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At least 865 records · Page 48Linked to original sources
PubMed1995

Pharmacokinetics of chimeric L6 conjugated to indium-111- and yttrium-90-DOTA-peptide in tumor-bearing mice.

UNLABELLED: A bifunctional chelating agent, DOTA-Gly3-L-(p-isothiocyanato)-phenylalanine amide (DOTA-peptide-NCS), was studied in nude mice bearing human breast cancer xenographs (HBT 3477) to determine its potential for radioimmunoconjugate therapy. METHODS: Indium-111 and yttrium-90 were attached to an anti-adenocarcinoma chimeric L6 (ChL6) monoclonal antibody (MAb) after pre-chelation to the DOTA-peptide-NCS and the desired neutral radiochelates were obtained by purification. The unique characteristic of the DOTA-peptide-NCS to form neutral complexes with trivalent metals was utilized to separate the resulting 111In and 90Y radiochelates from excess chelating agent and other anionic by-products resulting from metal impurities. The purified radiochelates were then conjugated to ChL6. The pharmacokinetics of 111In- and 90Y-DOTA-peptide-ChL6 were obtained for 5 days after injection in nude mice bearing HBT 3477 xenographs. The results were compared with the pharmacokinetics of 125I-ChL6 obtained in the same mouse model. RESULTS: The whole-body clearance of 125I-ChL6, 90Y- and 111In-DOTA-peptide-ChL6 was monoexponential with biologic half-times of 92, 104 and 160 hr, respectively. Blood clearances of the three radiopharmaceuticals were biphasic. The radiometal immunoconjugates had greater tumor uptake and slower clearances. CONCLUSION: Indium-111- and 90Y-DOTA-peptide-ChL6 can be produced at high specific activity with fewer than one chelate per MAb by using a pre-labeling method that permits radiochelate purification by charge selection. Studies in mouse xenografts indicate that tumor uptake is enhanced and a favorable therapeutic index is achieved using these agents.

Animals↗
PubMed1995

Identification of a monoclonal antibody, TV-1, directed against the basement membrane of tumor vessels, and its use to enhance the delivery of macromolecules to tumors after conjugation with interleukin 2.

mAbs reactive with epitopes expressed on tumor vessels were evaluated as universal delivery agents of peptides with vasoactive properties to enhance the uptake of macromolecules in tumors. Unlike other reported approaches to target tumor vessels, a mAb designated TV-1 targets a basement membrane antigen that is found in all tissues but that is accessible only in tumor vessels, making it an alternative vehicle for the delivery of biologically active peptides to tumors. A panel of 30 monoclonal and polyclonal antibodies was screened by immunohistochemistry on sections of human tumors, normal vascular endothelium, and connective tissues. Five antibodies were chosen for in vivo evaluation, including two antifibronectin antibodies (TV-1, HFN 7.1), one anti-basic fibroblast growth factor antibody (anti-BFGF), and two antibodies reactive with a mesenchymal cell antigen (TP-1, TP-3). Three nude mouse tumor models characterized by varying degrees of vascularization (low to high) were used. After chemical conjugation to interleukin 2 (IL-2), these antibodies were used to pretreat tumor-bearing nude mice 3 h before injection with a radiolabeled mAb directed to the transplanted tumors. Pretreatment with TV-1/IL-2 or HFN 7.1/IL-2 produced a 3-fold higher tumor uptake of radiolabel compared to control mice pretreated with mAb alone. The other three vasoactive immunoconjugates failed to show significant increases in these tumor models. When TV-1/IL-2 was compared with the specific vasoconjugate (Lym-1/IL-2) as a pretreatment in the Raji lymphoma model, which has low vascularization, TV-1/IL-2 yielded approximately 60% of the tumor uptake seen with Lym-1/IL-2. In comparison, pretreatment with TV-1/IL-2 in the LS174T colon carcinoma model, which has high vascularization, yielded approximately the same tumor uptake seen with the B72.3/IL-2 vasoconjugate, which directly targets the tumor cells. These studies demonstrate that a mAb directed against fibronectin in the endothelial subcellular matrix can be used to deliver vasoactive agents to tumors.

Animals↗
PubMed1994

Improving radioimmunotargeting of tumors: the impact of preloading unlabeled L6 monoclonal antibody on the biodistribution of 125I-L6 in rats.

In the radioimmunotherapy of malignancies the uptake of monoclonal antibodies (MoAb) is commonly low in tumors compared with normal tissue. Several methods have been suggested to increase the tumor-to-normal tissue (T/N) ratio. In this study we have investigated the biodistribution of different amounts of 125I-L6-biotin MoAb in combination with a preload of unlabeled L6 MoAb. Nude rats were injected with 50 micrograms or 250 micrograms of unlabeled L6 24 hours prior to the injection of 10 micrograms, 50 micrograms or 250 micrograms of 125I-L6, antipancarcinoma MoAb. Dissections were performed 24 hours after the injection of radiolabeled MoAb. The maximal enhancement of tumor uptake with simultaneously decreased uptake in normal tissues was with 250 micrograms of 125I-L6 preceded by a preload of 50 micrograms unlabeled L6. Mean T/N ratios were improved by a factor of 2.9 for bone marrow, 3.4 for liver, 3.7 for lungs and 2.3 for kidneys as compared with the corresponding controls. This study demonstrated that preinjection of optimal amounts of unlabeled L6 MoAb may increase the uptake of 125I-L6 by tumor and improve the T/N ratios. Based on present data, preloading with unlabeled MoAb should be considered in future clinical studies with immunoconjugates to improve the radioimmunotargeting of tumors. It is essential to titrate an appropriate amount of the preload, thus avoiding possible tumor antigen saturation of unlabeled MoAbs but simultaneously decreasing the uptake of subsequently injected radiolabeled MoAb in normal tissues.

Animals↗
PubMedDate not supplied

In vivo expression of P-glycoprotein in a human colon carcinoma xenograft is modulated by therapy with free and monoclonal antibody-conjugated vinca alkaloids.

Well established UCLA-P3 human lung tumor xenografts were significantly regressed by treatment with a monoclonal antibody-vinca immunoconjugate whereas no regressions were observed for the LS174T and SW948 human colon carcinoma xenografts by this therapy. Antibody and complementary DNA probes utilized for detection of the MDR1 gene product and mRNA levels, respectively, revealed that prior to drug treatment the lung tumor had virtually no detectable P-glycoprotein while both colon carcinomas displayed low and heterogeneous expression of this resistance-related protein. It was subsequently determined, however, that the low level of P-glyocoprotein expression observed for one of the colon tumors could be rapidly modulated following therapy with free or MoAb-conjugated vinca. These data indicated that elevated P-glycoprotein levels resulting from drug therapy may play a role in the lack of regression of the human colon xenografts. Most significantly, our results also indicated that the time interval between drug treatment and tissue sampling may be a critical factor to be considered in studies which attempt to correlate P-glycoprotein expression with chemotherapy.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1994

A phase I-II study of high-dose thiotepa, busulfan and cyclophosphamide as a preparative regimen for allogeneic marrow transplantation.

Thirty adults with hematologic malignancies at high-risk for relapse were treated on a phase I-II study of high-dose thiotepa, busulfan (BU) and cyclophosphamide (CY) as the preparative regimen for allogeneic marrow transplantation. Cyclosporine and methylprednisolone or anti-CD5 ricin A chain immunoconjugate were used as graft-versus-host disease prophylaxis. Filgrastim was given from day 1 to enhance engraftment. Median follow-up time is 16 months (range 9-29 months). Grades III-IV regimen-related toxicity occurred in 5 (26%) of 19 patients treated with thiotepa 250 mg/m2 x 3, BU 1 mg/kg x 12 and CY 60 mg/kg x 2 and this was considered the maximal tolerated dose-schedule. Stomatitis and hepatoxicity were dose-limiting. All patients engrafted and had complete donor chimerism. The actuarial rate of acute graft-versus-host disease was 71% (95% CI 62-80%). The relapse rate at 1 year was 38% (95% CI 25-50%) and the actuarial survival at 1 year was 30% (95% CI 22-38%). The combination of thiotepa, BU and CY is tolerable as a preparative regimen for allogeneic marrow transplantation.

Adolescent↗
PubMed1994

Radioimmunotherapy of nude mice bearing a human interleukin 2 receptor alpha-expressing lymphoma utilizing the alpha-emitting radionuclide-conjugated monoclonal antibody 212Bi-anti-Tac.

The efficacy, specificity, and toxicity of bismuth (212Bi) alpha particle-mediated radioimmunotherapy was evaluated in nude mice bearing a murine lymphoma transfected with the human CD25 [human Tac; interleukin 2 receptor alpha (IL-2R alpha)] gene. The therapeutic agent used was the tumor-specific humanized monoclonal antibody anti-Tac conjugated to 212Bi. The human IL-2R alpha-expressing cell line was produced by transfecting the gene encoding human Tac into the murine plasmacytoma cell line SP2/0. The resulting cell line, SP2/Tac, expressed approximately 18,000 human IL-2R alpha molecules/cell. Following s.c. or i.p. injection of 2 x 10(6) SP2/Tac cells into nude mice, rapidly growing tumors developed in all animals after a mean of 10 and 13 days, respectively. The bifunctional chelate cyclohexyldiethylenetriaminepentaacetic acid was used to couple 212Bi to the humanized anti-Tac monoclonal antibody. This immunoconjugate was shown to be stable in vivo. Specifically, in pharmacokinetic studies in nude mice, the blood clearance patterns of i.v. administered 205/206Bi-anti-Tac and coinjected 125I-anti-Tac were comparable. The toxicity and therapeutic efficacy of 212Bi-anti-Tac were evaluated in nude mouse ascites or solid tumor models wherein SP2/Tac cells were administered either i.p. or s.c., respectively. The i.p. administration of 212Bi-anti-Tac, 3 days following i.p. tumor inoculation, led to a dose-dependent, significant prolongation of tumor-free survival. Doses of 150 or 200 microCi prevented tumor occurrence in 75% (95% confidence interval, 41-93%) of the animals. In the second model, i.v. treatment with 212Bi-anti-Tac 3 days following s.c. tumor inoculation also resulted in a prolongation of the period before tumor development. However, prevention of tumor occurrence decreased to 30% (95% confidence interval, 11-60%). In both the i.p. and s.c. tumor trials, 212Bi-anti-Tac was significantly more effective for i.p. (P2 = 0.0128 50/100 microCi 212Bi-anti-Tac versus 50/100 microCi Mik beta; P2 = 0.0142 150/200 microCi anti-Tac versus 150/200 microCi Mik beta) and for s.c. tumors (P2 = 0.0018 100 microCi anti-Tac versus 100 microCi Mik beta; P2 = 0.0042 200 microCi anti-Tac versus 200 microCi Mik beta 1) than the control antibody Mik beta 1 coupled to 212Bi at comparable dose levels. In contrast to the efficacy observed in the adjuvant setting, therapy of large, established s.c. SP-2/Tac-expressing tumors with i.v. administered 212Bi-anti-Tac (at doses up to 200 microCi/animal) failed to induce tumor regression.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1994

[Progress in targeting therapy for hepatic cancer].

Targeting therapy for hepatic cancer is divided into a method using Lipiodol as drug carrier and a method employing immunological responses of monoclonal antibodies to the tumor antigens. For the latter method, immuno-conjugates of antibodies and cytotoxic agents have been studied. Because of the lower response rates of conventional chemotherapy. Lipiodol as drug carrier provides the most effective targeting therapy on hepatic cancer at the present time. Immunotherapy using cytotoxic cells, however, did not result in sufficient clinical efficacy on the liver cancer. The system for accumulation of the effective and sufficient number of cytotoxic cells or immunoconjugates in the targeting tumor tissues are expected to be investigated.

Antibodies, Monoclonal↗
PubMed1993

Kinetics and tissue distribution of the radiolabeled chimeric monoclonal antibody MOv18 IgG and F(ab')2 fragments in ovarian carcinoma patients.

Twenty-four patients suspected of having ovarian carcinoma received i.v. injection with a combination of radiolabeled intact IgG (1 mg) and F(ab')2 fragments (1 mg) of the chimeric monoclonal antibody MOv18, each form labeled with 1.85 MBq 131I or 125I. Laparotomy was performed either 2 or 6 days after injection, and the uptake of radioactivity was determined in a total of 329 biopsies of normal and malignant tissues. The mean elimination half life in plasma of cMOv18 IgG and F(ab')2 was 70 +/- 8 (SD) and 20 +/- 5 h, respectively. The mean uptake of IgG in tumor biopsies was 3.6-fold higher two days after injection and 6.9-fold higher than the uptake of F(ab')2 6 days after injection. Uptake in normal tissues was 3.3 and 5.5 times higher for IgG at 2 and 6 days, respectively. Two days after injection, the mean ratio of the uptake in tumor:normal tissue/patient was 3.8 +/- 1.5 and 4.0 +/- 1.8 for radiolabeled cMOv18 IgG and F(ab')2, respectively. Six days after injection, this was 6.7 +/- 4.7 for Ig G and 5.7 +/- 4.1 for F(ab')2. cMOv18 IgG has a longer circulation time in blood, a higher uptake in tumor and normal tissues, and a longer retention time compared to the F(ab')2 fragments. However, the tumor:normal tissue ratios are similar. The results do not warrant a definite conclusion as to which antibody form is most suitable for therapeutic application of antibodies but provide a more firm basis for rational design of therapeutic targeting studies using immunoconjugates.

Adult↗
PubMed1993

Labeling of monoclonal antibodies with rhenium-186 using the MAG3 chelate for radioimmunotherapy of cancer: a technical protocol.

A detailed technical protocol is provided for reproducible and aseptical production of stable 186Re-monoclonal antibody conjugates. Labeled Mab E48 IgG and its F(ab')2 fragment which are promising candidates for radioimmunotherapy of squamous cell carcinoma of the head and neck were used for evaluation. S-benzoylmercaptoacetyltriglycine (S-benzoyl-MAG3) was used as a precursor. Rhenium-186-MAG3 was prepared via a unique solid-phase synthesis, after which known strategies for esterification and conjugation to Mab IgG/F(ab')2 were applied. The biodistribution of 186Re-E48 F(ab')2 in tumor-bearing nude mice was found to be comparable to that of analogously labeled 99mTc-E48 F(ab')2 or 131I-E48 F(ab')2, indicating that the intrinsic behavior of the antibody remains preserved when using this labeling technique. Radiolytic decomposition of 186Re-E48 IgG/F(ab')2 solutions of 10 mCi.ml-1 was effectively reduced by the antioxidant ascorbic acid. Upon increase of the Re-MAG3 molar amount, a conjugation of seven to eight Re-MAG3 molecules per Mab molecule was generally the maximum ratio that could chemically be obtained. Such a ratio did not impair the immunoreactivity or alter the in vivo biodistribution characteristics of the immunoconjugate, making this labeling procedure suitable for general clinical application.

Animals↗
PubMedDate not supplied

Immunocytochemical study on internalization of anti-carbohydrate monoclonal antibodies.

The fate of anti-tumor monoclonal antibodies (mAbs) after binding to the cell surface is one of the important factors for application of mAbs in therapy. For mAbs to remain on the cell surface for a long time is preferable character for complement-dependent cytotoxicity (CDC) and antibody-dependent cellular cytotoxicity (ADCC). On the other hand, quick internalization of mAbs into cytoplasm is advantageous for cytotoxic effects of toxins or cytotoxic drugs conjugated with mAbs. In this study we investigated the localization of anti-carbohydrate mAbs in vitro by immunocytochemical methods at the electron microscopic level. Anti-ganglioside GM3 mAb (mouse IgM) was localized both in cytoplasmic vesicles and on the cell surface membrane of mouse melanoma cells after incubation for 30 min at 37 degrees C. Anti-ganglioside GM2 mAb (mouse IgM), anti-ganglioside GD2 mAb (mouse IgG3) anti-ganglioside GD3 mAb (mouse IgG3) mainly existed on the cell surface of human small cell lung carcinoma cells, human neuroblastoma cells and human melanoma cells, respectively, after incubation for 30 min at 37 degrees C. On the other hand, anti-sialyl Lea mAb (mouse IgG1) was intensively incorporated into the cytoplasm of human colon tumor cells under the same conditions. Anti-ganglioside GD3 mAb and anti-sialyl Lea mAb were radiolabelled with 125Iodine and traced in in vitro culture. When the cells were incubated in the presence of the 125I-mAb for 90 min on ice, the ratio of intracellular counts to surface counts was 8/92 for anti-ganglioside GD3 mAb and 31/69 for anti-sialyl Lea mAb respectively. After the subsequent incubation for 60 min at 37 degrees C, the ratio altered to 13/87 for anti-ganglioside GD3 mAb and 54/46 for anti-sialyl Lea antigen mAb. This study suggested that internalization of anti-carbohydrate mAbs after the binding to the cell surface was different among the mAbs depending on the character of antigens. In conclusion, anti-ganglioside mAbs have beneficial characters for CDC or ADCC while anti-sialyl Lea mAb is suitable for immunoconjugates.

Animals↗
PubMed1993

[Targeting therapy using monoclonal antibody directed against growth factor receptors].

Targeting therapy is expected to be a new effective anti-cancer treatment in near future. Major advances are achieved by considerable effort in this area. Monoclonal antibodies that recognize tumour-associated antigens were conjugated to chemotherapeutic drugs, toxins and radionuclides with various procedures. To apply this new therapy for clinical use, many problems still remain to be clarified. These problems consist of human anti-mouse antibody, antigenic heterogeneity and low tumour uptake. By our experiment, growth factor receptor was an ideal target for targeting therapy and immunoconjugate directed against growth factor receptor showed selective cytotoxicity to cancer cells with expression of growth factor receptor. Moreover, cytotoxic effect was positively correlated with expression level of growth factor receptor.

Animals↗
PubMed1993

A phase I trial of a rhenium 186-labeled monoclonal antibody administered intraperitoneally in ovarian carcinoma: toxicity and clinical response.

OBJECTIVES: To determine the maximum tolerated dose, spectrum of toxicity, and response of persistent and recurrent ovarian carcinoma to intraperitoneal injection of a conjugate of rhenium 186 (186Re) and a monoclonal antibody; to measure the radiation distribution to normal structures; and to establish the fate of the infused isotope. METHODS: Rhenium 186 was conjugated to murine monoclonal antibody NR-LU-10, which binds to a cell surface antigen present on ovarian carcinoma. In a dose-escalating phase I trial, a single dose of 25 mg/m2 of antibody complexed with 25-150 mCi/m2 of 186Re was administered intraperitoneally to 17 women with ovarian carcinoma that was recurrent or persistent after platinum-based chemotherapy. RESULTS: Severe myelosuppression was observed at 150 mCi/m2 of 186Re in two evaluable patients. Other clinically significant toxicities included low-grade fever and transient skin rash. Hepatic enzyme elevation was seen in 12 of 17 patients, but was not clinically significant. No chronic enteric toxicity was observed. Decreased tumor size was demonstrated by repeat operation in four of seven patients with disease measuring less than 1 cm at the time of treatment (four of 17 total). All four responders had serum CA 125 levels of 35 U/mL or less at the time of treatment and had received only one regimen of chemotherapy. CONCLUSION: This immunoconjugate can be administered intraperitoneally with acceptable toxicity and produces objective responses after a single dose in patients with minimal objective disease.

Adult↗
PubMed1993

From monoclonal antibodies to peptides and molecular recognition units: an overview.

Various antigen-specific monoclonal antibodies (Mabs) are now being used clinically. Applications include in vitro testing (radioimmunoassay) and in vivo imaging (radioimmunoscintigraphy) for the early detection and staging of disease. Mabs can also be used as vehicles for delivering therapy (radioimmunotherapy) or to assess effects of therapeutic interventions. This review delineates those components making up antibody structure and discusses their functional significance. The method for radiolabeling immunoconjugates without altering their immunoreactivity or biological properties is dependent on an understanding of the structural units of the antibody and the labeling technique used. With the advent of genetic engineering, it has become feasible to design antibodies to circumvent certain adverse features or enhance a certain property. A review of the various "designer" antibodies and their relative advantages in the clinical setting is presented.

Antibodies, Monoclonal↗
PubMed1995

Gold, electron microscopy, and cancer therapy.

Radioactive gold has properties suitable for radiotherapy and can provide lethal irradiation to cells. If the gold is conjugated to a targeting molecule, such as an antibody, it may be possible to specifically deliver the dose to tumor cells. Various gold particles are possible candidates and include gold colloids with adsorption of antibodies or gold clusters with covalent attachment. Different sizes of gold particles are available and some may be preferred for certain situations. Problems with intravenous injection and in vivo delivery are numerous, and a more tractable application is the direct instillation into the urinary bladder of radiogold immunoconjugates to treat superficial bladder carcinoma. Preliminary studies indicate the feasibility of this approach.

Animals↗
PubMed1996

[Diagnosis and targeting therapy of colorectal cancer using antibody].

Application of monoclonal antibody for diagnosis and therapy of colorectal cancer was reviewed. The history and present status of radioimmunoimaging of cancer were presented. Immuno-guided surgery using radiolabeled antibody and hand-aided detector during surgery is a promising approach for complete excision of cancerous region. Also, a new antibody labeling method using a micro-magnet instead of radioisotopes may lead to a new era in immunodiagnosis of cancer. Finally, immunotargeting chemotherapy using antibody-anticancer drug conjugates was reviewed. A new type of immunoconjugate composed of human/mouse chimeric antibody and Neocarzinostatin seems to be one of the most promising drug formulas for immunotargeting chemotherapy.

Antibiotics, Antineoplastic↗
PubMed1996

Synthesis of different immunotoxins composed by ribosome inactivating proteins non-covalently bound to monoclonal antibody.

This study describes the synthesis of a panel of immunotoxins made by a non-covalent interaction between a monoclonal antibody derivatized with a dichlorotriazinic dye and six different ribosomal inhibitor proteins: colocin 1, momorcochin, momordin, bryodin, saporin 6 and PAP-S. The scheme of preparation showed several advantages respect to commercially available heterobifunctional cross-linkers, such as an higher overall yield of production and the homogeneity of the obtained conjugates. Nevertheless this procedure allowed the synthesis of immunoconjugates only for the four glycosilated RIPs since the not glycosilated ones saporin 6 and PAP-S precipitated in the presence of the dye. The non covalent linkage did not significantly affect the toxic activity of the glycosilated RIPs, as shown by their antitumoral activity on three different cell lines: HT-29 and A431 as target and MeWo as control. Furthermore, the monoclonal antibody cell-antigen recognition was preserved if a maximum derivatization ratio of 4 between the antibody and the dye was applied. The described original procedure may be of general application to prepare panels of immunotoxin for clinical use avoiding the expected RIP-related immune reaction.

Antibodies, Monoclonal↗
PubMed1996

Genetic engineering of immunotoxins.

Immunotoxins, composed of both targeting mechanisms and toxins, hold great promise for the treatment of some cancers and other pathological conditions. Research and manufacture of these drugs use various techniques of molecular biology, some of which are described in this article. A considerable amount of research has focused on ricin, a plant toxin, and its immunoconjugates. Areas currently under evaluation by our laboratory include structure-function studies based on mutational analysis, enhancement of intracellular trafficking, genetic fusion of the targeting and toxic moieties, and the expression of toxin in plant cell culture.

Biomedical Engineering↗
PubMed1996

Long-term survival in advanced chronic myelogenous leukemia following bone marrow transplantation from haploidentical related donors.

From 1987 to 1991, 26 patients with CML and a median age of 31 years received allogeneic BMT from a partially mismatched related donor (PMRD) who shared at least one haplotype with the recipient. Nine patients were in accelerated phase (AP), and 11 patients were in blast crisis (BC) at the time of BMT. Patients were mismatched either in graft-versus-host or host-versus-graft directions for one antigen in 3 patients, two antigens in 14 patients, and three antigens in 9 patients. All patients were prepared with a regimen consisting of total body irradiation, etoposide, cytosine arabinoside, cyclophosphamide and methylprednisolone. All marrows were treated ex vivo with T10B91.A-31, a monoclonal antibody directed toward the alpha beta heterodimer of the CD3 receptor, and rabbit complement. Additional GVHD prophylaxis included either the anti-CD5 immunoconjugate XomaZyme-H65, cyclosporine, or both in combination with methylprednisolone. Eight patients did not have sustained engraftment. The 100-day survival was 42%. The incidence of > or = grade II acute GVHD was 29%. The incidence of chronic GVHD was 50% and was limited in all cases. The median survival at 4 years for all 26 patients was 27%. Seven patients (CP 1, AP 3, BC 3) remain in hematologic remission 1297-2241+ days after transplantation. AlloBMT from a PMRD may be considered for patients with advanced CML who lack a matched sibling or unrelated donor.

Adolescent↗