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J. Biol. Chem., Vol. 278, Issue 52, 52551-52558, December 26, 2003

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Caspase 3-mediated Proteolysis of the N-terminal Cytoplasmic Domain of the Human Erythroid Anion Exchanger 1 (Band 3)^*

Debabrata Mandal, Veronique Baudin-Creuza, Asima Bhattacharyya, Shresh Pathak, Jean Delaunay, Manikuntala Kundu, and Joyoti Basu¶

From the Department of Chemistry, Bose Institute, 93/1 Acharya, Prafalla Chandra Road, Kolkata 700009, India and INSERM U 473, 84 rue du General-Leclerc, 94276 Le Kremlin-Bicetre, France

The N-terminal cytoplasmic domain of the anion exchanger 1 (AE1 or band 3) of the human erythrocyte associates with peripheral membrane proteins to regulate membrane-cytoskeleton interactions, with glycolytic enzymes such as glyceraldehyde-3-phosphate dehydrogenase and aldolase, with the protein-tyrosine kinase p72^syk, with hemoglobin and with hemichromes. We have demonstrated that the N-terminal cytoplasmic domain of band 3 (CDB3) is a substrate of the apoptosis executioner caspase 3 (1). CDB3 has two non-conventional caspase 3 cleavage sites, TATD⁴⁵ and EQGD²⁰⁵ (2). In vitro treatment of recombinant CDB3 with caspase 3 generated two fragments, which could be blocked by pretreatment with the caspase 3 inhibitor Z-DEVD-fmk (3). Recombinant CDB3 in which the caspase 3 cleavage sites Asp⁴⁵ and Asp²⁰⁵ were mutated, was resistant to proteolysis (4). Proteolytically derived fragments crossreactive with polyclonal anti-band 3 antibody appeared with simultaneous cleavage of poly (ADP-ribose) polymerase and procaspase 3 in staurosporine (STS)-treated HEK293 cells transiently transfected with CDB3 (5). In vivo cleavage of CDB3 could be blocked by pretreatment of cells with Z-DEVD-fmk or in cells transfected with mutant CDB3 (D45A, D205A) (6). Co-transfection experiments showed that STS-mediated cleavage of CDB3 diminished its interaction with the N-terminal domain of protein 4.2, confirming that such cleavage interferes with the interaction of CDB3 with cytoskeletal proteins (7). Active caspase 3 was observed in aged red cells but not in young cells. This red cell caspase 3 could cleave band 3 present in inside-out vesicles prepared from young erythrocytes arguing in favor of a physiological role of caspase 3 in aged erythrocytes.

Received for publication, June 29, 2003 , and in revised form, October 7, 2003.

^* This work was supported by Grant 1903-1 from the Indo-French Centre for the Promotion of Advanced Research and a grant from the Department of Biotechnology, Government of India. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Fax: 91-33-23506790; E-mail: joyoti{at}vsnl.com.

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				D. Mandal, A. Mazumder, P. Das, M. Kundu, and J. Basu Fas-, Caspase 8-, and Caspase 3-dependent Signaling Regulates the Activity of the Aminophospholipid Translocase and Phosphatidylserine Externalization in Human Erythrocytes J. Biol. Chem., November 25, 2005; 280(47): 39460 - 39467. [Abstract] [Full Text] [PDF]