Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0005684 (bladder cancer)
 16,431 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Superficial bladder cancer represents a promising target for intravesical, antibody-guided therapy. The construction of an optimum antibody-cytotoxic drug conjugate depends mostly on the appropriate selection of a monoclonal antibody (mAb). We have used immunogold labeling and SEM to specifically map the distribution of antigens expressed on three bladder cancer cell lines and on the luminal surface of biopsies from human transitional cell carcinoma of various grades and from normal bladder mucosa. The 48-127 mAb, which recognizes a M(r) 54,000 surface glycoprotein (gp54), was found to be very promising as a potential drug carrier. This antibody reacts with the surface of cells from low- and high-grade tumors; it does not react with the normal urothelium. Labeling of normal bladder mucosa was observed, however, on microvillous intermediate urothelial cells occasionally exposed by small areas of desquamation. The 48-127 mAb could target drugs to all areas of transformed urothelium while avoiding drug delivery to the normal, undesquamated bladder mucosa. Kinetics of gp54/48-127/gold complexes were tested in vitro with T24 and RT4 human bladder carcinoma cell lines incubated in the presence of the 48-127 mAb directly conjugated with 17.7-nm gold particles. Internalization of the gp54/48-127/gold complex was readily demonstrated by transmission electron microscopy. These results suggest that the 48-127 mAb represents a valuable drug carrier for intravesical therapy, allowing specific tumor targeting and internalization of various cytotoxic agents.
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PMID:Antibody drug carrier for immunotherapy of superficial bladder cancer: ultrastructural studies. 159 26

Over the past several years, many tumor markers, including cell surface antigens, T-antigen, ras p55, and ras p52 proteins, have been studied as potential tumor markers of bladder cancer. The lack of specificity and inconsistency of these markers led us to develop a new method for studying the urinary excretion of autocrine motility factor (uAMF) and tumor cell collagenase stimulating factor (TCSF) in 24-hour and first morning voided specimens. AMF is a glycoprotein secreted by the malignant cells and is responsible for cell locomotion, a key event in invasion and metastases of the malignant cells. TCSF is a membrane bound glycoprotein of tumor cells that stimulates fibroblast collagenase production. We have utilized an enzyme-linked immunoabsorption assay to detect the levels of uAMF and TCSF in urine samples collected from normal volunteers, patients with benign diseases, and patients with bladder cancer. Our data indicate that urinary concentrations of uAMF and TCSF are elevated in patients with bladder cancer. Furthermore, the levels of uAMF and TCSF are more elevated in invasive tumors as compared with benign counterparts. We have localized uAMF and TCSF in bladder cancer cells, utilizing immunohistologic techniques.
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PMID:A new method for evaluation of urinary autocrine motility factor and tumor cell collagenase stimulating factor as markers for urinary tract cancers. 212 27

We surveyed the tumor-related proteins present in the urine specimens of 118 bladder cancer patients to seek a possible marker enabling future diagnosis and prognosis of this disease. We identified a protein of 180 kDa. by sodium dodecyl sulfate polyacrylamide gel electrophoresis in urine samples subjected to prior adsorption by protein-A conjugated to a sepharose bead. This protein appears to be a glycoprotein because it binds to concanavalin A-conjugated sepharose and can be eluted by alpha-methyl D-mannoside. It does not react immunochemically with antibodies prepared against either carcinoembryonic antigen or epidermal growth factor receptor, both of which have an apparent molecular weight close to 180 kDa. We found this protein in the urine of 74.3% of the patients with transitional cell carcinoma. It was not present in age-matched controls, patients with benign prostatic hyperplasia or patients with 10 other cancers. There was 1 false positive result in a patient with prostate cancer. It does not appear to be associated with urinary tract infection, blood contamination, premedication or anesthesia.
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PMID:A new 180 kDa. urine protein marker associated with bladder cancer. 235 80

Fibronectin is a glycoprotein that mediates the attachment of BCG to the murine bladder. To assess the potential role of fibronectin on bladder cancer cells as a specific substrate for BCG binding in man, a semi-quantitative method was employed to evaluate the presence of fibronectin on normal urothelium and bladder cancer. Monoclonal anti-fibronectin binding to normal and malignant urothelial tissues was evaluated by an immunoperoxidase assay. Human tumor cell lines were evaluated with mixed hemadsorption and immunoperoxidase assays. In both systems, immunoreactive fibronectin had low expression on unfixed normal and malignant urothelium. With fixation, immunoreactive fibronectin decreased on supporting stroma and increased in normal and malignant urothelium. Fibronectin distribution did not show tumor specificity either with fixed or unfixed specimens.
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PMID:Fibronectin distribution in normal and malignant urothelium. 240 93

The mouse monoclonal antibody (MoAb) B3 raised against a rat bladder cancer cell line and the MoAbs HBJ127 and HBJ98 raised against a human bladder cancer cell line recognize homologous antigens predominantly present on proliferating cells of the corresponding species. Examination of MoAb-defined antigen and epitopes revealed that both HBJ127 and HBJ98 MoAbs defined a human cell surface glycoprotein complex having an apparent molecular weight of 125,000-130,000 which was composed of a heavy subunit of a glycoprotein nature (Mr 90,000-95,000) and a disulfide-linked light subunit of protein nature (Mr 30,000-35,000), but the HBJ127 and HBJ98 MoAbs recognized a protein epitope and a sugar epitope on the heavy subunit, respectively. Likewise, the B3 MoAb recognized a protein epitope on the heavy subunit of a rat cellular glycoprotein complex of similar composition to the HBJ127/HBJ98-defined human antigen. Addition of the B3 MoAb to rat and the HBJ127 or HBJ98 MoAb to human tumor cells inhibited the nucleic acid synthesis or the proliferation of the tumor cells in vitro in a dose-dependent manner. The target tumor cells exposed to MoAb could regrow when they were freed from the antibody, indicating that the effect of these MoAbs on the tumor cells is cytostatic and reversible. These MoAbs did not cause down-regulation of the cell surface antigen and did not arrest the cell cycle in a certain phase. These observations indicate that the Mr 125,000 glycoprotein cell surface component detected in both rat and human systems may play a requisite role for cell proliferation and that our MoAbs could inhibit the function by binding to the functionally proximal region of the component.
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PMID:Inhibition of tumor cell growth in vitro by murine monoclonal antibodies that recognize a proliferation-associated cell surface antigen system in rats and humans. 241 4

Two mouse monoclonal antibodies (MoAbs), KM-93 raised against human lung adenocarcinoma and KM-231 raised against human gastric cancer, were useful in serum diagnosis of several human cancer. KM-93 and KM-231 recognize sialyl Lex epitope and sialyl Lea epitope, respectively, expressed on glycoprotein and glycolipid. We established a new "cocktail" sandwich enzyme-linked immunosorbent assay system using the two MoAbs and the advantage of this assay system, which can simultaneously detect sialyl Lex and sialyl Lea antigens, is assessed in the present study. The new assay system is composed of a mixture of KM-93 and KM-231 as 1st antibodies and a mixture of biotinylated two MoAbs as 2nd antibodies. We evaluated the concentration of MoAbs and optimized it to gain high cancer-positivity. This assay system covered sialyl Lex positive and/or sialyl Lea-positive sera and gave a high rate of positive results in lung adenocarcinoma (62.3%), gastric cancer (32.5%), colon cancer (37.5%), pancreatic cancer (83.3%), bile duct and gall bladder cancer (66.7%) and hepatoma (76.9%), whereas positive results in healthy adults remained low. Positive results in benign diseases of lung (12.5%), pancreas (10.8%), gall bladder and bile duct (9.1%) were very low, but were higher in liver cirrhosis (33.3%), hepatitis and liver injury (34.8%). Simultaneous detection of two carbohydrate antigens, sialyl Lex and sialyl Lea was clearly superior to single detection.
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PMID:Advantage of cocktail-use of two anti-tumor monoclonal antibodies, KM-93 and KM-231, in serum diagnosis of cancer. 247 31

Rates of [3H]glucosamine and mannose incorporation into glycoproteins and dolichol-linked oligosaccharides in exponentially growing T-24 bladder cancer cells were examined after exposure to homoharringtonine (HHT). Two-h treatment of HHT (10 ng/ml) reduced [3H]glucosamine and mannose incorporation into the glycoproteins to 61% and 32% of controls. Concomitantly, respective sugar incorporation into dolichol-linked oligosaccharides was elevated 29% and 30% above control. The maximal inhibition of glycoprotein biosynthesis and stimulation of the lipid-linked oligosaccharides occurred within 2 to 4 h after exposure to 50 ng/ml of the drug. Prolonged drug exposure (greater than 8 h) resulted in generalized suppression of glycoprotein biosynthesis and lipid-linked oligosaccharide formation. The kinetic study indicated that the time course on reduction of glycoprotein biosynthesis and accumulation of dolichol-linked oligosaccharides paralleled the decline in protein synthesis. Further, the inhibition of glycoprotein synthesis and stimulation of dolichol-linked oligosaccharides were reversible 4 h after drug withdrawal. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis autoradiographic analysis of the [3H]mannose-labeled glycoprotein revealed no pronounced difference between HHT-treated and control cells. These data suggest that the inhibition of glycosylation results from combined decrease of acceptors for glycoprotein biosynthesis with a simultaneous accumulation of the dolichol-linked oligosaccharides. Collectively these data may account for many of the HHT-induced bioresponses.
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PMID:Effects of homoharringtonine on protein glycosylation in human bladder carcinoma cell T-24. 290 54

A cell surface antigen expressed in association with cell proliferation was detected and identified as a glycoprotein of molecular weight of 125,000 (gp 125) by using monoclonal antibodies against human or rat bladder cancer cells. We have found that appearance of the antigen in stimulated lymphocytes precedes the emergence of interleukin 2 receptor and that it is regulated by Ca ion and protein kinase-C.
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PMID:[Properties of glycoprotein 125, a proliferation-associated cell surface antigen]. 360 41

A tumor-associated antigen was preliminarily identified in urine from bilharzial (squamous-cell carcinoma) bladder cancer patients. Monospecific rabbit antisera were made by immunization with concentrated bladder cancer urine and exhaustive absorption with insoluble normal human serum and urine. The urine tumor-associated antigen was identical to an antigen from 3M KCl bladder tumor extract by immunodiffusion. The antigen in urine was found in nine of 10 bladder cancer patients and was absent from normal urine and serum by immunodiffusion and immunoelectrophoresis. The antigen was a concanavalin-A-binding glycoprotein which was anodal on immunoelectrophoresis. It was stable up to 2 years at -20 degrees C and did not cross-react with carcinoembryonic antigen or with Schistosoma haematobium antigens.
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PMID:Preliminary identification of a tumor-associated glycoprotein in bilharzial bladder cancer urine. 641 32

Previous work in our laboratory has demonstrated that antisera to proteins found in the urine of bladder cancer patients can distinguish between urine samples from these patients and those from normal individuals when tested by a complement-fixation assay. Antisera which were reactive with individual tumor-associated antigens were used to detect the antigens in the urine of bladder cancer patients and control individuals. One antigen was found in 66% of the bladder cancer patients (n = 38) and 25% of control individuals (n = 20). This antigen is a glycoprotein with a molecular weight of about 200,000 and beta-electrophoretic mobility and is distinct from carcinoembryonic antigen. A second molecule detected by an antiserum to urine fractions proved to be completely identical to serum C-reactive protein. C-Reactive protein was found in the urine of 72% of the bladder cancer patients (n = 39) and 32% of the control population (n = 32). Although a third protein detected with these antisera proved to be a normal urinary component, two of these tumor-related proteins appear to have potential as diagnostic markers for bladder cancer.
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PMID:Tumor-associated antigens in the urine of patients with bladder cancer. 708 80


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