Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04626 (erbB-2)
 5,251 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Class-switched monoclonal antibody SV2-61r recognized the extracellular domain of c-erbB-2 protooncogene products separate from the epidermal growth factor receptor. We studied the potential of SV2-61r for evaluating the amplification of c-erbB-2 protooncogene on cancer cells, which has been reported to have prognostic value in adenocarcinoma patients. Radiolabeled SV2-61r specifically bound to various adenocarcinoma cells in addition to c-erbB-2-transfected NIH-3T3 cells (A4) with the affinity constant of 4.4 x 10(8) M-1. SV2-61r injected i.v. localized well to A4 cells xenografted in nude mice. Tumor uptake and localization index of radioiodinated SV2-61r were lower than those of 111In-labeled SV2-61r, probably due to the internalization and dehalogenation of formed antibody-antigen complexes. Biodistribution and specificity of targeting were assessed by comparison among three cells, A4, lung cancer SBC-3 (c-erbB-2 weakly positive) and B-lymphoblastoid Manca cells (c-erbB-2 negative). Tumor:blood ratios, obtained 48 h after injection, were 5.63, 1.45, and 0.68, respectively, indicating the potential of 111In-labeled SV2-61r for evaluating the amplification of c-erbB-2 protooncogene on cancer cells. Because of its close relationship with carcinogenesis and the uniform expression, c-erbB-2 protooncogene products seem to be the optimal target of imaging and therapy of adenocarcinoma patients.
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PMID:Scintigraphic detection of overexpressed c-erbB-2 protooncogene products by a class-switched murine anti-c-erbB-2 protein monoclonal antibody. 167 Oct 1

A sandwich radioimmunometric assay using monoclonal antibodies 6G10 and SV2-61 gamma directed to the extracellular domain of the c-erbB-2 oncogene product was developed and the antigen levels in sera from normal donors and patients with breast carcinoma were determined. The antigen levels in normal donors were uniformly low (9.52 +/- 0.91 ng/ml) and 3.0% (2/66 cases) slightly exceeded the cutoff value (11.4 ng/ml). In patients with breast carcinoma, serum c-erbB-2 protein levels increased and the positivity was as high as 45.7% (16/35 cases) in recurrent cases. Determination of c-erbB-2 protein may be a useful marker for serological diagnosis of breast carcinoma.
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PMID:[Development of sandwich radioimmunometric assay for serum c-erbB-2 oncogene product and its significance in diagnosing breast carcinoma]. 168 26

A murine IgM monoclonal antibody, designated SV2-61, was generated against human c-erbB-2 gene-transfected NIH-3T3 (SV11) cells. SV2-61 defined a 185-kDa molecule present on the surface of SV11 cells, another line of c-erbB-2 gene-transfected NIH-3T3 (A4-15) cells, and MKN-7 human gastric cancer cell line carrying an amplified human c-erbB-2 gene. The SV2-61-defined antigen was found to show protein kinase activity in vitro. The SV2-61 was reactive with human c-erbB-2 gene-transfected NIH-3T3 cell lines but not with transfectants carrying c-erbB-2 gene mutants which lack a coding region for the extracellular domain. It was reactive with a portion of human epithelial cell lines but not with native NIH-3T3, TGF-alpha-coding gene-, activated c-raf gene- or Ha-ras gene-transfected NIH-3T3 cells, or non-epithelial human cells. These results indicate that the SV2-61 is an antibody which recognizes an extracellular domain of the c-erbB-2 gene product, 185-kDa protein.
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PMID:A murine monoclonal antibody that recognizes an extracellular domain of the human c-erbB-2 protooncogene product. 256 25

Monoclonal antibodies (mAbs) were modified with a photo-cross linker, sulfosuccinimidyl 2-(m-azido-o-nitrobenzamido)-ethyl-1,3'-dithiopropionate (SAND), and their efficacy in immunohistochemical staining of tissue sections was examined comparatively with that of unmodified mAbs. mAbs used were HBJ127 and SV2-61 gamma which recognized a proliferation-associated human gp125 cell surface antigen and a human c-erbB-2 protooncogene product, respectively. Both mAbs could stain relevant cancer tissue in frozen sections but not that in paraffin sections. Whereas SAND-modified mAbs intensely stained the cancer tissue in paraffin sections too, and the UV irradiation to SAND-modified mAb-treated tissue sections further increased the intensity of the staining. Scatchard plot analysis using 125I-labeled mAbs indicated that the augmentation of staining capacity by the SAND modification is due to the increase of the mAb amount capable of binding to the antigen.
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PMID:Efficient immunostaining of tissue sections with chemically modified monoclonal antibody. 769 66

Modification of monoclonal antibodies (mAbs) with a photo-crosslinker, sulfosuccinimidyl 2-(m-azido-o-nitrobenzamido)-ethyl-1, 3'-dithiopropionate (SAND), enhanced their antigen binding activity. By SAND modification, SV2-61 gamma mAb against human c-erbB-2 protooncogene product could immunoprecipitate approximately an 8-fold greater amount of antigen, and AB-3 mAb against bovine serum albumin (BSA) bound to BSA more efficiently than unmodified mAb as determined by an enzyme-linked immunosorbent assay. Relative binding affinity of SAND-modified AB-3 was about 4-fold of unmodified AB-3. Augmented binding of mAbs was observed with or without photosensitization.
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PMID:Enhanced binding to antigen of monoclonal antibodies modified with a crosslinker. 809 84

The human c-erbB-2 protooncogene product (erbB-2 protein) is a 185 kilodalton glycoprotein closely related to epidermal growth factor receptor protein. In this study, we measured the concentration of circulating erbB-2 protein in cancer patients by means of a new immunoradiometric assay (IRMA). Two monoclonal antibodies (MoAbs), SV2-61 gamma and 6G10, recognize erbB-2 protein but bind to separate epitopes. SV2-61 gamma was used as an immunoadsorbent and 6G10 as an 125I-labeled probe. A serum was considered positive for erbB-2 protein if the percent binding exceeded the mean of the normal group by more than 3 standard deviations. Eleven of 21 patients with advanced breast cancer and 1 of 15 with advanced gastric cancer were positive. Serum erbB-2 protein levels correlated well with the therapy and the status of the patients with breast cancer. On the contrary, all patients with advanced colon, ovarian, or pancreatic cancers, showed levels below the cut-off value. These results suggest that circulating erbB-2 protein can be measured using the newly constructed IRMA. Since c-erbB-2 protooncogene amplification and overexpression are accepted as a good marker of aggressiveness, relapsing potency, and poor prognosis, this IRMA should be a promising tool with which to help manage breast cancer patients.
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PMID:Construction of immunoradiometric assay for circulating c-erbB-2 protooncogene product in advanced breast cancer patients. 809 2

In this report, we characterized the c-erbB-2 gene and its product in prostatic cancer cells. Three prostatic cancer cell lines (PC3, DU145 and TSU-Pr1), one primary prostatic cancer and four benign prostatic hyperplasias (BPH) were studied. In reverse transcribed polymerase chain reaction, c-erbB-2 mRNA was demonstrated in all three cell lines and prostatic cancer tissues as well as BPH. The c-erbB-2 protein was expressed higher in prostatic cancer cells and tissues as compared with benign tissue by enzyme immunoassay, but it was not statistically significant. Immunohistochemical study, with the monoclonal antibody SV2-61gamma that recognizes the extracellular domain of c-erbB-2, showed that all the prostatic tissues and cells had reactivity. Antigenicity was mainly in the cytoplasm. Analysis of genomic DNA failed to disclose gene amplifications or rearrangements of c-erbB-2 in both prostatic cancer and BPH. The sequence of amplified c-erbB-2, which corresponds to transmembrane domain, disclosed wild type in all prostatic cancer cells. These results demonstrate that although the number is limited, c-erbB-2 gene and protein are expressed in prostatic cancers and benign prostates. In the previous studies on c-erbB-2 expression in prostatic tissue, mainly conducted by immunohistochemistry, its frequency varies among each study, ranging from less than 0% to 100%. Therefore, to evaluate the c-erbB-2 in prostatic tissue precisely, it is also necessary to detect mRNA of c-erbB-2 as demonstrated in our study.
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PMID:Analysis of protooncogene c-erbB-2 in benign and malignant human prostate. 1040 5