Linked Life Data

14570914

Source:http://linkedlifedata.com/resource/pubmed/id/14570914

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
52
pubmed:dateCreated
2003-12-22
pubmed:abstractText
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 p72syk, 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
52551-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:14570914-Aging, pubmed-meshheading:14570914-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:14570914-Apoptosis, pubmed-meshheading:14570914-Binding Sites, pubmed-meshheading:14570914-Blotting, Western, pubmed-meshheading:14570914-Caspase 3, pubmed-meshheading:14570914-Caspase 8, pubmed-meshheading:14570914-Caspases, pubmed-meshheading:14570914-Cell Line, pubmed-meshheading:14570914-Cloning, Molecular, pubmed-meshheading:14570914-Cytoskeleton, pubmed-meshheading:14570914-Enzyme Inhibitors, pubmed-meshheading:14570914-Erythrocytes, pubmed-meshheading:14570914-Escherichia coli, pubmed-meshheading:14570914-Humans, pubmed-meshheading:14570914-Models, Genetic, pubmed-meshheading:14570914-Mutagenesis, Site-Directed, pubmed-meshheading:14570914-Mutation, pubmed-meshheading:14570914-Oligopeptides, pubmed-meshheading:14570914-Plasmids, pubmed-meshheading:14570914-Precipitin Tests, pubmed-meshheading:14570914-Protein Structure, Tertiary, pubmed-meshheading:14570914-Time Factors, pubmed-meshheading:14570914-Transfection
pubmed:year
2003
pubmed:articleTitle
Caspase 3-mediated proteolysis of the N-terminal cytoplasmic domain of the human erythroid anion exchanger 1 (band 3).
pubmed:affiliation
Department of Chemistry, Bose Institute, 93/1 Acharya, Prafalla Chandra Road, Kolkata 700009, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't