00:00:00.000

Last update: 2012-06-04 10:19:19.000

External links

OAI-PMH: Dublin Core

OAI-PMH: Mods

OAI-PMH: RDF

External IDs

CNR OAI-PMH: oai:it.cnr:prodotti:17646

ISI Web of Science (WOS): 000263916500004