The spontaneous release of a high-molecular-weight aggregate containing immunoglobulin G from the surface of Ehrlich ascites tumor cells
dc.contributor.author | Rittenhouse, Harry G. | en_US |
dc.contributor.author | Ar, Diane | en_US |
dc.contributor.author | Lynn, Matthew D. | en_US |
dc.contributor.author | Denholm, David K. | en_US |
dc.date.accessioned | 2006-04-28T16:45:50Z | |
dc.date.available | 2006-04-28T16:45:50Z | |
dc.date.issued | 1978 | en_US |
dc.identifier.citation | Rittenhouse, Harry G.; Ar, Diane; Lynn, Matthew D.; Denholm, David K. (1978)."The spontaneous release of a high-molecular-weight aggregate containing immunoglobulin G from the surface of Ehrlich ascites tumor cells." Journal of Supramolecular Structure 9(3): 407-419. <http://hdl.handle.net/2027.42/38207> | en_US |
dc.identifier.issn | 0091-7419 | en_US |
dc.identifier.issn | 1547-9366 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/38207 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=571032&dopt=citation | en_US |
dc.description.abstract | The spontaneous release of tumor cell antigens from the cell surface into the circulation has been proposed as a mechanism whereby tumors may escape the immune response of the host. In this study we have found that Ehrlich ascites tumor cells after removal from the host (mouse) spontaneously release significant amounts of cell surface components during incubation for 1 h in cold isotonic buffer. Immunodiffusion studies revealed that immunoglobulin G (IgG) and a complement component (C3) are included in this spontaneously released material. These surface-bound humoral immune components are apparently released in the form of a high-molecular-weight aggregate (cell coat particle) as shown by ultracentrifugation and ultrafiltration experiments. Precipitation of IgG from the cell coat particle preparation with antibodies directed against mouse IgG followed by detergent gel electrophoresis of the immune precipitate revealed five major bands in addition to the heavy and light chains of IgG. These results suggest that host IgG is tightly bound to several other components at the cell surface, perhaps in the form of immune complexes. IgG is localized on the tumor cell surface in a highly heterogeneous pattern with the appearance of patches and caps in some cells as shown by immuno-fluorescence analysis. The possibility that humoral immune components bind to the tumor cell surface and result in the shedding of high-molecular-weight aggregates of cell surface antigens into extracellular fluids is discussed. | en_US |
dc.format.extent | 892885 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Alan R. Liss, Inc. | en_US |
dc.publisher | Wiley Periodiocals, Inc. | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Molecular Cell Biology | en_US |
dc.title | The spontaneous release of a high-molecular-weight aggregate containing immunoglobulin G from the surface of Ehrlich ascites tumor cells | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.identifier.pmid | 571032 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/38207/1/400090311_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/jss.400090311 | en_US |
dc.identifier.source | Journal of Supramolecular Structure | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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