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PubMed1995

Developing Yoshida sarcoma does not influence the fatty acid composition of adipose tissues in the rat.

The potential involvement of individual fatty acids from diet or from adipose tissue in the outcome of cancer emphasizes the need for more insight into the relationship between fatty acids and tumor growth. The main objective of the present study was to examine whether rapid tumor growth would induce changes in the fatty acid composition of adipose tissue, indicating selective use and thus deposition of dietary fatty acids and/or selective removal of stored fatty acids from adipose tissue. We used a rodent model of transplanted solid tumor (Yoshida sarcoma) and measured the fatty acid composition from different adipose sites in the absence and in the presence of tumor but at the same intake of dietary fatty acids. We found that Yoshida sarcoma could grow rapidly without significantly altering the fatty acid composition of adipose tissue, irrespective of its location. These results do not favor the hypothesis of a selective removal of fatty acids from adipose tissue by growing tumors. They moreover indicate that tumors do not modify the storage of individual dietary fatty acids.

Adipose Tissue↗
PubMed1981

Antitumor activity of new nitrosoureas on Yoshida sarcoma ascites cells implanted into the colon wall of rats.

The chemotherapeutic activity of 12 newly synthesized nitrosoureas was compared in tests using Yoshida sarcoma ascites cells implanted into the wall of the descending colon in Sprague-Dawley rats. Cyclophosphamide and the nitrosoureas BCNU, MeCCNU, and chlorozotocin served as positive controls. Among the nitrosoureas tested, 1-(2-hydroxyethyl)-3-(2-chloroethyl)-3-nitrosourea (hydroxyethyl-CNU), chlorozotocin, 1-(2-chloroethyl)-1-nitroso-3-(4-morpholino) urea, 1-(2-chloroethyl)-1-nitroso-3-(1-piperidino) urea, 4-[1-(2-chloroethyl)-1-nitroso-3-[4-(2,6-dimethylmorpholino)] urea, and 1-(2-chloroethyl)-1-nitroso-3-(3,4-methylenedioxybenzyl) urea were found to be the most active compounds in this tumor model. Based on the present results, morpholino-CNU is considered the most promising compound among these newly synthesized BCNU analogues.

Animals↗
PubMed1975

Intracellular distribution of various enzymes concerned with DNA synthesis from normal and regenerating rat liver, and Yoshida sarcoma.

During the fractionation of various enzymes concerned with DNA synthesis from the postmicrosomal supernatant fraction of various tissues, DNA polymerace [EC 2.7.7.7], thymidine kinase [EC 2.7.1.75], dTMP kinase [EC 2.7.4.9], deoxycytidine kinase [EC 2.7.1.74], and deoxycytidine monophosphokinase (dCMP kinase) [EC 2.7.4.14] were found in the pellet fraction of postmicrosomal supernatant. Further, the uridine kinase [EC 2.7.1.48] and aspartate transcarbamylase [EC 2.1.3.2] activities of postmicrosomal supernatant from various tissues were also present in this pellet fraction. The activities of DNA polymerase, thymidine kinase, uridine kinase, and aspartate transcarbamylase from normal and regenerating rat liver, and Yoshida sarcoma were higher in the pellet fraction than in the supernatant. On the other hand, the activities of dTMP kinase, dCMP kinase, and orotidine-5'-phosphate decarboxylase [EC 4.1.1.23] were lower in the pellet fraction than in the supernatant. The pellet fractions of regenerating rat liver and Yoshida sarcoma showed a remarkable incorporation of various precursors (thymidine, dTMP, deoxycytidine, and dCMP) into DNA in the presence of a suitable DNA template, ATP and all four deoxynucleoside 5'-triphosphates for DNA synthesis. Normal adult rat liver catalyzed a much smaller incorporation of all these precursors, except for dCMP.

Animals↗
PubMed1989

[Increase in the generation of superoxide radicals and in the inhibitory effect on Yoshida sarcoma of anthracycline antitumor agents by ultrasound].

The antitumor effects of ultrasonic (US) irradiation in combination with the administration of an anthracycline drug, such as adriamycin and THP-adriamycin, were investigated from a viewpoint of the generation of superoxide radicals (SOR). In the in vitro experiments, the generation of SOR by US irradiation was measured by the amount of cytochrome c reduced. The addition of the drug stimulated the generation of SOR by US irradiation. In the in vivo experiments, Donryu rats inoculated subcutaneously by Yoshida sarcoma were treated with US irradiation in combination with the drug. During US irradiation, the temperature of the rat tissue irradiated was kept below 37 degrees C to avoid thermal effects. To know the optimum timing of US irradiation after the administration of the drug, the drug concentrations in the tumor and blood were determined and the time course of drug concentrations was analyzed pharmacokinetically. The effects of drugs and/or US irradiation showed antitumor activity judged by the growth of the tumor size or the survival time of rats. The combination treatments of US irradiation with the drug marked additional or synergistic effects on Yoshida sarcoma. Considering the relationship between the antitumor effect in vivo and the generation of SOR in vitro, the increase of anti-tumor effect of US irradiation by the anthracycline drug may be caused by the stimulation of the generation of SOR.

Animals↗
PubMed1976

[On the angio-architecture of intramuscularly implanted Yoshida-sarcoma in untreated and lithium carmine-treated rats (author's transl)].

Investigations were made on the angio-architecture of intramuscularily implanted Yoshida-sarcomas in untreated Wistar-rats and in animals treated with lithium carmine. The injected quantity of lithium carmine led to RES-activation according to the data in the literature. The presentation of the vessels was made by corrosion technique using the synthetic material KALLOCRYL after rinsing the vessels with the proper ester. The pre-existent vessels in the surrounding of the tumor showed an adaptation the expansive growth of the tumor. After starting the experiment the tumor-owned vessels showed an increasing tendency to grow out. The vessels of the treated animals rected in a more regularly and orientated course than those of the untreated animals. In the following time vascularisation in the untreated animals was considerably decreasing, whereas a clear vascularisation was evident in the treated animals until the end of the study. These different findings may be the expression of a local vascular reaction in the implanted tumor following RES-activation induced by lithium carmine.

Animals↗
PubMed1980

Effect of hyperglycemia on blood flow, pH, and response to hyperthermia (42 degrees) of the Yoshida sarcoma in the rat.

Hyperglycemia (blood glucose, > 20 mmol/liter) caused a 90 to 100% inhibition of blood flow in the solid Yoshida sarcoma of rat feet, as measured by the fractional distribution of 86Rb and 133Xe clearance. Blood flow through the normal gastrocnemius muscle was increased by 50%, while liver blood flow remained unaltered. Hyperglycemia abrogated the temperature differential (approximately 1 degree) between the heating bath and the tumor, promoting more uniform tumor heating. During the period of reduced blood flow, the pH of the tumor extracellular fluid, measured by miniature glass electrode, declined from 7.19 to 6.63 due to decreased efflux of lactate from the tumor. Tumor intracellular pH, measured by partitioning of dimethyloxazolidinedione across the cell membrane, increased from 7.21 to 7.36. At a very high blood glucose concentration (50 mmol/liter), the tumor was isolated from the host, with almost total blockade of water, chloride, glucose, lactate, and dimethyloxazolidinedione exchange between the tumor and the blood. Hyperglycemia therefore represents a convenient means of isolating the Yoshida sarcoma from the host blood supply to enable more selective treatment with hyperthermia and possibly other modalities.

Animals↗
PubMed1980

Purification and properties of adenylosuccinate synthetase from Yoshida sarcoma ascites tumor cells.

Adenylosuccinate synthetase (IMP:L-aspartate ligase (GDP-forming), EC 6.3.4.4) was purified about 750-fold to a homogeneous state from Yoshida sarcoma ascites tumor cells. A yield of 38% purified enzyme was achieved by a procedure including affinity chromatography on hadacidin-Sepharose 4B. Ultracentrifugal analyses showed that the molecular weight of the native enzyme was 102 000 with an s20,w value of 4.5 and that the molecular weight in 6 M guanidine-HCl was 47 000. These values indicate that the native enzyme is composed of two subunits. The isoelectric point was determined to be 5.9 by isoelectric focusing. The optimum pH for activity was 6.8-7.0. The Km values for IMP, aspartate and GTP were calculated to be 4.1, 9.8 and 0.7 . 10(-4) M, respectively. The antibiotic, hadacidin was strongly inhibitory, causing competitive inhibition with respect to aspartate with a Ki value of 2.5 . 10(-6) M. Nucleoside mono- and diphosphate also inhibited the enzyme activity, but their inhibitions were not apparently specific. The purified enzyme showed full activity in the presence of Mg2+, and Mg2+ could be partially replaced by Mn2+, Co2+, Ca2+ or Cu2+. Divalent metal ions, such as Cd2+, Pb2+, Zn2+, Cu2+ and Mn2+, interfered with the activity by antagonizing Mg2+. Hg2+ or PCMB inactivated the enzyme, suggesting that an SH-group may be important for activity.

Adenylosuccinate Synthase↗
PubMed1991

[Does parenteral linoleic acid modify tumor growth? Studies with the Yoshida sarcoma model].

In an experimental study with sprague-dawley-rats we tested the effect of parenteral substituted LCT-fats on tumor growth of the Yoshida sarcoma in its ascites form. Therefore we tested 4 groups with 10 tumor-bearing and 10 non-tumor-bearing rats. We added group 1-3 LCT-fats in different doses. Group 4 was fed enterally. We found that tumor-bearing rats had a higher nitrogen retention than non-tumor-bearing rats. Non-tumor-bearing rats showed a higher nitrogen concentration in the muscles. The portion of nitrogen increased with increasing portion of fat. The content of nitrogen in the ascites, the quantity and the number of tumor cells was reversed in proportion to the portion of fat. For the host we showed that he cannot make use of the energy directly. The tumor does not grow in proportion to the available energy but has to support itself from the catabolism of the host.

Animals↗
PubMedDate not supplied

Factors governing hyperthermia-induced pH changes in Yoshida sarcomas.

The impact of various factors modulating the acidification of tumour tissue upon localized ultrasound hyperthermia (1.7 MHz) at 44 degrees C for 60 min was investigated. Yoshida sarcomas were implanted into the hind foot dorsum of Sprague-Dawley rats. Frequency distributions of tumour tissue pH values were measured with miniaturized needle glass pH electrodes (diameter of the sensitive tip: 650 microns). During normothermia the average tumour pH is 6.87 +/- 0.21. No relationship is found between tumour pH and tumour size (range: 0.6-5.4 g). A pH gradient exists from the tumour periphery (0.5-3.5 mm) to more central tissue layers (7.5-10.5 mm; delta pH = 0.17). During hyperthermia with heating-up rates greater than 1.5 degree C/min, mean tumour pH drops to 6.71 +/- 0.20 considering all tumours. The pH reduction observed is size-dependent being most pronounced in medium-sized tumours (wet weights around 2.4 g, delta pH = 0.26). Using the same tumour sizes, but heating-up rates less than 0.7 degree C/min, the tissue acidification is more severe (delta pH = 0.40). To a small extent, pH changes also depend on the tumour region investigated (e.g. central vs. peripheral tissue layers) leading to a flattening of the pH gradient from the tumour shell to the centre during heat treatment. During hyperthermia an interstitial oedema occurs, being mostly marked in small tumours (around 1.4 g). Considering systemic changes, a transient increase in perfusion pressure (leading to a change in blood flow), as well as a slight elevation of blood glucose levels (leading to a higher glucose supply), during hyperthermia may contribute to the pH drop.

Animals↗
PubMed1983

Molecular properties of a granulocyte/macrophage colony-stimulating factor obtained from the serum-free culture of Yoshida sarcoma cell Line YSSF-212T.

A granulocyte/macrophage colony-stimulating factor (Peak-1 CSF) was partially purified from the medium of a serum-free culture of Yoshida sarcoma cells (Line YSSF-212T). Its elution position in gel-filtration chromatography corresponded to a molecular weight of about 22,000. The factor had an isoelectric point at pH 4.5 and a sedimentation coefficient of 2.3 S. The major part of its activity was not bound by Concanavalin A-Sepharose. Although CSF activity behaved as a single component in the gel-filtration and isoelectrofocussing procedures, subsequently it was resolved into two species by preparative discontinuous polyacrylamide gel-electrophoresis. This resolution indicates microheterogeneity of the CSF molecule. Oxidation with periodate readily inactivated L . P3-cell CSF, but the YSSF-cell CSF was fairly resistant. Moreover, titration with anti-L cell CSF serum showed a definite difference between L . P3-cell CSF and YSSF-cell CSF.

Animals↗
PubMed1981

DNA strand breaks and repair synthesis in Yoshida sarcoma: cells with differential sensitivities to bi-functional alkylating agents and UV light.

The induction of DNA-strand breaks and repair synthesis has been examined in cultured Yoshida sarcoma cell lines sensitive (YS) and resistant (YR) to methylene dimethanesulphonate (MDMS). Using an alkaline DNA unwinding-hydroxylapatite technique, we were able to detect breaks in DNA immediately after MDMS treatment and at similar levels in both YS and YR cells. MDMS treatment and post-treatment incubation in the presence of 1-beta-D-arabino-furanosylcytosine (araC) lead to a large increase in the numbers of breaks when compared with MDMS treatment alone which indicated that many of the DNA-strand breaks seen after MDMS treatment were intermediates in excision repair. The magnitude of break incidence with the araC treatment was again equal in YS and YR cells indicating that these 2 lines made enzymic incisions next to MDMS-induced lesions with equal capacities. During incubation following MDMS treatment, the levels of DNA-strand breaks in YR cells were found to decrease more rapidly than in YS cells. Parallel DNA-repair synthesis estimations, using BND-cellulose chromatography, revealed that the increased rate of decline in breaks in YR cells was accompanied by an increase in repair-synthesis activity compared to YS cells. This was interpreted as indicating that an intermediate step in an excision-repair pathway for MDMS-induced lesions was relatively deficient in YS compared to YR cells. A similar difference in the rates of decline of DNA-strand breaks between YS and YR cells was also observed following treatment with UV light to which MDMS-resistant YR cells also display cross-resistance. However, no such difference was detected following treatment with the monofunctional alkylating agent, methyl methanesulphonate, to which YS and YR cells are equally sensitive. These results suggest that resistance to MDMS in the YR cell line is achieved by an increased efficiency in the gap-sealing component of the excision-repair process.

Alkylating Agents↗
PubMed1975

Change in immunosensitivity of Yoshida sarcoma produced by chemical modification of cell-surface membrane.

Change in immunosensitivity of various chemically modified cells to the specific antibody was investigated in the Donryu rat-Yoshida sarcoma system. Among various agents, Amphotericin-B and cetyltrimethylammonium bromide were effective in increasing the immunosensitivity. This effect was not due to the general damage of cell membrane but to the increase of antigen exposed on the cell-surface membrane.

Amphotericin B↗
PubMed1994

Field bean protease inhibitor preparations, unlike methotrexate, can completely suppress Yoshida sarcoma tumor in rats.

Protease inhibitor preparations (PIP) with antitryptic and antichymotryptic activities, isolated from field bean legume as well as doxorubicin and cyclophosphamide could effectively suppress the growth of Yoshida sarcoma ascites tumor cells transplanted in adult rats and prevent their death. As against this, methotrexate and heat-inactivated PIP were ineffective in such rats at varied doses of treatment tried. The percent survival of animals appeared to be related to the purity, treatment mode and the dose of PIP used. Zymographic analysis of the trypsin activated sarcoma cell homogenate revealed the presence of six protease bands in the molecular weight range of 51kD to 206kD. Prolonged interactions of such zymograms with protease inhibitors such as 20mM EDTA or 5mM diisopropyl flurophosphate (DIFP) or 400 micrograms/ml of PIP in reaction buffer indicated that these are not metalloproteases but serine proteases whose activities are inhibited by PIP and DIFP. Since proteases are involved in cell growth regulation and cell transformation, we hypothesize a positive relationship between the field bean protease inhibitor's blocking action on tumor cell proteases and its tumor suppressing activity.

Animals↗
PubMed1978

Colony-stimulating factors active on human bone marrow cells from a Yoshida sarcoma cell line.

Colony-stimulating factors (CSF) active on both human and murine bone marrow colony-forming units in culture (CFU-C) were found in the conditioned medium of Yoshida sarcoma cells (line YSSF-212T), although the cells originated from rats. The CSF were inactivated by digestion with trypsin, alpha-chymotrypsin, and pronase. By chromatography on DEAE-cellulose, the CSF were separated into five subgroups with different capacities to stimulate mouse granulocyte and macrophage progenitors. CSF in these five peaks were eluted from an Ultrogel AcA 44 gel filtration column with apparent molecular weights of 22,000-25,000 daltons. CSF of nonhuman origin stimulating human CFU-C would be useful in hematologic studies of bone marrow cells.

Animals↗
PubMed1991

Structured lipid made from fish oil and medium-chain triglycerides alters tumor and host metabolism in Yoshida-sarcoma-bearing rats.

The effects of structured lipid composed of fish oil and medium-chain triglycerides (Fish/MCT) on tumor and the host metabolism was compared with conventional long-chain triglycerides (LCTs) in Yoshida-sarcoma-bearing rats receiving TPN for 3 d. The two parenterally fed groups were divided into two treatments, saline or tumor necrosis factor (TNF), given intravenously at 20 micrograms/kg body wt. Changes in tumor volume, body weight, urinary nitrogen, whole-body and tissue protein kinetics, and fatty acid composition were measured. The study revealed that Fish/MCT feeding inhibited tumor growth, which could be attributed to decreased tumor protein synthesis. Body weight and nitrogen were better maintained by Fish/MCT feeding. In addition, the effects of Fish/MCT on tumor growth were synergistic with TNF treatment. The results demonstrate that dietary fat composition can influence fatty acid compositions of tumor tissue as well as tumor protein kinetics after a short period of TPN feeding.

Animals↗
PubMed1984

Cytochemical characterization of Yoshida sarcoma cells resistant to dibromodulcitol.

Two Yoshida ascites sarcoma cell populations, one of them originally sensitive and another rendered resistant to the alkylating agent dibromodulcitol (DBD), were compared for doubling time, labeling index, survival time, morphological features, cellular DNA content and modal DNA value. Cross-resistance studies were carried out on bilaterally growing solid tumours derived from the sensitive and resistant Yoshida cell populations. Glycogen-containing granules appeared in the cytoplasm of the DBD-resistant sarcoma cells; these were not present in the sensitive tumour. The growth parameters of the sensitive tumour were throughout the 10-day observation period characteristic of rapidly proliferating tumours, whereas those of the DBD-resistant tumour was characteristic of slowly proliferating systems. As compared to the mean DNA values for normal somatic cells (lymphocytes), those found for both tumours indicated that the cells were hyperdiploid aneuploid. The DNA stem line in the resistant tumour proved to be significantly smaller than that in the sensitive tumour. These results indicate that a reduction of malignancy in the Yoshida tumour is associated with a developed resistance to dibromodulcitol. The resistant tumour showing cross-resistance to dianhydrogalactitol, diacetyl-dianhydrogalactitol and to nitrogen mustard retained full sensitivity to cyclophosphamide and adriablastin (Adriamycin), and proved to be collaterally sensitive to vincristin.

Animals↗
PubMed1983

IMP dehydrogenase. II. Purification and properties of the enzyme from Yoshida sarcoma ascites tumor cells.

The preceding paper showed that IMP dehydrogenase [IMP:NAD+ oxidoreductase, EC 1.2.1.14] tended to form a precipitable complex(es) through ionic and hydrophobic interactions. On the basis of these observations, a method was developed for purification of IMP dehydrogenase from Yoshida sarcoma ascites cells. On SDS-polyacrylamide gel electrophoresis, the purified preparation (1.19 U/mg protein) appeared homogeneous and its minimum molecular weight was estimated to be 68K daltons. Amino acid analyses indicated a subunit molecular weight of 68,042. Molecular sieve chromatography in the presence of 10% (NH4)2SO4 showed that the molecular weight of the native enzyme was 127K daltons. These values indicate that the native enzyme is composed of two identical subunits. However, the purified enzyme gave 4 protein bands on polyacrylamide gel electrophoresis under non-denaturing conditions, and appeared as a single fraction in the vicinity of the void volume on Ultrogel AcA 34 column chromatography at low salt concentration, indicating that its molecular weight exceeded 200K daltons. These findings indicate that the enzyme tends to aggregate owing to its own physicochemical characteristics. The Km values for IMP and NAD were calculated to be 12 and 25 microM, respectively, and the Ki values for XMP, GMP, and AMP to be 109, 130, and 854 microM, respectively. The purified enzyme showed full activity in the presence of K+, and K+ could be partially replaced by Na+. PCMB inactivated the enzyme, but the activity was completely restored by the addition of DTT. Cl-IMP also inactivated the enzyme and IMP prevented this inactivation.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗