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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1999-9-7
pubmed:abstractText
Sera of healthy humans contain natural cytotoxic IgM antibodies that specifically recognize a Mr 260,000 antigen (NB-p260) on the surface of human neuroblastoma (NB) cells. Here we demonstrate that anti-NB IgM antibodies prepared from different healthy individuals induce, in all human NB cell lines analyzed thus far, typical morphological and biochemical features of apoptosis including nuclear fragmentation, chromatin condensation, and DNA fragmentation. Both the binding of human anti-NB IgM to NB cells and the induction of apoptosis could be inhibited by preincubation of NB cells with murine IgG raised against purified NB-p260. Furthermore, preincubation of human anti-NB IgM with purified NB-p260 immobilized onto a solid support abolished its ability to induce apoptosis in NB cells. Natural human anti-NB IgM failed to bind to and induce apoptosis in control tumor cell lines that lack expression of NB-p260. The anti-NB IgM-induced apoptotic response was also observed in vivo in xenografted human NB tumors. After a single i.v. injection of anti-NB IgM into nude rats bearing solid NB xenografts, many areas of pyknotic cells with fragmented nuclei were observed that stained positive using the terminal dUTP nick end labeling method. In conclusion, the data demonstrate that natural anti-NB IgM antibodies in the sera of healthy individuals are potent mediators of apoptotic cell death of NB cells both in vitro and in vivo. The NB-p260 antigen was identified as the apoptosis-inducing receptor for anti-NB IgM. Whereas natural anti-NB IgM and NB-p260 may be useful tools for immunotherapy of NB, their biological significance remains to be determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3768-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10446994-Animals, pubmed-meshheading:10446994-Antibody Specificity, pubmed-meshheading:10446994-Antigens, Neoplasm, pubmed-meshheading:10446994-Apoptosis, pubmed-meshheading:10446994-Bone Neoplasms, pubmed-meshheading:10446994-Chickens, pubmed-meshheading:10446994-DNA Fragmentation, pubmed-meshheading:10446994-Flow Cytometry, pubmed-meshheading:10446994-Goats, pubmed-meshheading:10446994-Humans, pubmed-meshheading:10446994-Immunization, Passive, pubmed-meshheading:10446994-Immunoglobulin G, pubmed-meshheading:10446994-Immunoglobulin M, pubmed-meshheading:10446994-Immunoglobulins, pubmed-meshheading:10446994-Male, pubmed-meshheading:10446994-Melanoma, pubmed-meshheading:10446994-Mice, pubmed-meshheading:10446994-Molecular Weight, pubmed-meshheading:10446994-Neoplasm Transplantation, pubmed-meshheading:10446994-Neuroblastoma, pubmed-meshheading:10446994-Osteosarcoma, pubmed-meshheading:10446994-Rats, pubmed-meshheading:10446994-Rats, Nude, pubmed-meshheading:10446994-Rhabdomyosarcoma, pubmed-meshheading:10446994-Skin Neoplasms, pubmed-meshheading:10446994-Tumor Cells, Cultured
pubmed:year
1999
pubmed:articleTitle
Human natural immunoglobulin M antibodies induce apoptosis of human neuroblastoma cells by binding to a Mr 260,000 antigen.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, University of Hamburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't