USE OF ANTI-SINGLE-STRANDED DNA ANTIBODIES TO LOCALIZE AND QUANTIFY DENATURED DNA DURING CELL DEATH

2000 ◽  
Vol 24 (9) ◽  
pp. 657-659 ◽  
Author(s):  
C Gagna
Keyword(s):  
Cell Death ◽  
Single Stranded Dna ◽  
Dna Antibodies

scholarly journals SOS Induction by Stabilized Topoisomerase IA Cleavage Complex Occurs via the RecBCD Pathway

2008 ◽  
Vol 190 (9) ◽  
pp. 3399-3403 ◽  
Author(s):  
Jeanette H. Sutherland ◽  
Bokun Cheng ◽  
I-Fen Liu ◽  
Yuk-Ching Tse-Dinh
Keyword(s):  
Escherichia Coli ◽  
Cell Death ◽  
Topoisomerase I ◽  
Single Stranded Dna ◽  
Sos Induction ◽  
Cleavage Complex

ABSTRACT Accumulation of mutant topoisomerase I cleavage complex can lead to SOS induction and cell death in Escherichia coli. The single-stranded break associated with mutant topoisomerase I cleavage complex is converted to double-stranded break, which then is processed by the RecBCD pathway, followed by association of RecA with the single-stranded DNA.

scholarly journals IgA anti-single stranded DNA antibodies and IgA-containing circulating immune complexes (IgA-CIC) in MRL mice.

Ensho ◽  
1985 ◽  
Vol 5 (2) ◽  
pp. 103-105
Author(s):  
Gakuji Ohshio ◽  
Fukumi Furukawa ◽  
Hitoshi Tanaka ◽  
Kenichi Sekita ◽  
Yoshihiro Hamashima
Keyword(s):  
Immune Complexes ◽  
Circulating Immune Complexes ◽  
Single Stranded Dna ◽  
Dna Antibodies

scholarly journals Platelet binding properties of monoclonal lupus autoantibodies produced by human hybridomas

Blood ◽  
1985 ◽  
Vol 66 (6) ◽  
pp. 1254-1260 ◽  
Author(s):  
T Asano ◽  
BC Furie ◽  
B Furie
Keyword(s):  
Lupus Erythematosus ◽  
Platelet Rich Plasma ◽  
Inhibit Platelet Aggregation ◽  
Binding Properties ◽  
Single Stranded Dna ◽  
Platelet Surface ◽  
Phospholipid Micelles ◽  
Activated Platelets ◽  
Platelet Binding ◽  
Dna Antibodies

Abstract The platelet binding properties of human monoclonal lupus autoantibodies have been studied. These IgM autoantibodies, produced by human X human hybridomas derived from lymphocytes of patients with systemic lupus erythematosus, are known to bind to single-stranded DNA. Four anti-DNA antibodies that express the dominant 16/6 idiotype--HF2′1/17, HF2′18/2, HF2′1/13b, and HF3′16/6--bound to glutaraldehyde-fixed platelets. In contrast, HF6′21/28, HF9′11/3, and polyclonal IgM bound poorly to platelets. [35S]Methionine was incorporated into HF2′1/17, and the interaction of the intrinsically radiolabeled HF2′1/17 with fixed platelets was evaluated in a solution phase radioimmunoassay. [35S]Methionine HF2′1/17 bound to fixed platelets and could be displaced by equivalent amounts of HF2′1/17, HF2′18/2, HF2′1/13b, and HF3′16/6. HF2′1/17 bound with greater affinity to fresh platelets and to thrombin-activated platelets than to glutaraldehyde-fixed platelets. Single-stranded DNA competed with platelets for the HF2′1/17 combining site. Treatment of fresh platelets with nuclease I, trypsin, chymotrypsin, and neuraminidase did not alter the binding of antibody to the platelet surface. No binding of antibody to phospholipid micelles was observed. Purified IgM autoantibodies did not inhibit platelet aggregation induced with ADP, thrombin, or ristocetin in platelet-rich plasma. These results indicate that the human IgM monoclonal anti-DNA autoantibodies that express the dominant 16/6 idiotype are polyspecific, bind to platelets, and interact with a platelet epitope that does not appear to involve DNA, protein, or sialic acid. These antibodies interact with platelets through the same sites responsible for antibody-DNA binding.

scholarly journals Platelet binding properties of monoclonal lupus autoantibodies produced by human hybridomas

Blood ◽  
1985 ◽  
Vol 66 (6) ◽  
pp. 1254-1260
Author(s):  
T Asano ◽  
BC Furie ◽  
B Furie
Keyword(s):  
Lupus Erythematosus ◽  
Platelet Rich Plasma ◽  
Inhibit Platelet Aggregation ◽  
Binding Properties ◽  
Single Stranded Dna ◽  
Platelet Surface ◽  
Phospholipid Micelles ◽  
Activated Platelets ◽  
Platelet Binding ◽  
Dna Antibodies

The platelet binding properties of human monoclonal lupus autoantibodies have been studied. These IgM autoantibodies, produced by human X human hybridomas derived from lymphocytes of patients with systemic lupus erythematosus, are known to bind to single-stranded DNA. Four anti-DNA antibodies that express the dominant 16/6 idiotype--HF2′1/17, HF2′18/2, HF2′1/13b, and HF3′16/6--bound to glutaraldehyde-fixed platelets. In contrast, HF6′21/28, HF9′11/3, and polyclonal IgM bound poorly to platelets. [35S]Methionine was incorporated into HF2′1/17, and the interaction of the intrinsically radiolabeled HF2′1/17 with fixed platelets was evaluated in a solution phase radioimmunoassay. [35S]Methionine HF2′1/17 bound to fixed platelets and could be displaced by equivalent amounts of HF2′1/17, HF2′18/2, HF2′1/13b, and HF3′16/6. HF2′1/17 bound with greater affinity to fresh platelets and to thrombin-activated platelets than to glutaraldehyde-fixed platelets. Single-stranded DNA competed with platelets for the HF2′1/17 combining site. Treatment of fresh platelets with nuclease I, trypsin, chymotrypsin, and neuraminidase did not alter the binding of antibody to the platelet surface. No binding of antibody to phospholipid micelles was observed. Purified IgM autoantibodies did not inhibit platelet aggregation induced with ADP, thrombin, or ristocetin in platelet-rich plasma. These results indicate that the human IgM monoclonal anti-DNA autoantibodies that express the dominant 16/6 idiotype are polyspecific, bind to platelets, and interact with a platelet epitope that does not appear to involve DNA, protein, or sialic acid. These antibodies interact with platelets through the same sites responsible for antibody-DNA binding.

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