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Radioimmunoscintigraphy with 111In labelled monoclonal antibody fragments (F(ab')2 BW 431/31) against CEA: radiolabelling, antibody kinetics and distribution, findings in tumour and non-tumour patients.

Forty seven patients with suspected malignant disease (mainly colorectal cancer) were studied with 111In labelled F(ab')2 fragments of an anti-CEA monoclonal antibody (BW 431/31). The kinetic data revealed a long whole body retention of the label (62% after 4 days) and a rapid blood clearance (77% within 24 h, 89% within 48 h) leading to an early positive tumour contrast 24 h p.i. and optimal scintigrams 48 h p.i. Diagnostic results were promising in local recurrences of colorectal cancer (8/10 positive = 80%) though false positive findings in patients with inflammatory bowel disease occurred probably due to cross-reaction with a human granulocyte antigen. Liver metastases and tumours neighbouring liver and spleen were often missed (10/27 = 37%) because of high nonspecific uptake in these organs. Thus BW 431/31 proved to be a suitable compound for radioimmunodetection, however, further improvements to optimize tumour affinity and specificity of the antibody are mandatory.

Aged↗

Enhanced tumor localization of monoclonal antibody by treatment with kininase II inhibitor and angiotensin II.

The effect of kininase II inhibitor, enalapril, on the delivery of monoclonal antibody A7 to the targeted tumor was investigated using athymic mice bearing human colon cancer, SW1116. Enalapril alone, which enhances tumor vascular permeability through the kinin-generating cascade, did not increase the uptake of 125I-labeled A7 (125I-A7) in SW1116 due to the systemic hypotension induced by its inhibitory effect on angiotensin converting enzyme. However, with combined angiotensin II (AT-II) and enalapril treatment, a 2-fold increase in the accumulation of 125I-A7 was seen when compared to A7 alone. This marked increase was presumably due to increased tumor vascular permeability induced by enalapril combined with the absence of hypotension due to the actions of AT-II. This approach might be useful in radioimmunodetection and immunotargeting chemotherapy using monoclonal antibody.

Angiotensin II↗

Use of I-131 labeled, murine Fab against a high molecular weight antigen of human melanoma: preliminary experience.

High molecular weight antigen (HMWA) is a tumor-associated proteoglycan of human malignant melanoma. I-131 labeled Fab fragments of these specific antibodies were used for preliminary feasibility studies for radioimmunodetection and therapy of human subjects who had inoperable metastatic melanoma. Ten patients received tracer doses of 5-13 mCi (185-481 MBq) of I-131 (anti-HMWA) Fab. All patients (8/8) who had melanoma lesions greater than 1 cm by correlative diagnostic methods had one or more lesions that had localization to tumor of the radiolabeled Fab. In all, 17 of 23 (74%) documented metastases were seen. There were no false positives in this series. Two patients who had avid uptake received potentially radiotherapeutic doses of 142 mCi (5,254 MBq) (one patient) and 181 mCi (6,697 MBq) and 193 (7,141 MBq) (total: 374 mCi or 13,838 MBq) (one patient). For both of these patients, whole body imaging studies showed that the localization of the high dose I-131 Fab was predominantly in tumor. The patient who received the larger dose showed a greater than 50% reduction in the size of pelvic and pericaval nodes, with stabilization of disease at the smaller nodal size for a period of three months. On whole body images, the anti-Fab HMWA appears to be more tumor selective than Fab preparations that target the p97 antigen for melanoma, and there is less uptake in liver.

Animals↗

Radioimmunoimaging of venous thrombi using iodine-131 monoclonal antibody.

Murine monoclonal antibody (Mab) specific for the NH2-terminal region of human fibrin, but not cross-reactive with fibrinogen, was used in radioimmuno-imaging of fresh, induced venous thrombi in three dogs. Iodine-131-labeled Mab was injected intravenously, with iodine 125-labeled polyclonal murine gamma-G globulin (IgG) simultaneously injected as a control. Images were strongly positive at 24 and 48 hours in all three animals, with thrombus-to-blood and thrombus-to-muscle ratios of 8.4 and 228.0, respectively, for I-131-labeled Mab; these ratios for control IgG were 1.2 and 13.0. Radioimmunodetection of thrombi in vivo is feasible in dogs and may have clinical application since Mab is specific to human fibrin.

Animals↗

Antiferritin antibodies in immunoscintigraphic detection of human tumor xenografts.

Affinity-purified antibodies against human placental ferritin and their F(ab)2 fragments labeled with 131I were examined for suitability for radioimmunodetection of ferritin-containing tumors. The nude mouse model (BALB/c, nu/nu) with xenografts of HeLa cell tumors and human adenocarcinoma of the rectum (with proven ferritin content) was used. Gamma-camera imaging and tissue distribution studies revealed that both kinds of tumor selectively accumulate antiferritin antibodies and their fragments. In large necrotic tumors nonspecific uptake of radiolabeled normal IgG occurred, but otherwise there was no tumor localisation. This study, in accordance with the literature, confirms the utility of antiferritin antibodies for the detection of human tumors in an animal model.

Adenocarcinoma↗

Cytokeratins and tissue polypeptide antigen.

Cytokeratins (CKs), which are biochemically related to intermediate filaments (IFs), form an intracellular network of filaments that is believed to participate in maintaining the structural integrity of cells. Twenty individual polypeptides, divided into two groups, constitute the cytokeratin family. Each type of epithelial cell can be characterized by its content of cytokeratin polypeptides since the expression pattern varies with the type of epithelium. During transformation of normal epithelial cells into malignant cells, the cytokeratin patterns are usually maintained. This property has enabled the use of cytokerations as histological tumor markers, especially for tumors that are not easily classified. Cytokeratins 8, 18 and 19 are the most abundant cytokeratins in carcinomas. They are released into necrotic areas and can be found intratumorally and in blood, circulating as partially degraded complexes, and can as such be used as tumor markers. Cytokeratin deposits in tumors make these structures potential targets for radioimmunodetection and immunotherapy. The usefulness of tissue polypeptide antigen (TPA) as a serological tumor marker has been known for a long time. TPA is a molecular complex containing CK 8, 18 and 19 and determinations of TPA in serum samples can be used in the follow-up of patients with many types of cancer.

Biomarkers, Tumor↗

Imaging of primary and metastatic liver cancer with 131I monoclonal and polyclonal antibodies against alphafetoprotein.

Thirteen patients with a history of confirmed liver carcinoma were given either I131 goat polyclonal or murine monoclonal antibodies against alpha-fetoprotein (AFP), and then scanned with a gamma camera. In order to reduce background, nontarget activity, especially in the liver, blood pool, and reticuloendothelial system, 99mTc imaging agents were used for tumor image enhancement by computer-assisted subtraction. A sensitivity of 91% for the primary site, 50% for the lungs (33% for the chest area), and 75% for the abdomen and pelvis was achieved, with a specificity of 100%, 94%, and 100% for these sites, respectively. The accuracy was determined to be 93% for the liver, 86% for the lungs (77% for the chest), and 85% for the abdominal and pelvic area, resulting in an overall accuracy rate for imaging primary and metastatic hepatocellular cancer of 84% (90% if bone metastases are excluded). In two of the 13 patients, lesions that had been missed by conventional liver scintigraphy and transmission computed tomography (CT) were first shown by radioimmunodetection (RAID).

Abdominal Neoplasms↗

Tumor suppressive monoclonal antibody belonging to the V(H) 7183 family directed to the oncodevelopmental carbohydrate antigen on human hepatocellular carcinoma.

Hep27 monoclonal antibody (Hep27 Mab) was raised by immunizing BALB/c mice with cells of the Thai human hepatocellular carcinoma (HCC) cell line HCC-S102 using hybridoma technology. The Hep27 Mab recognizes oncofetal development antigens by reacting with many HCC, other cancers, fetal and newborn liver but not adult liver. The Hep27 Mab alone markedly inhibits the growth of hepatocellular carcinoma cell lines (65% viability on the third day), suggesting its clinical usefulness. Moreover, complementary DNA (cDNA) for active variable regions of both heavy and light chains of the antibody has been cloned. Sequence analysis of the variable region of the Hep27 Mab revealed that the V(H) and V(L) genes belong to the V(H) 7183 and V(K) families, respectively. We have also characterized the reactivity of the Hep27 Mab to synthetic carbohydrate epitopes and 1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP)-treated HCC-S102 cells. The results showed that the Hep27 Mab recognizes a neoglycolipid containing a mucin core unit and PDMP treatment reduced Hep27 Mab binding activity to HCC-S102 cells, indicating that the Hep27 Mab recognizes a glycolipid antigen on HCC-S102 cells. This Mab may be potentially useful for studying antigenic expression in hepatocellular carcinoma and as a targeting agent for radioimmunodetection and immunoconjugated therapy.

Journal Article↗

Tumor localization and biodistribution with radiolabeled monoclonal antibody against pancreatic cancer in tumor-bearing nude mice.

Nd2 is a murine monoclonal antibody produced against a mucin fraction purified from xenografts of a human pancreatic cancer cell line SW1990. Immunoperoxidase staining showed that the antigen recognized by Nd2 was present in 82.9% of pancreatic cancer tissues but not in tissues of normal pancreas and chronic pancreatitis. However Nd2 antigen was found not to be elevated in the sera of patients with pancreatic cancer. Four days after injection of 111In-Nd2 into athymic nude mice bearing SW1990 xenograft there was a higher accumulation in the tumor compared to 111In-normal mouse IgG1. When these mice were scanned with a gamma camera, labeled Nd2 was shown to accumulate in the tumor rapidly on the 1st day after injection and by the 4th day tumor accumulation was more distinctly visualized than non-specific accumulation in liver. These results indicate that Nd2 has high specificity and reactivity for pancreatic cancer and may have possible applicants in radioimmunodetection or targeting of therapeutic drugs in pancreatic cancer.

Animals↗

Human monoclonal antibody against colon cancer.

The purpose of the study was to produce human monoclonal antibodies (hMcAb) against human colon cancer for use in radioimmunoimaging. Human-mouse heterohybridomas were developed by fusing SHM-D33 mouse-human hybrid heteromyeloma cells with human lymphocytes from colon cancer tumor-draining lymph nodes. The hybridomas capable of secreting human monoclonal antibodies were screened by using human colon cancer cell lines and pathological biopsies with ELISA and immunohistochemical methods. hMcAb clone H11 was selected for a large-scale antibody production, which was purified from mouse ascites. Biodistribution study demonstrated that specific uptake of 125I-hMcAb H11 by human colon cancer xenografts was significantly higher than by normal tissues. Radioimmunoimaging of human colon cancer xenografts exhibited distinct tumor visualization during the period of 72-96 hr after intraperitoneal injection of 125I-hMcAb H11. The development of human monoclonal antibodies such as hMcAb H11 may be useful for radioimmunodetection and therapy of colon cancer.

Animals↗

Forskolin increases the expression of the pancreatic tumor antigen, Nd2, and uptake of Nd2 antibody.

Nd2 antibody recognizes an antigen that is tumor specific in pancreas. It has been used successfully in clinical radioimmunodetection studies to identify exocrine pancreatic tumors. In the present study we show that the uptake of radiolabeled Nd2 antibody by SW1990 pancreatic carcinoma cells was increased by the adenyl cyclase activator, forskolin. Dibutyryl cyclic AMP and forskolin were both effective in increasing the level of Nd2 antigen in SW1990 cells. Immunoprecipitation studies showed that the Nd2 epitope is associated with MUC1 mucin. Forskolin increased Nd2/MUC1 antigen in both a membrane fraction and a high buoyant density mucin-like fraction. Nd2 immunoreactivity was reduced by treatment of mucins with proteases and beta-mercaptoethanol. Immunohistochemical studies showed that periodate catalyzed beta-elimination greatly reduced Nd2 immunoreactivity. These results suggest that the Nd2 epitope is unusual in having characteristics of both a peptide and a carbohydrate, protease and conformation sensitivities and involvement of O-linked oligosaccharides. Nd2 antibody does not react with several known pancreatic cancer antigens. In summary, activation of the cyclic AMP pathway increased cellular uptake of Nd2 antibody and the cellular expression of the tumor-specific, mucin-associated Nd2 antigen. These results suggest a means of improving the effectiveness of monoclonal antibodies in targeting tumor antigens for the diagnosis and treatment of malignancy.

Amino Acid Sequence↗

Conjugation with (111)In-DTPA-poly(ethylene glycol) improves imaging of anti-EGF receptor antibody C225.

UNLABELLED: Significant liver uptake often limits the clinical application of radiolabeled antibodies in radioimmunodetection. The purpose of this study was to evaluate the gamma-imaging properties of an antiepidermal growth factor receptor (EGFR) antibody, C225, conjugated with heterofunctional poly(ethylene glycol) (PEG) with 1 terminus of the polymer attached to a radiometal chelator, diethylenetriaminepentaacetic acid (DTPA). METHODS: Two preparations of PEG-modified C225, one with 20% and the other with 60% amine substitution, were labeled with (111)In. The conjugates, (111)In-DTPA-PEG-C225, were injected intravenously into nude mice with EGFR-positive A431 tumors. For comparison, C225 directly labeled with (111)In was also injected. In a competitive study, mice with A431 tumors were pretreated intravenously with 100-fold excess of native C225, followed by an injection of (111)In-DTPA-PEG-C225 30 min or 20 h later. In addition, (111)In-DTPA-PEG-C225 was injected into mice with EGFR-positive MDA-MB-468 tumors and EGFR-negative MDA-MB-435 tumors. Images were acquired at 5 min and at 2, 6, 24, and 48 h after injection of the radiotracers. Regions of interest (ROIs) were drawn on the computer images around the whole body, liver, muscle, and tumor. The counts per pixel in the tumor and normal tissues were calculated. At 48 h, the mice were killed and dissected. Blood, liver, muscle, and tumor samples were removed and the radioactivity of each sample was measured. RESULTS: In A431 tumor xenografts, the tumor uptake of C225 modified with PEG was not significantly different than the uptake of unmodified (111)In-DTPA-C225. Uptake in the liver, however, was reduced by 38%-45%, and the reduction increased with increasing degree of PEG substitution. Tumors of A431 and MDA-MB-468 xenografts were clearly visualized with (111)In-DTPA-PEG-C225, whereas tumors of the MDA-MB-435 xenograft, which expresses low levels of EGFR, were not as readily visible. The tumor-to-blood ratios of (111)In-DTPA-PEG-C225 in A431 and MDA-MB-468 xenografts were about 3 fold higher than in MDA-MB-435 xenografts. Blocking EGFR by pretreatment with native C225 significantly reduced the uptake of (111)In-DTPA-PEG-C225 in the liver. The tumor-to-blood ratios in mice with A431 tumors were decreased 2.5-2.7 fold after pretreatment with a large excess of C225. Similar results were obtained with MDA-MB-468 tumor xenografts. In contrast, the tumor-to-blood ratios in mice with MDA-MB-435 tumor xenografts were not significantly different in C225-pretreated mice than in nonpretreated mice. CONCLUSION: These findings indicate that (111)In-DTPA-PEG-C225 selectively localized to the tumors expressing high levels of EGFR. PEG-modification of C225 significantly reduced its liver uptake, resulting in improved visualization of EGFR-positive tumors. Using PEG as a linker between the monoclonal antibody and metal chelator is a useful strategy to optimize the imaging characteristics of antibody-based scintigraphic agents.

Animals↗

Immunotargeting of human cervical carcinoma xenograft expressing CA IX tumor-associated antigen by 125I-labeled M75 monoclonal antibody.

The aim of our present study was to explore a potential use of 125I-labeled murine monoclonal antibody M75 that recognizes carbonic anhydrase IX (CA IX) in the immunotargeting of human cervical carcinoma xenografts in nude mice. CA IX is a hypoxia-inducible antigen, whose expression is significantly associated with carcinomas of the uterine cervix, whereas normal cervical tissue does not express CA IX protein. M75 monoclonal antibody was labeled with 125I and used to quantify hypoxic induction of CA IX expression in vitro in HeLa human cervical carcinoma cells by immunoradiometric assay. HeLa cells showed inducible expression of CA IX in vitro by hypoxia (0.1% O2) and various hypoxia mimicking agents (Co2+, Ni2+, Mn2+, desferrioxamine, o-phenanthroline and Na2S2O4). CA IX expression was also upregulated in the centre of HeLa multicellular clusters (spheroids) corresponding to the conditions of chronic hypoxia. For the immunotargeting study, 125I-M75 was intravenously injected into immunodeficient mice bearing HeLa cervical carcinoma xenografts. Biodistribution profile showed selective and preferential accumulation of 125I-M75 mAb in CA IX expressing HeLa xenografts in comparison with control unreactive 125I-T111 antibody. Specificity was also confirmed by low uptake in CA IX negative C33A xenografts. In addition, CA IX expression in cervical carcinoma xenografts was analyzed by immunohistochemistry with M75. Detailed immunohistochemical analysis of HeLa xenograft sections revealed perinecrotically intensified expression of CA IX. These results indicate that M75 mAb, recognizing CA IX antigen, has targeting properties which could be potentially useful in radioimmunodetection or radioimmunotherapy of human cervical carcinomas and derived metastases.

Adenocarcinoma↗

Expression and secretion of an assembled tetrameric CH2-deleted antibody in E. coli.

We have expressed in E. coli a functional assembled antibody variant that is secreted into the media. The antibody variant is a CH2-deleted chimeric antibody 14.18, which was previously shown to be a potentially useful reagent for radioimmunodetection of human tumors. The bacterial expression vector contains a dicistronic unit comprised of a L-chain cDNA and a CH2-deleted H-chain cDNA. For translocation across the bacterial membranes, we have replaced the natural signal peptides of the H and L chains with the signal peptide of the bacterial protein pectate lyase B. When expressed in the JM105 host under the control of the trp-lac promoter, the products were secreted into the M9 growth media to about 350 micrograms/L. The secreted antibody, which can be readily purified from the media without any denaturation or renaturation steps, retains antigen-binding activity. SDS-PAGE and nondenaturing size exclusion high-pressure liquid chromatography showed that it is a mixture of assembled HL and fully assembled H2L2. In H2L2, inter-H chain disulfide bonds are not formed, and the two HL half-molecules are likely held together by the trans interaction between the two CH3 domains.

Antigens↗

Application of anti lung adenocarcinoma monoclonal antibody recognizing cytokeratin-like cytoplasmic antigen for tumor diagnosis.

An anti lung adenocarcinoma murine monoclonal antibody (MoAb), KM195 (IgG1), was generated using mice which underwent tolerance treatment to normal lung tissues. KM195 was selected from among a number of hybridoma clones because of its advantageous reactivity such as high binding to cell membranes of lung adenocarcinoma tissues and low binding to cell membranes of major normal tissues. In a binding assay using cultured cell lines KM195 was found to bind cytoplasmic antigen in many adenocarcinoma cells. Detailed immunohistochemical analysis using paraffin-fixed tissue sections showed that many adenocarcinoma cells such as gastric cancer, colorectal cancer, pancreatic cancer, mammary cancer, ovary cancer and cervical cancer reacted positively with KM195, as well as lung adenocarcinoma cells. KM195 also positively stained a small number of normal cells found in adult and fetal tissues like lung, intestine, pancreas, liver and kidney. Western blot analysis using membrane fraction of lung adenocarcinoma tissues revealed two major KM195-positive bands which were electrophoresed nearby at molecular weights (M.W.) of 40 Kd. The protein corresponding to the two major bands was purified by immuno-affinity chromatography and sequenced. The amino-terminal 19 residues of the lower band was identified as VLEVDPNIQAVXTQEXEQI, which is identical to that of the human cytokeratin 8 (residues 77 to 95), M.W. 52Kd. The amino-terminal sequence of the upper band was blocked and not determined. To examine the ability of KM195 for tumor imaging, 125I-labeled KM195 was injected i.v. into nude mice bearing SW1116 xenografts. Significantly higher radioactivity was observed in the tumor compared with major organs at days 3 and 5. These data indicate that KM195, which recognizes cytokeratin 8-like cytoplasmic antigen, could be a potential MoAb for use in the immunohistochemical diagnosis and radioimmunodetection of adenocarcinoma.

Adenocarcinoma↗

Immunotargeting of human small cell lung cancer xenografts in athymic mice using a monoclonal antibody (RNL-1) against a neuroendocrine-related antigen.

A mouse monoclonal antibody (RNL-1) was raised against the variant small cell lung cancer (SCLC) cell line NCI-H82. Immunohistochemical studies on frozen sections showed that the antibody was reactive with most SCLC (15 out of 16) and lung carcinoids (six out of seven), while in general adenocarcinomas and squamous cell carcinomas of the lung were negative. Immunocytochemical studies on 29 different cell lines derived from human lung tumours confirmed the neuroendocrine-related expression of the RNL-1 defined antigenic determinant. Immunoelectron microscopy showed that RNL-1 recognises an extracellular membrane domain, concentrated at adhesion sites between adjacent cells. The tissue distribution of the RNL-1 defined antigen was mainly restricted to neural and neuroendocrine tissues. These immunohistochemical data suggest that RNL-1 is directed against a neuroendocrine-related cell adhesion molecule. Being reactive with an epitope expressed on the surface of most neuroendocrine malignant cells, RNL-1 (IgG1 isotype) is a potential vehicle for targeting SCLC in vivo. We evaluated the ability of radiolabelled RNL-1 to localise human SCLC xenografts in nude mice as a first step in determining the in vivo value for radioimmunodetection. RNL-1 was radioiodinated using the Bolton-Hunter labelling technique. Nude mice bearing NCI-H82 xenografts were injected intravenously with the radiolabelled RNL-1 preparations, and animals were dissected 4, 24, 48, 72 and 120 h post injection (p.i.) to determine the biodistribution of the radiolabel. The iodine-125 label accumulated in the tumour up to 48 h p.i. (6.5% injected dose per gram of tissue [ID g-1]), while the label content of the normal tissues decreased with time.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenocarcinoma↗

[Localization of hepatocellular carcinoma with monoclonal antibodies].

We prepared monoclonal antibodies (MAbs) against hepatocellular carcinoma using cell suspensions isolated from surgical fresh hepatoma specimens as antigen. Totally we got 6 strains of hybridoma cell lines stably secreting MAbs for more than 2 years. Immunocytochemically they stained positively most of the paraffin embedded hepatoma tissues (63.1 to 91.1%) without reaction to the normal liver tissues. Localization of human hepatoma with 125I or 131I labelled MAbs in nude mice was done by IV injection, which showed clear tumor image by ECT radioimmunodetection and autoradiography of tissues. The T/N ratios of different MAbs were 3.1, 3.6, 5.15 and that of HAb 18-F (ab')2 was 14.4. Among 15 patients suspected to have hepatoma and given the labelled MAb, 13 proved pathologically to be hepatocellular carcinoma.

Animals↗

Carcinoembryonic antigen and alpha-fetoprotein expression and monoclonal antibody targeting in a human hepatoma/nude mouse model.

Hep G2, a human hepatocellular carcinoma, was grown s.c. in nude mice, as well as in tissue culture. This line retains the normal liver parenchymal cell capacity to synthesize human plasma proteins such as albumin, but there is no indication that it harbors the hepatitis B virus. We have detected the oncofetal antigens alpha-fetoprotein (AFP) and carcinoembryonic antigen (CEA) in both Hep G2 xenografts and spent tissue culture media by Ouchterlony double diffusion assays, enzyme-linked immunosorbent assay, and immunohistology. By enzyme-linked immunosorbent assay, the AFP levels were 544.9 ng/ml in the cell culture and 1.6 microgram/g in saline extracts of the xenograft. The CEA levels were 35.2 ng/ml in the cell culture and 5.4 micrograms/g in the xenograft. The biodistribution of a radioiodinated anti-AFP murine monoclonal antibody and an anti-CEA monoclonal antibody were studied separately in nude mice bearing s.c. Hep G2 xenografts in comparison to an isotype-matched irrelevant IgG (Ag8). Anti-CEA antibody showed a preferential localization for Hep G2, but anti-AFP antibody did not. Immunohistochemical studies of the Hep G2 tumor, using biotinylated anti-AFP and anti-CEA, indicate both cytoplasmic and luminal staining of CEA and AFP in the tumor. These results suggest that Hep G2 may be a useful cell line for radioimmunodetection and radioimmunotherapy studies using anti-CEA and possibly anti-AFP monoclonal antibodies.

Animals↗