Vitiligo is a disease in which melanocytes are selectively destroyed. The disease is thought to be an autoimmune process being there are antibodies to pigment cells in the sera of patients and animals with vitiligo. In the present study, sera from vitiligo patients were examined for reactivity with the human melanoma cell line, SK-Mel-28, by Western blot analysis of solubilized membrane antigens of these cells to identify the pigment cell antigens defined by antibodies in the patients with vitiligo. Antibody reactivity to human melanoma cells (SK-Mel-28) was investigated in 14 patients with vitiligo, and 16 with normal control individuals. Antibodies to the 116-113, 60, 40 KD antigens were associated with vitiligo being present in 79%, 86%, and 43% respectively of the patients with vitiligo, but in only 6%, 38% and 6% of the normal controls. In contrast, antibodies to the 160-155, 78 and 64 KD antigens were equally common in vitiligo and in normal individuals. The results suggest that autoreactivity to pigment cells occurs more commonly in patients with vitiligo than in the normal control and high autoreactivity to pigment cells in the vitiligo sera might be an impertinent epiphemenon to destroyed pigment cell.
Antibodies, Neoplasm/*blood ; Antigens, Neoplasm/immunology ; Autoantibodies/blood ; Blotting, Western ; Human ; Melanoma/*immunology ; Vitiligo/*immunology

Angiopoietin2( ANGPT2 ) plays an important role in tumor angiopoiesis. ANGPT2 antagonises ANGPT1 resulting in an effect on the stability of blood vessels, which promotes tumor growth, invasion, proliferation as well as relating to tumor vascular density. A lot of researches published papers about anti-ANGPT2 for the treatment of tumor, and have made some progresses. In this review, the role of ANGPT2 in the pathogenesis of acute myelogenous leukemia (AML), including its effects on proliferation of leukemia cells, bone marrow angiopoiesis, tumor invasion and metastasis are briefly summarised in order to provide the basis for targeted ANGPT2 in treatment of AML.
Angiopoietin-1 ; immunology ; Antibodies ; immunology ; Bone Marrow ; Humans ; Leukemia, Myeloid, Acute ; immunology ; Neoplasm Invasiveness ; Neoplasm Metastasis

OBJECTIVETo evaluate the in vitro and in vivo function of anti-human bladder tumor human-mouse chimeric antibody ch-BDI and its future clinical application.

METHODSWith ch-BDI in high-expression cell-line medium, affinity chromatography was used for the purification. Labeled with (99m)Tc through reduction method, its immunoreactive fraction and association constant were measured. The constant was injected into nude mice with xenografted human bladder tumor. The biodistribution of the labeled ch-BDI was studied with radioimmunoimaging.

RESULTSch-BDI showed desirable immunoreactive fraction (76%) and association constant (3.56 x 10(9) M(-1)) in vitro and a terrific specific targeting effect in vivo.

CONCLUSIONch-BDI has fairly good function against human bladder tumor both in vitro and in vivo, and is promising in clinical use.

Animals ; Antibodies, Monoclonal ; immunology ; Antibodies, Neoplasm ; immunology ; Antibody Affinity ; Humans ; In Vitro Techniques ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Recombinant Fusion Proteins ; immunology ; Urinary Bladder Neoplasms ; immunology

A mouse-anti-human monoclonal antibody was produced by using the membrane proteins of human lung carcinoma cell line A549 as the immunogen to generate monoclonal antibodies against lung carcinoma with the use of hybridoma techniques. McAb4E7 was prepared successfully. To identify its antigen, proteomic technologies such as two-dimenstional electrophoresis, western blotting and mass spectrometry were employed. The targeting antigen of McAb4E7 expressed positive in human lung cancer cell lines A549 and human hepatocarcinoma cell line HepG2, moreover, the expression of the antigen was stronger in A549 cells. Finally, we obtained one positive protein in A549 cell line that has strong affinity and specificity for McAb4E7, which was identified to be ATP synthase beta subunit. We identified ATP synthase beta subunit as the targeting antigen of lung carcinoma special monoclonal antibody McAb4E7.
Animals ; Antibodies, Monoclonal ; biosynthesis ; chemistry ; immunology ; Antibodies, Neoplasm ; immunology ; Antibody Specificity ; Antigens, Neoplasm ; genetics ; immunology ; Cell Line, Tumor ; Humans ; Lung Neoplasms ; immunology ; Membrane Proteins ; immunology ; Mice ; Mice, Inbred BALB C ; Mitochondrial Proton-Translocating ATPases ; immunology

The use of monoclonal antibodies (mAbs) for cancer therapy has achieved considerable success in recent years. Approximate 17 monoclonal antibodies have been approved as cancer therapeutics since 1997. Antibody-drug conjugates (ADC) are powerful new treatment options for cancer, and naked antibodies have recently achieved remarkable success. The safety and effectiveness of therapeutic mAbs in oncology vary depending on the nature of the target antigen and the mechanisms of tumor cell killing. This review provides a summary of the current state of antibody-based cancer therapy, including the mechanisms of tumor cell killing by antibodies, tumor antigens as antibody targets, clinical effectiveness of antibodies in cancer patients and nanoparticles-based ADCs.
Antibodies, Monoclonal ; immunology ; therapeutic use ; Antigens, Neoplasm ; immunology ; Antineoplastic Agents ; therapeutic use ; Humans ; Immunoconjugates ; therapeutic use ; Nanoparticles ; Neoplasms ; immunology ; therapy

OBJECTIVESTo obtain a single-chain antibody with high affinity against hepatocellular carcinoma (HCC).

METHODSA second single-chain antibody mutant library was established using an error-prone PCR and a phage display. Single-chain antibodies with high affinity for hepatocellular carcinoma were selected using ELISA.

RESULTSThe content of the second single-chain antibody mutant library was about 4.5 x 10(7). Two selected mutants, M90 and M116, were obtained after 3 rounds of panning and ELISA. Immunoassay showed that both M90 and M116 could bind to human HCC cells. The relative affinity of M90 was 1.7-fold higher than that of the original antibody, and M116 was 2-fold higher than that of the original antibody.

CONCLUSIONError-prone PCR is an effective and simple method for affinity maturation of antibodies isolated from a phage antibody library.

Antibodies, Neoplasm ; immunology ; Antibody Affinity ; Antibody Specificity ; Carcinoma, Hepatocellular ; immunology ; pathology ; Humans ; Immunoglobulin Fragments ; immunology ; Immunoglobulin Variable Region ; genetics ; immunology ; Liver Neoplasms ; immunology ; pathology ; Mutation ; Peptide Library

OBJECTIVETo construct a human phage antibody library and screen the single chain variable fragment (ScFv) antibudies to peroxiredoxin I (Prx I) of lung adenocarcinoma.

METHODSThe total RNA was isolated from the lymph nodes of lung cancer patients to amplify V(H) and V(L) genes by RT-PCR. V(H) and V(L) were linked with a DNA linker by SOE-PCR to construct the single chain variable fragment gene. The ScFvs were coloned into the phage vector pCANTAB5E. The insert ratio of the ScFv antibody library was identified by PCR, and the products were digested by SfiI/NotI and analyzed with 1% agarose gel electrophoresis. Three rounds of panning against lung adenocarcinoma cell line A549 and Prx I were performed, and the positive clones were identified for soluble expression. The soluble antibodies were identified by SDS-PAGE and Western blotting, and ELISA and immunocytochemistry were used to characterize the activity of the antibodies.

RESULTSA recombination phage antibody library was constructed. The insert ratio of ScFv gene was 77% (23/30), and enzyme digestion identified the target product. The sixth phage harvest resulted in a yield 180 folds of that of the first one. Positive reactions to A549 cells were detected in 6 of 10 random clones, with a positivity rate of 60%. The soluble human ScFvs against Prx I of lung adenocarcinoma were expressed in E. coli HB2151 and confirmed by SDS-PAGE and Western blotting. ELISA and immunocytochemistry demonstrated a relative specific affinity of the soluble antibodies to A549 cells.

CONCLUSIONScFv antibodies against lung adenocarcinoma have been acquired by phage display antibody library technique, and the soluble antibodies have a relative avidity specific to human lung adenocarcinoma A549 cells overexpressing PrxI.

Adenocarcinoma ; immunology ; pathology ; Antibodies, Neoplasm ; biosynthesis ; genetics ; immunology ; Antibody Specificity ; Cell Line, Tumor ; Humans ; Immunoglobulin Variable Region ; immunology ; Lung Neoplasms ; immunology ; pathology ; Peptide Library ; Peroxiredoxins ; immunology ; Single-Chain Antibodies ; biosynthesis ; genetics ; immunology

Antibodies, Monoclonal ; pharmacology ; therapeutic use ; Antibodies, Neoplasm ; immunology ; therapeutic use ; Antibody Affinity ; Antibody Specificity ; Antigen-Antibody Reactions ; Antigens, Neoplasm ; analysis ; immunology ; Carcinoma, Hepatocellular ; immunology ; therapy ; Humans ; Liver Neoplasms ; immunology ; therapy

OBJECTIVETo identify cancer-derived immunoglobulin G (IgG) whole molecule-interacting proteins to provide important clues for studying IgG biological functions.

METHOSHeLa cell lysate was immunoprecipitated with rabbit antihuman IgG whole molecule antibody and normal rabbit IgG. The immunocomplex underwent sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and was detected with silver staining. Three prominently enhanced bands were subjected to protein identification with liquid chromatography-tandem mass spectrometry (LC-MS/MS), and the MS data were analyzed with Swiss-Prot database. Cancer-derived IgG whole molecule-interacting proteins were screened and functionally annotated.

RESULTS AND CONCLUSIONWe identified 6 potential cancer-derived IgG whole molecule-interacting proteins with co-immunoprecipitation combined with LC-MS/MS, which provides valuable clues for studying the function of cancer-derived IgG.

Antibodies, Neoplasm ; immunology ; Chromatography, Liquid ; Electrophoresis, Polyacrylamide Gel ; HeLa Cells ; Humans ; Immunoglobulin G ; immunology ; Neoplasms ; immunology ; Proteins ; immunology ; Tandem Mass Spectrometry

OBJECTIVETo investigate the correlation between BRAF V600E mutation and anti-epidermal growth factor receptor (EGFR) monoclonal antibodies (MoAbs) therapeutic effects in metastatic colorectal cancer.

METHODSStudies were included into meta-analysis to investigate the association between BRAF V600E mutation and clinical outcome in metastatic colorectal cancer patients treated with anti-EGFR MoAbs.

RESULTSA total of 7 studies were included in this meta-analysis. The 7 studies included 1352 patients in total, sample sizes ranged from 67 to 493. Objective response rate (ORR), progression-free survival (PFS) and overall survival (OS) were collected from included studies and were used to assess the strength of the relation. In patients with wild-type KRAS, the pooled odds ratio for ORR of mutant BRAF over wild-type BRAF was 0.27 (95% CI=0.10-0.70). BRAF mutation predicted a deterioration in PFS and OS in wild-type KRAS patients treated with anti-EGFR MoAbs (hazard ratio=2.78, 95% CI=1.62-4.76; hazard ratio=2.54, 95% CI=1.93-3.32).

CONCLUSIONBRAF V600E mutation is related to lack of response and worse survival in wild-type KRAS metastatic colorectal cancer patients treated with anti-EGFR MoAbs.

Antibodies, Monoclonal ; immunology ; Colorectal Neoplasms ; immunology ; pathology ; Humans ; Mutation ; Neoplasm Metastasis ; immunology ; Proto-Oncogene Proteins B-raf ; genetics ; Receptor, Epidermal Growth Factor ; immunology