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      Lentinan Enhances Sensitivity of Mouse Colon 26 Tumor to cis‐Diamminedichloroplatinum(II) and Decreases Glutathione Transferase Expression

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          Abstract

          We investigated the influence of a combination of lentinan, a biological response modifier, and cis‐diamminedichloroplatinum(II) (CDDP) on the growth and glutathione S‐transferase (GST) content of colon 26 tumor to examine whether lentinan represses GST expression and enhances the therapeutic effects of CDDP. Female CDF 1 mice inoculated subcutaneously with transplantable colon 26 adenocarcinoma cells (1X10 6/mouse) received intraperitoneal administrations of lentinan, CDDP, or the two drugs in combination, on days 10, 14, 17 and 21 after the inoculation. On day 24, tumor weights (estimated from their length and width) were significantly lower in the CDDP+lentinan group (2.7±1.3g) than in the CDDP alone group (4.3±0.7g, p<0.05), both values being less than in the nontreated control group (7.2±1.5g). The major GST form of colon 26 tumor was identified as GST‐II, the Pi class form, and a minor form as GST‐III belonging to the Mu class. Both GST‐II and GST‐III values on day 24 were significantly decreased in the lentinan alone (0.90±0.29 and 0.26±0.11 μg/mg protein, respectively) and lentinan+CDDP groups (0.98±0.22 and 0.29±0.07 μg/mg protein), as compared with the control levels (1.39±0.20 and 0.52±0.11 μg/mg protein). However, these values were not different between the CDDP alone and lentinan+CDDP groups. Neither tissue interleukin (IL)‐6, glutathione nor platinum values were different between the two groups. IL‐6 values were elevated in about half of the samples treated with lentinan or CDDP and exhibited a modest inverse correlation with GST‐II levels ( r= ‐ 0.46). A GST inhibitor, ethacrynic acid, enhanced the sensitivity of cultured colon 26 cells to CDDP, suggesting the possible involvement of GST in modulating the cytotoxicity of CDDP to this cell line. These results indicated that lentinan administration decreases tissue GST‐II and GST‐III contents and enhances the sensitivity of colon 26 tumor to CDDP.

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          Most cited references 41

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          High resolution two-dimensional electrophoresis of proteins.

           P H O'Farrell (1975)
          A technique has been developed for the separation of proteins by two-dimensional polyacrylamide gel electrophoresis. Due to its resolution and sensitivity, this technique is a powerful tool for the analysis and detection of proteins from complex biological sources. Proteins are separated according to isoelectric point by isoelectric focusing in the first dimension, and according to molecular weight by sodium dodecyl sulfate electrophoresis in the second dimension. Since these two parameters are unrelated, it is possible to obtain an almost uniform distribution of protein spots across a two-diminsional gel. This technique has resolved 1100 different components from Escherichia coli and should be capable of resolving a maximum of 5000 proteins. A protein containing as little as one disintegration per min of either 14C or 35S can be detected by autoradiography. A protein which constitutes 10 minus 4 to 10 minus 5% of the total protein can be detected and quantified by autoradiography. The reproducibility of the separation is sufficient to permit each spot on one separation to be matched with a spot on a different separation. This technique provides a method for estimation (at the described sensitivities) of the number of proteins made by any biological system. This system can resolve proteins differing in a single charge and consequently can be used in the analysis of in vivo modifications resulting in a change in charge. Proteins whose charge is changed by missense mutations can be identified. A detailed description of the methods as well as the characteristics of this system are presented.
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            A new rapid and simple non-radioactive assay to monitor and determine the proliferation of lymphocytes: an alternative to [3H]thymidine incorporation assay.

            A one-step non-radioactive assay to determine the proliferation of murine lymphocytes, lymphoid tumor cells and hybridoma cells is described. This assay requires the addition of Alamar Blue dye to cell cultures and the degree of change in its color, which is reflective of the extent of cellular proliferation, can be determined by an ELISA plate reader. Alamar Blue must be added during the initial phase of cell culture. The pattern of concanavalin A (ConA) or anti-CD3 antibody-induced proliferative response of murine lymphocytes as assessed by Alamar Blue was similar to that of a [3H]thymidine assay. Similarly, the spontaneous proliferation curve of anti-CD3 antibody secreting cell line (YCD3-1), monocytic macrophage cell lines (PU5-1.8, P388D1, J774.1) and myeloma cells (Sp2/0) as determined by Alamar Blue closely resembled that of the [3H]thymidine assay. The minimum detectable number of proliferating cells was comparable in Alamar Blue and [3H]thymidine assays. Since cell lysis/extraction and washing procedures are not involved in the Alamar Blue assay, this approach has several distinct advantages over currently available assays (eg. [3H]thymidine). First, it allows daily monitoring of proliferation without compromising the sterility of cultures. An indication of proliferation can be evaluated (spectrophotometrically or visually) as early as 24 h after ConA stimulation. Second, unlike previously reported assays, Alamar Blue permits further analysis of proliferating cells by other methods. Analysis of cells in culture with Alamar Blue for various surface antigens (CD44, CD45RB, CD4, heat stable antigen) by flow cytometry revealed that the fluorescent profile and relative percentage of cells in cultures with the Alamar Blue were comparable to those without this reagent. The salient advantages of Alamar Blue assay over the [3H]thymidine assay include: (i) non-radioactivity; (ii) simplicity; (iii) less costly; (iv) non-labor intensive; (v) rapidity of assessment of proliferation of large number of samples; (vi) non-toxicity; (vii) usefulness in determining the kinetics of cell growth of hybridomas; and (viii) non-interference of secretion of antibodies by a hybridoma cell line.
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              Drugs five years later. Cisplatin.

               L Einhorn,  P Loehrer (1984)
              Cisplatin is a metal coordination compound that was approved for clinical use in treating testicular cancer 5 years ago. Although early trials showed marked gastrointestinal and renal toxicities, treatment-related morbidity has been significantly alleviated with modern antiemetic therapy and adequate pretreatment hydration. More recent clinical studies of cisplatin have shown a broad range of activity and provide a better understanding of the drug's pharmacology, mechanism of action, and toxicity. Variations in the dosage and mode of administration as well as development of cisplatin analogues are being currently studied.
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                Author and article information

                Journal
                Jpn J Cancer Res
                Jpn. J. Cancer Res
                10.1111/(ISSN)1349-7006a
                CAS
                Japanese Journal of Cancer Research : Gann
                Blackwell Publishing Ltd (Oxford, UK )
                0910-5050
                1876-4673
                November 1996
                : 87
                : 11 ( doiID: 10.1111/cas.1996.87.issue-11 )
                : 1171-1178
                Affiliations
                [ 1 ]Second Department of Biochemistry, Hirosaki University School of Medicine, 5 Zaifu‐cho, Hirosaki 036
                Author notes
                [* ]To whom correspondence should be addressed.
                Article
                CAE1171
                10.1111/j.1349-7006.1996.tb03128.x
                5921014
                9045947
                Page count
                References: 47, Pages: 8
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                Custom metadata
                2.0
                November 1996
                Converter:WILEY_ML3GV2_TO_NLMPMC version:4.6.9 mode:remove_FC converted:04.11.2015

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