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At least 19 recordsLinked to original sources
PubMed1980

Radioimmunodetection of gastrointestinal neoplasms with antibodies to carcinoembryonic antigen.

Primary and secondary gastrointestinal tumors have been identified using sheep immunoglobulin G antibody to carcinoembryonic antigen radiolabeled with 131I. 99mTc-pertechnetate and 99mTc-human serum albumin were used to identify tissue spaces and blood pool and to facilitate external substraction imaging. In 13 patients with tumors, 4 of 5 primary sites and 8 of 11 secondary sites were successfully demonstrated. Two patients with benign disease had negative scans. Comparison with conventional methods of scanning showed good correlation.

Antibodies, Neoplasm↗
PubMed1982

An immunohistochemical study of nasopharyngeal neoplasms using keratin antibodies: epithelial versus nonepithelial neoplasms.

Forty cases of nasopharyngeal neoplasia were analyzed using immunohistochemical staining employing keratin antibodies. Using this probe the tumors were classified as being keratin-positive or negative. In this study, all squamous cell carcinomas labeled with keratin antibodies whether they were classified as keratinizing or nonkeratinizing by usual staining methods. In contrast, lymphoid and mesenchymal tumors of the nasopharynx did not label with keratin antibodies. Thus, the presence of keratin proteins as detected by immunohistochemical means on paraffin-embedded tissues appears to be a useful, reliable, and sensitive method for aiding in the accurate diagnosis and classification of nasopharyngeal neoplasms.

Antibodies↗
PubMed1987

Immunostaining for leukocyte common antigen using an amplified avidin-biotin-peroxidase complex method and paraffin sections. A study of 735 hematopoietic and nonhematopoietic human neoplasms.

Antibodies to leukocyte common antigen (LCA) are valuable in surgical pathology in the diagnostic separation of malignant lymphomas from poorly differentiated neoplasms of other types. However, several publications have reported difficulty in obtaining adequate LCA labeling in paraffin-embedded specimens. To assess this problem further, we applied an amplified version of the avidin-biotin-peroxidase complex procedure to 315 formaldehyde-fixed hematopoietic malignancies, and 420 nonhematopoietic tumors that had been similarly processed. All non-Hodgkin's lymphomas were LCA-reactive with this method, whereas none of the nonhematopoietic neoplasms were stained. Twelve of 25 cases of Hodgkin's disease displayed LCA-positivity in Reed-Sternberg cells, but all contained reactive, benign inflammatory cells. Hence, the specificity of the amplified anti-LCA/avidin-biotin-peroxidase technique was 100%, and its sensitivity was 96%. This procedure should allow surgical pathologists to obtain reliable, reproducible staining of hematopoietic neoplasms in paraffin-embedded tissues.

Antibodies, Monoclonal↗
PubMed1995

Analysis of proliferative grade in glial neoplasms using antibodies to the Ki-67 defined antigen and PCNA in formalin fixed, deparaffinized tissues.

In an effort to optimize immunocytochemical methods to evaluate cell kinetics in brain tumors, we studied two newly-developed antibodies which react with formalin resistant epitopes of Proliferating Cellular Nuclear Antigen (PCNA) and Ki-67. These results were compared with standard flow cytometric cell cycle data from the same tumor specimens to determine if these methods correlate with each other, and whether retrospective analysis using these antibodies is feasible for cell kinetic analysis of brain tumors. Thirty-one specimens of glial tumors submitted for flow cytometry during 1992 were also reacted with antibodies to PCNA (PC-10) and Ki-67 (MIB-1). Flow cytometry scores for S-phase Fraction were compared with immunocytochemical scores for both antibodies, using an arbitrary rating of 1 (low, < 4%), 2 (intermediate, 4-6%), 3 (high, > 6%), and 1 (< 25% positive), 2 (26-75% positive), 3 (> 75% positive), respectively. MIB-1 results were found to correlate significantly with the S-phase fraction as determined by flow cytometry. The MIB-1 data showed a trend toward underestimating, i.e., lower scores, the proliferative index compared with flow cytometry. There was less of a correlation between PC-10 antibody scores and flow cytometry S-phase fraction, as PC-10 immunostaining typically overestimated the proliferative rate of brain tumors when compared with flow cytometry. There was an exact correlation between PC-10 and MIB-1 in only 4 cases, whereas in the remaining specimens, PC-10 results were always higher than MIB-1.(ABSTRACT TRUNCATED AT 250 WORDS)

Antibodies, Monoclonal↗
PubMed1983

Monoclonal antibodies against gastrointestinal tumour-associated antigens isolated as monosialogangliosides.

Monoclonal antibodies were produced after immunization of mice with a colorectal adenocarcinoma cell line or liver metastasis membranes from a patient with colon adenocarcinoma. Many monoclonal antibodies were found to react with colorectal adenocarcinoma cells but not with normal colon mucosa, blood lymphocytes, myeloma cells or lung epithelial carcinoma cells. Three of these 'colorectal tumour-specific' antibodies appear to define different antigens that were found in the complex monosialoganglioside fraction from 60 to 90% of the colorectal and pancreatic adenocarcinoma tumours or metastases examined but essentially lacking in normal colon mucosa and other normal or tumour tissues tested.

Adenocarcinoma↗
PubMed1975

Investigations for skin antibodies in malignant neoplasms.

A group of 451 patients with various malignant neoplasms was investigated for the presence of antibodies against the intercellular substance in epidermis and against the basement membrane in the skin, using the immunofluorescence method. None of the patients had bullous disease. Circulating basement membrane antibodies were found in a 63-year-old man with lung cancer. None of the patients had antibodies against the intercellular substance. No in vivo bound intercellular or basement membrane antibodies were found.

Antibodies, Neoplasm↗
PubMed1992

Isolation and characterization of a monoclonal antibody, K1, reactive with ovarian cancers and normal mesothelium.

We have isolated a new monoclonal antibody (MAb), K1, that reacts with an epitope on the surface of human ovarian carcinoma cells. This antibody was generated by immunization of mice with periodate-treated human ovarian carcinoma (OVCAR-3) cells. These mice had been previously made tolerant with normal human kidney membranes. Spleen lymphocytes from these mice were selected prior to fusion using a panning purification method on living OVCAR-3 cells. Initial screening of surface-reactive clones was performed in a single day using immunofluorescence on living OVCAR-3 cells, and secondary screening was performed using immunoperoxidase histochemistry on cryostat sections of normal human tissues and human tumors. The K1 clone was subcloned and identified as an IgM isotype, but was subsequently isotype-switched to IgG1K using a panning selection method. When evaluated by immunohistochemistry, the antigen reactive with K1 was found in many ovarian non-mucinous tumors, as well as in squamous tumors of the esophagus, and cervical cancer. The only normal adult human tissues showing uniform reactivity with K1 were the mesothelia of the peritoneal, pleural and pericardial cavities. There was also limited reactivity with epithelia of the trachea, tonsil and Fallopian tube. A similar tissue reactivity for K1 was found in tissues from cynomolgus monkeys. K1 reacted with many of the same tissues and tumors as the previously identified antibody OC125, but several lines of evidence indicate that K1 reacts with a different epitope and probably a different molecule, when compared to OC125. This evidence included assays employing immunofluorescence competition, double-label immunofluorescence, and solid-phase and live-cell radioimmunoassays. Since our data indicate that the antigen reactive with the K1 antibody is a new molecular species, we have named the antigen CAK1. Unlike the shed antigen CA125, CAK1 was only cell-associated and was not found in the supernatant of cultured OVCAR-3 cells or in the blood of ovarian cancer patients. The K1 antibody may be useful as a targeting agent for therapy and in the diagnosis of ovarian carcinoma, as well as some other human cancers.

Antibodies, Monoclonal↗
PubMed2000

Epitope-specific antibody response to HT-1080 fibrosarcoma cells by mimotope immunization.

Mouse monoclonal antibody (mAb) BCD-F9, which recognizes an unknown antigen found on the surface of many tumor cells, was used to screen a phage display library expressing random peptide decamers. The phage that was selected encoded the unique sequence GRRPGGWWMR, representing the peptide capable of binding to the BCD-F9 mAb. The peptide was synthesized and found to specifically inhibit the binding of mAb to HT-1080 fibrosarcoma cells. Alanine mutagenesis of the sequence encoding this peptide indicated that three residues, PXXWW, were critical for its binding to the BCD-F9 mAb. Polyclonal antibodies generated by immunization of rabbits with the synthetic peptide GRRPGGWWMR (anti-mimotope antiserum or AM-F9) bound specifically to HT-1080 cells and inhibited the binding of the BCD-F9 mAb to these cells. Using an experimental animal model in which CD-1 nude mice are inoculated i.v. with HT-1080 cells, develop lung metastasis, and die within 30 days, we have shown that AM-F9 could significantly prolong the life span of these animals. Our results suggest that a peptide mimotope can potentially be used as a novel immunotherapy to induce a beneficial antitumor response.

Amino Acid Sequence↗
PubMed1976

Humoral reactions in syngeneic hosts against tumor cell surface incomplete saccharide moieties.

Components on the surface of MM2 ascites mammary carcinoma cells induce agglutination factors in the serum of syngeneic host C3H/He mice, and bind the factors in vitro. These components have been classified into three groups: MM2-specific substances, mammary tumor virus (MTV)-associated substances and tumor-associated embryonic materials. The substances contained saccharide moieties and their terminal sugar residues were essential for the binding of the serum factors. These terminal saccharides were exposed during cell proliferation,but masked in stationary cells, at least partly, due to elongation of the saccahride moieits. The terminal structures of these polysaccharide moities of growing and stationary cells were studied by semiquantitative tumor cell agglutination using the agglutinating activities against MM2 cells of MM2-regressor serum and of FMA/R- and Ehrlich-regressor sera which had partial cross-agglutination activities. Agglutination by phytohemagglutinins, inhibition of the agglutination by saccharides or with isolated cell surface components and treatment of the cells with glycosidases were also used for this purpose.

Agglutination↗
PubMed1975

Endogenous immune complex nephropathy associated with malignancy I. Studies on the nature and immunopathogenic significance of glomerular bound antigen and antibody, isolation and characterization of tumor specific antigen and antibody and circulating immune complexes.

Three patients with clear cell renal carcinoma and one with another intrarenal malignancy were studied for the presence of glomerular localized immunoglobulins, complement components and tumor specific antigen and antibody by immunofluorescence. To determine the association and elucidate the pathogenic mechanisms involved in the relationship between tumors and glomerular deposits, antibody eluted from tumor tissue and renal glomeruli, cryoproteins, serum antibodies and rabbit antisera to tumor tissue were tested for specificity to antigen. The relationship between tumor antigens and the lipoprotein antigen localized in normal proximal tubular brush border (RTE) and the small bowel mucosa, was studied by immunofluorescence, absorption and blocking studies as well as complement fixation. Immunoglobulins and complement components were localized in the glomeruli and tumor membrane of all patients. Sera and glomerular fixed antibody from three patients with renal cell carcinoma localized to normal proximal tubular brush border and jejunal mucosa as well as to tumor membrane and the glomeruli and proximal tubules of all of these three patients. Anti RTE activity was also detected by complement fixation. Immunologic similarity between RTE and renal cell carcinoma antigen was confirmed by absorption studies. Furthermore, cryoprecipitable complexes of tumor antigen and specific antibody were isolated from the serum. The tumor antibody was immunologically similar to RTE. In the other case the rabbit anti-tumor antibody and the patient's serum fixed to the tumor membrane and kidney of the patient but did not show cross reactivity with the renal cell carcinoma or RTE. These studies suggest that the tumor antigen in renal cell carcinoma is similar to RTE and the glomerular deposits represent tumor antigen and antibody complexes. In addition these investigations support the hypothesis that tumor immune complexes are significant in the glomerular lesions, and that the origin of renal cell carcinoma is in the proximal tubule. The investigations also show that tumor antibodies are specific for tumors of the same morphological type but not for other tumors in the same tissue. Moreover, the renal glomerulus appears to be a chosen anatomic site for deposition of tumor antigens and antibodies and studies of the kidney may provide insight into the nature of tumor antigens and antibodies. Cryoprecipitation appears to be a valuable method in isolation of tumor complexes and characterization of tumor specific antigen and antibody.

Absorption↗
PubMed1983

Monoclonal antibodies to human colon and colorectal carcinoma.

A series of monoclonal antibodies was produced by immunizing mice with fresh carcinoma of the colon and with the cell line HT-29. These antibodies could be classified into 3 different groups: (a) those which were HT-29 specific and reacted with no other cell line or fresh colon carcinoma samples; (b) antibodies which reacted with HT-29 and were also reactive with a number of other in vitro cell lines; and (c) antibodies which appeared to be specific for carcinoma of the colon cell lines in that they reacted selectively with colon carcinoma cell lines and not with carcinoma lines derived from other tissues. It was clearly shown by immunoperoxidase staining of both normal and neoplastic cells of the gastrointestinal mucosa, from stomach to colon, that these antibodies were not tumour-specific. Indeed, one antibody (250-30.6) has a remarkable specificity for secretory epithelium of any tissue whether it be found in the gastrointestinal tract, respiratory system or urinary system. We question the existence of tumour-specific antigens detected by monoclonal antisera described thus far, and comment on the remarkable specificity of some of the sera produced, emphasized by the secretory cell-specific antibody described herein.

Animals↗