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PubMed1970

Natural causes of variations in the weight of sarcoma 180.

The weights of mouse sarcoma 180 differed according to the varieties of mouse. In two varieties in which both sexes were studied the tumour weights were lower in females. In three varieties the tumours weighed less at lower environmental temperatures than at higher ones. At three environmental temperatures in the physiological range the surfaces were cooler than the adjacent skin, and the tissues of tumours were cooler than the surrounding subcutaneous tissues. These differences were greater in cooler than in warmer environments and increased as tumours grew larger. There were no histological changes to account for the different tumour weights at different environmental temperatures and it seems probable that tumours are unable to maintain their temperature and their metabolism in cool environments. In mice of the same breed kept at room temperature the smallest animals had the largest tumours in a weight range of 18-28 g.

Animals↗
PubMed1983

Relationship between antitumor effect and metabolites of 5-fluorouracil in combination treatment with 5-fluorouracil and guanosine in ascites sarcoma 180 tumor system.

The antitumor activity of 5-fluorouracil (FUra) against ascites Sarcoma 180 was significantly enhanced by coadministration of guanosine, and slightly by adenosine, but not by cytidine or uridine. In advanced ascites Sarcoma 180, guanosine also enhanced the action of FUra, but adenosine, uridine, and cytidine did not. The potentiation of antitumor activity by guanosine was reversed by addition of cytidine. The antitumor activity of FUra was significantly potentiated when guanosine was administered either 0 to 15 min before or 5 min after FUra. Changes in metabolites of FUra after potentiation by guanosine were investigated. Total radioactivity in the plasma was significantly decreased 10 min after the combined administration of [6-14C]FUra (3 mg/kg i.p.) and guanosine (100 mg/kg i.p.) in comparison with that of [6-14C]FUra alone and was slightly decreased by coadministration of [6-14C]FUra and adenosine. Conversely, it was significantly increased by uridine or cytidine. The decrease in total radioactivity in the plasma caused by guanosine was completely reversed by addition of cytidine. FUra, 5-fluorouridine, alpha-fluoro-beta-ureidopropionic acid, and alpha-fluoro-beta-alanine were found in the plasma. Intact FUra accounted for about 55% of the total radioactivity. The proportion of metabolites of [6-14C]FUra was not changed by coadministration of [6-14C]FUra and guanosine, adenosine, or cytidine, but the proportion of FUrd was increased by uridine. In the ascitic fluid, the total radioactivity derived from [6-14C]FUra was decreased by its combined administration with guanosine, and it was reversed by addition of cytidine. This pattern was similar to that in the plasma. The main FUra compound was intact FUra itself (90%), and 5-fluorouridine accounted for 1% of the total radioactivity in the ascitic fluid. On the other hand, total radioactivity of [6-14C]FUra in the tumor cells was significantly and slightly increased by guanosine and adenosine, respectively. Total radioactivity after [6-14C]FUra in combination with uridine or cytidine was less than that after [6-14C]FUra alone. Incorporation of [6-14C]FUra into RNA was increased about 3.7 times by its combination with guanosine in comparison with FUra alone, and it was increased 2.0, 0.6, and 0.7 times by adenosine, uridine, and cytidine, respectively. Moreover, FUra-nucleotides were significantly increased by guanosine. The increased radioactivity in RNA and FUra-nucleotides of tumor cells caused by guanosine was completely reversed by cytidine. These changes in incorporation into tumor cells were comparable to those in antitumor activity against ascites Sarcoma 180. The potentiation of antitumor activity of FUra by guanosine was considered to be due to an increase in incorporation of FUra into FUra-nucleotides and RNA in the tumor cells.

Adenosine↗
PubMed1984

Differential expression of intermediate-filament proteins in murine sarcoma 180 ascites or solid tumor.

The intermediate-filament proteins in Sarcoma 180 ascites cells and solid tumors generated by s.c. injection of ascites cells in NMRI or nude mice were analyzed by one- and two-dimensional gel electrophoresis and identified by immunological methods. The ascites form of Sarcoma 180 coexpresses keratin and vimentin, whereas the solid tumor ceases to synthesize keratins but continues to express vimentin. These reversible changes in the expression of intermediate-filament proteins may be due to a change in the differentiation program induced by environmental conditions like growth with or without cell contact.

Animals↗
PubMed1985

Demonstration of hepatic triglyceride lipase-like activity in ascites fluid of mice with sarcoma 180.

The contents of apolipoproteins of plasma and ascites fluid of mice with Sarcoma 180 were measured. The apolipoprotein A-I contents of plasma decreased with development of the tumor. The apolipoprotein C-II and C-III contents of plasma reached a maximum on day 7 after tumor inoculation and then decreased. The apolipoprotein A-I content of the ascites fluid was lower than that of normal mouse plasma. In contrast, the apolipoprotein C-II and C-III contents of the ascites fluid were higher than those of normal mouse plasma. The ascites fluid of mice with Sarcoma 180 was found to contain at least two lipases. One had a pH optimum of 5.5-7.0 and was strongly inhibited by chlorpromazine. The other had an alkaline pH optimum and was inhibited only slightly by chlorpromazine. When the ascites fluid was applied to a heparin-Sepharose column 40-45% of the applied triglyceride lipase activity was retained on the column, which was eluted with 0.75 M NaCl. This fraction was inhibited by heat-inactivated (56 degrees C, 10 min) human serum, and was relatively resistant to l M NaCl. These results suggest that one of the lipolytic enzymes present in the ascites fluid of mice with Sarcoma 180 is hepatic triglyceride lipase.

Animals↗
PubMed1984

Photoaffinity labeling of the Sarcoma 180 cell surface by daunomycin.

We have used photoaffinity labeling to investigate the distribution and function of daunomycin binding sites in Sarcoma 180 cells. When native daunomycin is irradiated at 366 or 488 nm in the presence of cells, the drug is irreversibly incorporated into cellular molecules. The cellular acceptor for the photoincorporation cannot be extracted by chloroform-methanol nor can it be degraded by DNase. However, the drug acceptor is susceptible to trypsin digestion. These results show that the photoincorporation site is composed of protein but not of lipid or DNA. Furthermore, the fact that photoincorporation proceeds equally well at 0 degrees (where drug does not accumulate inside the cells) as compared to 37 degrees (where free drug concentrates in the cells) suggests that the labeling reaction occurs principally at the cell surface. The photolabeling process is not highly specific since it is not saturable at high drug concentrations and cannot be competed for by unlabeled daunomycin. When 2 X 10(5) daunomycin molecules are incorporated per Sarcoma 180 cell, the cells can still accumulate free drug. This result suggests that the photolabeling reaction does not occur at the drug transport locus. Photoincorporation of daunomycin also does not affect the viability of Sarcoma 180 cells, as judged by a cloning assay. Thus, there is probably no surface receptor for the drug which mediates cytotoxicity when occupied. This result is as expected from previous work predicting that the mechanism of daunomycin involves disruption of some generalized membrane property like fluidity. However, in a series of Sarcoma 180 sublines selected for increasing resistance to daunomycin, the photoincorporation increases in direct proportion to drug sensitivity. Consequently, daunomycin appears to be capable of photoaffinity labeling a cell surface protein which, although not directly involved in the mechanism of cytotoxicity is implicated in the expression of drug resistance.

Animals↗
PubMed1982

Augmentation of antitumor activity by combined cryo-destruction of sarcoma 180 and protein-bound polysaccharide, EA6, isolated from Flammulina velutipes (Curt. ex Fr.) Sing. in ICR mice.

Augmentation of antitumor activity by combined in situ freeze-destruction of tumor (cryosurgery) and administration of antitumor active substances isolated from a hot water extract of an edible mushroom, Flammulina velutipes (Curt. ex Fr.) SING., was investigated in sarcoma 180 bearing ICR mice. Antitumor active substances of the mushroom included beta-(1,3)-glucan (EA3) and protein-bound polysaccharide (EA6). Antitumor activity was evaluated by the growth rate of the solid tumor rechallenged subcutaneously (s.c.) or by cumulative mortalities of the mice rechallenged intraperitoneally (i.p.) with the ascites tumor, on day 7 after cryosurgery. Weak antitumor effect induced by cryosurgery against challenged solid tumor of sarcoma 180 was markedly augmented by i.p. administration of EA6 (10 mg/kg). Cryosurgery of the solid sarcoma 180 apparently did not induce any antitumor effect against challenged ascites sarcoma 180. However, when cryosurgery was combined with oral administration of the polysaccharides (50 mg/kg), prolonged survival of the mice challenged with ascites sarcoma 180 i.p. was recognized by EA6, but not by EA3. Timing of the administration of EA6 (i.p.) with cryosurgery was best in pre- and post-cryosurgery. Immunological activity of EA6 to the host was discussed.

Agaricales↗
PubMed1979

[Effect of UHF frequency on the growth of sarcoma 180].

Studies performed on mice transplanted sarcoma 180 subcutaneously indicated that the UHF-field of non-thermogenic intensity in multiple (5-10 fold) total irradiation inhibits the tumor growth (T = 60%) and produces a 1.5 times increase of an average survival in tumor-bearing animals. It is suggested that there is a direct relationship between the increased antiblastic function of the body and a stimulating effect of the UHF-field on the immune response in animals.

Animals↗
PubMedDate not supplied

Tumor inhibition by titanocene complexes: activity against sarcoma 180.

The antitumor activity of various titanocene derivatives was examined against ascitic and solid, subcutaneously growing sarcoma 180. The complexes investigated were two dihalide compounds, (C5H5)2TiCl2 (I) and (C5H5)2TiBr2 (II), two carboxylato complexes, (C5H5)2Ti (cis-OOCCH = CHCOOH)2(III) and (C5H5)2Ti(OOCCCl3)2(IV), and the p-aminothiophenolate hydrochloride (C5H5)2Ti(p-SC6H4NH3+Cl-)2(V). Against ascitic sarcoma 180, best results were obtained for I; an injection of 50 mg/kg resulted in the survival of 40-50% of the animals (ILS, 161-184%). A similar result was recorded for cis-diamminedichloroplatinum(II), whereas the compounds II-IV induced a maximum cure rate of 20% (ILS, 95-139%). Against solid sarcoma 180, triple injections of I-V caused reduction of mean tumor weight to 23-53% of control values, the dichloro complex I exhibiting most pronounced activity. These results clearly underline antitumor potency for titanocene complexes (C5H5)2TiX2 modified at the acido ligand X.

Animals↗
PubMed1987

Thiol proteinase inhibitor in the ascitic fluid of sarcoma 180 tumor-bearing mice.

A thiol proteinase inhibitor (TPI) has been purified from the ascitic fluid of Sarcoma 180 tumor-bearing mice. The molecular weight of the inhibitor was estimated to be 67,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the substance inhibited papain, cathepsins B and L, but not cathepsins H and D and trypsin. The inhibitor also liberated kinin upon treatment with trypsin or mouse glandular kallikrein, indicating that the inhibitor is a kininogen, and the kinin liberated upon trypsinization was identified as bradykinin. An immunoreactive TPI with a molecular weight indistinguishable from that of the ascites TPI was found in plasma of non-tumor-bearing mice as well as that of tumor bearers. Plasma levels of immunoreactivity were increased up to twice the normal levels in tumor bearers inoculated with Sarcoma 180 or 3LL tumor cells. Supplementation of the purified ascites TPI into Sarcoma 180 culture medium caused a significant suppression of cell growth as well as [3H]thymidine incorporation at a concentration below that normally present in plasma. In contrast, addition of ascites-TPI to cultured mouse embryonic cells caused enhancement of cell growth as well as [3H]thymidine incorporation. These results indicate that in mice responding to tumor growth, a TPI corresponding to a kininogen is induced which may regulate tumor growth by countering tumor-related proteolytic activity.

Animals↗
PubMedDate not supplied

Marked induction of HSP47, a collagen-binding stress protein, during solid tumor formation of ascitic Sarcoma 180 in vivo.

HSP47, a heat shock-inducible glycoprotein of Mr = 47,000, is assumed to be a molecular chaperone specific for collagen. In addition to its stress inducibility, HSP47 has transformation-sensitivity; that is, the synthesis of HSP47 decreases after malignant transformation. We developed a rat monoclonal antibody against mouse HSP47, which we then used to examine the amounts of HSP47 in transplanted tumors. HSC70 (HSP73) was expressed constitutively in these ascites as well as solid tumors. While HSP47 was not expressed in ascitic form of Sarcoma 180, its expression was markedly induced during solid tumor formation of ascitic Sarcoma 180 cells after subcutaneous transplantation. The average survival period of ascites Sarcoma 180-bearing mice was 20.3 +/- 3.6 days (mean +/- SD), and was much shorter than that of solid Sarcoma 180-bearing mice. These findings suggest an important role of HSP47 in solid tumor formation as well as a possible marker for tumor malignancy.

Animals↗
PubMed1981

Adriamycin-induced changes in the surface membrane of sarcoma 180 ascites cells.

Adriamycin increases (a) the rate of agglutination of Sarcoma 180 cells by concanavalin A after brief exposure of 2-3 h and (b) membrane fluidity as measured by ESR within 30 min of exposure at concentrations of the anthracycline of 10(-7)-10(-5) M. The effect of adriamycin on agglutination is not due to an increase in the number of surface receptors for concanavalin A, since the extent of binding of the lectin is not altered by adriamycin and no change occurs in the rate of occupancy of the concanavalin A binding sites by the lectin in cells treated with the antibiotic. The order parameter, a measurement of membrane fluidity, decreases in cells exposed to adriamycin and is dose-related. The results indicate that adriamycin can induce changes in the surface membrane of Sarcoma 180 cells within a brief period of exposure to a low but cytotoxic level of this agent.

Agglutination↗
PubMed1984

Lipoprotein lipase-like activity in the liver of mice with Sarcoma 180.

The triglyceride lipase (TGL) activity of liver homogenates of mice with Sarcoma 180 was measured. The liver homogenate of normal or tumor-bearing mice was treated with 0.25% Triton X-100 and centrifuged at 100,000 g for 60 min, and the supernatant was applied to a heparin-Sepharose column. In normal mice, most of the TGL activities in the supernatant was eluted with 0.75 M NaCl from the column. In mice with Sarcoma 180, the TGL gave two peaks on heparin-Sepharose column chromatography, which were eluted with 0.75 M and 1.5 M NaCl, respectively. The activity in the first peak (0.75 M NaCl eluate) decreased; that in the second peak (1.5 M NaCl eluate) increased, and the ratio of the second peak to the first peak increased during tumor development. The livers of normal mice and mice on day 10 after tumor inoculation were perfused with heparin. The highest rate of the TGL release occurred within 1 min of heparin perfusion, and the bulk of heparin-releasable activity appeared within 2 min of perfusion in both normal and tumor-bearing mice. The TGL activity in liver perfusate of tumor-bearing mice, as well as that of liver homogenate, was resolved on a heparin-Sepharose column into two peaks, which were eluted with 0.75 M and 1.5 M NaCl, and most of the activity was eluted with 1.5 M NaCl. The nature of the TGL activity eluted from a heparin-Sepharose column was investigated. In both liver homogenates and liver perfusates, the first peak did not require serum for maximal activity and was relatively resistant to a high concentration of NaCl or protamine sulfate.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1980

Optimal conditions for antitumor activity of C. parvum against the ascites form of sarcoma 180.

Single and multiple doses of Corynebacterium parvum (C. parvum) ranging from 0.1--60 mg/kg were tested for antitumor activity against 10(6) sarcoma 180 cells in male CD1 mice. Determinations were made of the optimal dose and time of treatment needed to produce maximum suppression of the tumor using both median survival time and percent survival to day 90 as endpoints. A dose of 1 mg/kg given 3 days before sarcoma 180 transplant produced complete protection (100% survival). All other treatment regimens produced less of an effect. Single doses of 1, 10 and 60 mg/kg had significant antitumor activity when administered either on day 3, 2, or 1 before tumor implant, 0.1 mg/kg protected only when given on day 3. All single doses given 5 or 8 days before and anytime after tumor were ineffective. Multiple doses were only of advantage over single doses when treatments were after tumor cell inoculation. In vitro cytotoxicity studies demonstrated that both 1 and 60 mg/kg enhanced tumor cell killing by cells isolated from the peritoneal cavity, with the 1 mg/kg dose producing a greater effect. It was concluded that dose and time of administration of C. parvum, in relation to tumor implant, were important in determining optimal antitumor activity against sarcoma 180.

Animals↗
PubMed1999

Photodynamic effects induced by meso-tetrakis[4-(carboxymethyleneoxy)phenyl] porphyrin on isolated Sarcoma 180 ascites mitochondria.

Using mitochondria isolated from Sarcoma 180 ascites tumour in Swiss mice as a model system, we have evaluated the ability of a novel porphyrin, meso-tetrakis[4-(carboxymethyleneoxy)phenyl]porphyrin (H2T4CPP), to induce damage on photosensitization. Oxidative damage to mitochondria, one of the primary and crucial targets of the photodynamic effect, is assessed by measuring products of lipid peroxidation such as thiobarbituric acid reactive substances (TBARS) and lipid hydroperoxides (LOOH), besides the loss of activity of the mitochondrial marker enzyme succinate dehydrogenase (SDH). Analysis of product formation, the effect of deuteration and selective inhibition by scavengers of reactive oxygen species (ROS) show that the damage observed is due mainly to singlet oxygen (1O2) and to a minor extent to hydroxyl radicals (.OH). The 1O2 generation and triplet lifetime of this porphyrin have also been estimated. Fluorescence spectroscopy, used to ascertain the binding of this porphyrin to the mitochondrial proteins, shows a rapid association within 0-2 h and a decline thereafter. Confocal microscopy reveals intracellular localisation of this porphyrin in cells in vitro. Our overall results suggest that the porphyrin H2T4CPP, due to its ability to bind to mitochondrial protein components and to generate ROS upon photoexcitation, may have potential applications in photodynamic therapy.

Animals↗
PubMedDate not supplied

Inhibition of HSP47 during the transition from solid to ascitic form of Sarcoma 180 in vivo.

HSP47, a collagen-binding stress protein, has transformation-sensitivity; that is, the synthesis of HSP47 decreases after malignant transformation. We examined the expression of HSP47 in transplanted tumours by Western blotting. While HSP47 was not detected in ascites tumours including Ehrlich, P388 and Sarcoma 180, marked expression of HSP47 was observed in solid tumours such as B16, B16-BL6 and Sarcoma 180. The expression of HSP47 in Sarcoma 180 cells disappeared completely after these solid tumour cells were dispersed and inoculated intraperitoneally. These findings suggested an important role of HSP47 as a marker for tumour malignancy.

Animals↗