摘要:

In this study, an IgM monoclonal antibody (MAb600D11) directed against human small cell lung cancer (NCI-H69) was radiolabeled with iodine-131, and the biodistribution and image quality of the radiolabeled antibody was evaluated. Radiolabeling was achieved in a solid-phase system consisting of l,3,4,6-tetrachloro-3a,6a-diphenylglycoluril. Labeling efficiencies and protein purification were accomplished using gel exclusion chromatography while radioimmunoreactivity was determined using a solid-phase radioimmunoassay procedure. The biodistribution of I-131-labeled MAbs was determined in Sprague-Dawley rats up to 7 days after injection. Highest organ concentrations were observed in liver (3.91 ± 0.47 (SD) and 0.17 ± 0.04 (SD) mean percent injected dose at 1-7 days after injections) and in thyroid (5.33 ± 0.71 (SD) and 5.32 ± 2.01 (SD) mean percent injected dose at 1-7 days after injection). Nude mice, bearing either a small cell lung tumor (NCI-H69) or a nonspecific tumor (adenocarcinoma), were injected with 400-800 μCi of I-131 labeled monoclonal antibody. Optimum tumor visualization was observed 2-4 days after injection with tumor concentrations as high as 10.4% of the initial injected dose. The results demonstrated that radioimmunoimaging of human small cell lung carcinoma was feasible with the tumor-specific IgM I-131-labeled

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.1

年代:1985

数据来源: MAL

摘要:

Neuron-specific enolase (NSE) has been increasingly recognized as a marker for neuroendocrine tumors including small cell carcinoma of the lung (SCCL). To prepare monoclonal antibodies (MAbs) specific for human NSE, we first developed a simple method of purifying NSE by direct chromatofocusing of a crude extract of human brain tissue. BALB/c mice were then immunized with our preparation of NSE, and MAbs against NSE were generated utilizing a hybridoma technique. The antibodies were screened against both NSE and non-neuronal enolase (NNE) by a solid-phase radioimmunoassay (SPRIA). After cloning and subcloning of hybridomas, two groups of anti-NSE MAbs were identified by SPRIA. One group reacted specifically with NSE but not with its isoenzyme NNE, irrespective of whether antigens were glutaraldehyde fixed or unfixed. A second group reacted with both NSE and NNE when the latter were glutaraldehyde fixed, but surprisingly with neither antigen in the absence of fixation. Group I antibodies were further characterized by immunoblotting, and by immunocytochemistry of normal brain and liver sections and sections of SCCL. The results further supported the specificity of group I antibodies for NSE. These MAbs have potential utility in the diagnosis and management of neuroendocrine tumors, and in further understanding the biology of NSE.

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.13

年代:1985

数据来源: MAL

摘要:

A comparative study of expression of class I major histocompatibility (MHC) antigens among lung, spleen, kidney, heart, liver, and brain tissues of the rat was performed. Monoclonal antibodies (MAbs) against RT1Aadeterminants were conjugated to125I and applied to frozen sections. Resulting autoradiograms showed antigen reactivity in lymphoid tissue, bronchial and alveolar epithelium, and endothelium of the lung. The Iymphoid tissue of the lung and spleen demonstrated the antigen after shorter autoradiographic exposures than was required for the epithelial components of these organs. The kidneys were heavily labeled over the glomeruli, but less intensely over the tubular epithelium. RT1A antigen content of capillary endothelium of the heart was demonstrable before that of the muscle bundles. In the liver, autoradiographic sections revealed high determinant density in sinusoidal regions. Brain sections show reproducibly low levels of labeling, with the exception of vascular structures. All of these tissues from PVG-RT1cand PVG-RT1uanimals show only background labeling.

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.27

年代:1985

数据来源: MAL

摘要:

Eight monoclonal antibodies (MAbs) raised against human prostate cancer cell lines are described. One MAb was derived from the fusion of mouse myeloma P3x63Ag8-653 cells with spleen cells of mice immunized with DU145 prostate cancer cells. The other seven were from the fusion of myeloma lines P3x63Ag8-653 or SP2/0 with spleen cells of mice immunized with PC3, DU145 and 1013L prostate cancer cells. All of the antibodies also reacted with cell lines of other human cancer types, especially carcinomas. Immunoperoxidase staining on fixed tissue revealed strong reactivity only with antibody PrN10. Seven other antibodies seemed to bind to cell surface-associated (glyco)proteins. Antibodies PrL22 and PrOll showed similar reactivity in radioimmunoassay, and immunoprecipitated a 160 kD molecular weight polypeptide from [125I]lactoperoxidase-labeled cells. Antibodies PrHk and PrQ12 bound to molecules with apparent MW of 115 kD and 100 kD, respectively; antibodies PrM24 and PrP14 revealed a more complex picture in immunoprecipitation of surface-labeled cells.

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.37

年代:1985

数据来源: MAL

摘要:

Three kind s of hybridomas secreting monoclonal antibodies (MAbs) against the ε chain of human IgE were constructed by somatic cell hybridization between mouse myeloma P3U1 cells and spleen cells from BALB/c mice immunized with human IgE purified from the culture supernatant of U-266 cells. These MAbs were used effectively for the purification and determination of human IgE. The recognition site in the IgE molecule of each antibody was examined by using various ε chain fragment peptides produced inEscherichia coli. From these experiments, it was suggested that one recognized Cε2 and the second Cε4. The third did not recognize the Cε1-Cε4 domains of the recombinant ε chain fromE. coli, although it bound to the ε chain of natural hu

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.47

年代:1985

数据来源: MAL

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.55

年代:1985

数据来源: MAL

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.56

年代:1985

数据来源: MAL

ISSN:0272-457X    

DOI:10.1089/hyb.1985.4.87

年代:1985

数据来源: MAL