UMLS:C0024623 - FACTA Search

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Query: UMLS:C0024623 (gastric cancer)
36,219 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Triptolide (Tri) is a diterpenoid triepoxide isolated from Tripterygium wilfordii Hook F. The effects of Tri on the colony formation of breast cancer cell lines MCF-7 and BT-20, stomach cancer cell lines MKN-45, MKN-7, and KATO-III, and promyelocytic leukemia cell line HL-60 were reported. Using Hamburger-Salmon's double layer agar technique with certain modifications, cancer cells were cultured in 0.3% agar in a highly humidified atmosphere of 5% CO2 at 37 degrees C for 14-21 d. Colonies were counted on d 14 (occasionally d 21) with the colony analyzer system CA-7A. Of the 5 solid tumor cell lines tested, 4 showed diminished colony formation in soft agar by greater than 70% of control value in Tri 10(-8) mol.L-1 (continuous exposure). The magnitudes of the inhibitory effect of Tri on most breast and stomach cancer cell lines were similar to that on the leukemia cell line HL-60. IC50 were 0.504-1.22 micrograms.L-1. The clinically achievable peak plasma concentration (PPC) of Tri was estimated as 0.15 mg.L-1, being 72-126 times higher than the IC70 of the cancer cell lines except KATO-III. The results suggest that Tri might have a potential therapeutic effect on some types of solid tumors, e.g., breast and stomach cancers.
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PMID:Inhibitory effect of triptolide on colony formation of breast and stomach cancer cell lines. 181 94

NH2-terminal amino acid sequence of the pS2 protein produced and secreted by human gastric cancer cells, MKN-45, was determined to be identical to that of MCF-7 cells. A clone encoding pS2 protein was isolated from the cDNA library constructed from MKN-45 cells. The nucleotide sequence was identical to that of pS2 cDNA previously isolated from human breast cancer cells, MCF-7, except for one nucleotide in the 3' untranslated region. Thus, in this cell line, the pS2 gene product is translated and secreted as in MCF-7 cells. RNA blot hybridization analysis revealed that pS2 gene was expressed well in two (MKN-45 and KATO-III; derived from poorly differentiated adenocarcinoma) but not in three cell lines (MKN-1, MKN-28 and MKN-74; from well differentiated adenocarcinoma), suggesting that expression of the pS2 gene depends on the state of cell differentiation. These results suggest that pS2 is expressed in human gastric cancer cells in an estrogen-independent manner and is possibly associated with the malignant state of cells.
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PMID:Expression of the pS2 gene in human gastric cancer cells derived from poorly differentiated adenocarcinoma. 231 59

Established human colon cancer cells with distinct degrees of differentiation (LoVo, well-differentiated; SW620, intermediate differentiation; and SW1116, poorly differentiated) were used to produce monoclonal antibodies (MoAbs) by standard hybridoma techniques. Specificity was tested by an enzyme-linked immunosorbent assay against human foreskin cells, 7 established human colon cancer lines, a panel of 17 established human tumor lines of different histological origins, purified carcinoembryonic antigen, panels of red blood cells, and a suspension of lymphocytes obtained from 30 random normal donors. MoAb LoVo-F4 3E4/1A1/2E10 (MoAb F4/2E10) reacted with five colon cancer lines and only slightly with MCF-7 cells (estrogen receptor positive breast carcinoma). MoAb LoVo-F4 3E4/1A1/5C10 also reacted with the previous five colon cancer lines and with two gastric cancer lines. A MoAb obtained with a LoVo 3 M KCl membrane extract reacted exclusively with LoVo cells. MoAb SW620-F1 4E5/1A3 reacted with only three colon cancer cell lines and an estrogen receptor negative breast cancer line. MoAb SW1116-F2 1E3/1A1 reacted with four colon carcinoma cell lines, one gastric cancer line, MCF-7 cells, and a lung cancer line. MoAb SW1116-F2 1F3/1B1 reacted intensely with purified carcinoembryonic antigen and with every carcinoembryonic antigen-producing cell line available in our laboratory. Further studies concentrated on the immunoglobulin G1 MoAb F4/2E10. We demonstrated that the purified MoAb did not inhibit binding of MoAb CA19-9 to any colon Ca lines and reacted with fresh human colon carcinoma specimens regardless of whether they were processed by cryostat or paraffin embedding after fixation in formalin for 24 through 96 h. Using the peroxidase-antiperoxidase technique, MoAb F4/2E10 did not react with 23 normal adult and 18 fetal (less than 3 months old) human tissue specimens. When tested on 312 specimens of diverse histological origins and diseases, the MoAb was positive in 57 of 62 colorectal cancers, in 12 of 19 villous adenomas, in 5 of 7 adenomatous polyps, and in 10 of 12 cases of ulcerative colitis. With the exception of 2 of 15 cases of Crohn's disease that were slightly positive, all tissues from nonmalignant diseases (regardless of histological origin) were consistently negative. There was only weak reactivity in 2 of 18 breast cancers, 7 of 21 squamous cell carcinomas, 4 of 27 lung tumors, 1 of 13 kidney carcinomas and in 7 miscellaneous tumors.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:New monoclonal antibodies against colon cancer-associated antigens. 242 73

The murine monoclonal antibody (MoAb)3H11 against human gastric cancer was purified with affinity column and conjugated with Mitomycin C (MMC). The binding activity of MoAb in the conjugate retained more than 90% of the original MoAb 3H11 when the molar ratios of MMC to 3H11 was 7-8:1. The killing rate of 3H11-MMC conjugate on human gastric cancer cells BGC 823 was increased significantly than that of free MMC in vitro. The selective cytotoxicity was verified with the following results: (1) the cytotoxicity of the conjugate was much higher than that of normal mouse IgG (nMuIgG) conjugated with MMC; (2) when breast cancer cells MCF-7 was used as target cells instead of BGC 823 cells, much lower cytotoxicity of the conjugate was observed; (3) the cytotoxicity of the conjugate on BGC823 cells could be blocked when the target cells was preincubated with MoAb 3H11, but not with MoAb 3G9 which did combine with BGC823 cells at binding sites different from MoAb 3H11. Nude mice were inoculated with BGC823 cells as a model of gastric cancer and treated with conjugate 3H11-MMC, nMuIgG-MMC, MMC or PBS (ip). It was shown that the time of tumor formation and the rate of tumor growth in 3H11-MMC conjugate treated animals were significantly different from that in control groups. The rate of inhibition of tumor weights was 60.4% for the conjugate 3H11-MMC treated group which was significantly higher than for other groups.
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PMID:[The selective cytotoxicity of monoclonal antibody conjugated with mitomycin C on human gastric cancer cells]. 261 75

Previous studies had shown that injection of Chinese herbal mixture (ICHM) had antitumor and anti-metastatic actions on various transplantable animal tumors. In the present study, the authors observed the obvious killing actions of ICHM on human gastric cancer cell line BGC-823 and breast cancer cell line MCF-7 in vitro. The IC50 were 0.02 g crude drug/ml and 0.018 g crude drug/ml respectively. The study of the effect of ICHM on the cell-cycle of BGC-823 cell showed that ICHM decreased the number of cells in S phase and increased the number of cells in G1 phase significantly. The results indicated that the BGC-823 cells was blocked on S phase by ICHM. Meanwhile, ICHM reduced 3H-TdR incorporation into DNA, the cpm value was much lower than that of the control.
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PMID:[The killing action of a Chinese herbal mixture on human tumor cells in vitro and its effect on cell-cycle]. 279 Nov 63

The difference in growth response between neoplastic and contact-sensitive normal cells was investigated by cell growth curve, colony forming efficiency and flow cytometric analysis. Neoplastic cells (MKN-28, MKN-45, and MCF-7), treated with paclitaxel at a concentration of 0.01 mM, showed growth inhibition, low colony-forming efficiency and a prolonged G2+M phase accumulation. Normal cells (Balb/c 3T3 cells and human fibroblasts originating from stomach cancer tissue), treated with paclitaxel at a concentration of less than 0.5 microM, showed no growth inhibition and no decrease in colony-forming efficiency. Normal cells treated with 1 microM of paclitaxel showed low accumulation in G2+M phases. The results show that paclitaxel at concentrations ranging from 0.01 to 0.5 microM had a cytotoxic effect against neoplastic cells but not against normal cells, such as fibroblasts around the cancer cells.
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PMID:Difference in cytotoxicity of paclitaxel against neoplastic and normal cells. 790 17

To ascertain whether the tumor cells can regulate the host immune systems through the production of the cytokines or their receptors, we examined the expressions of tumor necrosis factor alpha (TNF alpha), tumor necrosis factor beta (TNF beta), interleukin 2 (IL-2) and interleukin 2 receptor alpha chain (IL-2R alpha) on the human cancer cell lines by Northern blot analysis. We used K562 (leukemia cell line), MCF-7 (breast cancer cell line), LS180, HT29 (colon cancer cell lines), SH101 (gastric cancer cell line) and PH101 (pancreas cancer cell line). Expressions of TNF alpha, TNF beta and IL-2 mRNA were not detected in any of the tumor cell lines. However, 1.4 and 3.5 kilobases of the IL-2R alpha mRNA were expressed in the PH101 cells, but not in the other five cell lines. Furthermore, IL-2R alpha was detected on the cell surface of the PH101 cells by the flow-cytometric analysis with an anti-IL-2R alpha monoclonal antibody. Interestingly, the soluble IL-2R alpha (sIL-2R alpha) was found in the conditioned media obtained from the PH101 cell culture with a sandwich enzyme immunoassay. Moreover, the sIL-2R alpha secreted from the PH101 cells blocked the IL-2 dependent lymphocyte proliferation. These results indicate that the expression of IL-2R alpha on PH101 might suppress the IL-2 induced lymphocyte proliferation.
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PMID:The expression and biological activity of IL-2 receptor on a human pancreas cancer cell line. 850 43

Sialyl Lewis X serves as a ligand for selectins and is proposed to be implicated in hematogenous metastasis of cancers. When a cultured human breast cancer cell line, MCF-7, which does not express sialyl Lewis X, was transfected with human fucosyltransferase VI cDNA, a strong expression of sialyl Lewis X was induced on transfectant cells. The transfectant cells were found to be also reactive to the antibody NCC-ST-439, which was initially raised against human gastric cancer cells and later was shown to recognize a tumor-associated carbohydrate antigen in breast, gastric, and colon cancers. This suggested that the antigen recognized by NCC-ST-439 is closely related to sialyl Lewis X. Subsequent studies indicated that NCC-ST-439 specifically reacts to NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6GalNAcalpha1 -->R, the sialyl Lewis X on the mucin GlcNAcbeta1-->6 GalNAcalpha structure. The antibody was not reactive to the conventional sialyl Lewis X determinants on straight and/or branched polylactosamine structures including NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->3Galbeta1-->4 Glcbeta1-->R and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6Galbeta1-->4 Glcbeta1-->R. This was in clear contrast to most of the known anti-sialyl Lewis X antibodies, which do not discriminate internal structures carrying the sialyl Lewis X determinant. On the other hand, the newly generated monoclonal antibody GSC154-27 had a specificity completely the reverse of the specificity of NCC-ST-439 in that it was strongly reactive to the conventional sialyl Lewis X determinants in straight and branched polylactosamine structures, while far less reactive to the sialyl Lewis X determinant on the mucin GlcNAcbeta1-->6GalNAcalpha core structure. A set of these two antibodies would be useful in discriminating the molecular species of sialyl Lewis X expressed by malignant cells and in studying their functional significance.
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PMID:Specific detection of sialyl Lewis X determinant carried on the mucin GlcNAcbeta1-->6GalNAcalpha core structure as a tumor-associated antigen. 964 61

For the cancer cells which have overcome the second mitotic clock (M2), activated telomerase is essential and used as another marker of immortality. Many trials had been initiated to target telomerase, which is known to be specific to tumors. To determine the best in vitro cell system for testing the efficacy of telomerase inhibitors, we evaluated the telomerase activity of various cancer cell lines and measured their telomere lengths. We also treated some cancer cell lines with adriamycin and measured the changes of telomerase activity. Telomerase activity was evaluated in various cell lines with the TRAP (telomeric repeat amplification protocol) assay. Telomerase activity was calculated and translated into arbitrary units by computer-assisted densitometry with the control of telomerase activity in the 293 control cell line. Also, terminal restriction fragment lengths were measured using Southern blotting. We also measured telomerase activity and telomere lengths in 11 benign breast tumor tissues and 19 paired stomach cancer and normal tissues. Cancer cell lines treated with adriamycin we evaluated for changes of telomerase activity and the cell proliferation by MTT assay and dye exclusion test. Telomerase activity of cell lines was 95.3 24.1 unit with a range of 27.6-129.6 unit, while the telomere lengths of those cell lines were variable from 5.0 to 10.4 kbp with a median of 6 kbp. In 11 cancer cell lines which were not yet firmly established, we could not detect any telomerase activity. Low telomerase activity was detected in only 2 benign tumor tissues of breast with a median telomere length of 8.8 (7-10.5) kbp. Among paired 19 gastric cancer and normal tissues, only 7 cancer tissues showed weak telomerase activity. After adriamycin treatment, telomerase activity in YCC-S-1, YCC-S-3, MCF-7 and MCF-7/ADR was decreased in accordance with the changes of the cell numbers. Telomerase is specific to cancer tissues and is expressed differently from organ to organ. Telomerase activity by TRAP assay could be used as a chemosensitivity assay.
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PMID:Telomerase activity and telomere lengths in various cell lines: changes of telomerase activity can be another method for chemosensitivity evaluation. 968 83

We have constructed a fusion protein composed of tumor necrosis factor alpha (TNF-alpha) fused at its COOH terminus to the scFv region of monoclonal antibody (mAb) B1, an antibody that recognizes LeY antigen present on many human cancer cells. Our rationale for fusing the scFv to the COOH terminus of TNF was to diminish the binding of the fusion protein to TNF receptors because the COOH terminus of TNF is involved in binding, and thus to partially inactivate (detoxify) the molecule. The Fv region should then target and accumulate the fusion protein on cancer cells, which should compensate for the reduced binding affinity of the TNF moiety and lead to selective killing of TNF-sensitive antigen-expressing cancer cells. The fusion protein was expressed in Escherichia coli and found in insoluble inclusion bodies. After refolding and purification by anion exchange, Ni-NTA affinity, and size-exclusion chromatography, we obtained monomeric TNF-B1(Fv). This molecule binds to LeY antigen on cancer cells with the same affinity as B1(scFv) and B1(scFv) immunotoxins but with significantly lower affinity to the TNF receptor compared to the TNF trimer. TNF-B1(Fv) is very toxic to LeY antigen-expressing cancer cells that are sensitive to TNF (e.g., MCF-7 breast or CRL-1739 gastric cancer cells). This cytotoxicity is antibody targeted and TNF mediated because it can be prevented (as shown on MCF-7 cells) by an antibody competing for LeY antigen binding and by an antibody that neutralizes TNF-alpha. TNF-B1(Fv) kills TNF-alpha-sensitive cells that do not express the target antigen only at much higher doses than TNF trimer, and it does not kill LeY-bearing but TNF-alpha-resistant cells. TNF-B1(Fv) can cause significant tumor regression of MCF-7 tumor xenografts in mice at doses that are not toxic to the mice. Thus, the reduced binding of the TNF moiety to TNF receptors, combined with binding of the B1(Fv) portion to LeY antigen, makes TNF-B1(Fv) an agent for selective killing of LeY-expressing TNF-sensitive cancer cells.
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PMID:Cytotoxic and antitumor activity of a recombinant tumor necrosis factor-B1(Fv) fusion protein on LeY antigen-expressing human cancer cells. 981 29

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