phosphorus-radioisotopes and Testicular-Neoplasms

The effects of local irradiation and intraperitoneal injection of cisplatinum (CDDP) and VP-16 were examined in the sequential 31P magnetic resonance spectroscopy (MRS) in testicular cancer (TC-1) and bladder tumor (BT-8) of human origin, serially transplanted in nude mice. In the early phase of tumor growth, high-energy phosphate metabolites such as phosphocreatinine (PCr), adenosine triphosphate (ATP) and phosphomonoester (PME) were detected in both grafted tumors. However, the relative value of inorganic phosphate (Pi) to PCr increased with the growth of the tumor. Irradiation had the most pronounced effect to inhibit growth, followed by CDDP in both strains. However, growth inhibition was not observed in the VP-16 group. The effect of irradiation on the tumor histology was severely expressed in the nucleus and cytoplasm on the 4th to 7th day. The high PCr/Pi ratio during 2 to 14 days after irradiation suggested reoxygenation in the tumors with a high hypoxic cell fraction. In the CDDP and VP-16 groups, without histological change, the changes of PCr and Pi were milder than that in the irradiation group. Thus the spectroscopic analysis is presumably expected to give us an earlier and more accurate information on the tumor than the conventional parameters.

Topics: Adenosine Triphosphate; Animals; Antineoplastic Combined Chemotherapy Protocols; Humans; Magnetic Resonance Spectroscopy; Male; Mice; Mice, Inbred BALB C; Mice, Nude; Neoplasm Transplantation; Phosphocreatine; Phosphorus Radioisotopes; Testicular Neoplasms; Urinary Bladder Neoplasms

Sertoli cell intracellular protein 1 (SCc1) and 2 (SCc2) are polypeptides found in rat Sertoli cell cultures incubated with either FSH or (Bu)2cAMP. They were first identified in [35S]methionine-labeled Sertoli cell lysates using two-dimensional gel electrophoresis. Here we extend these observations by showing that SCc1 and SCc2 are present in rat seminiferous tubules, ovaries, and granulosa cells incubated with either FSH or (Bu)2cAMP and in testicular peritubular cells incubated with (Bu)2cAMP. Peritubular cells do not, however, respond to FSH with the production of SCc1 and SCc2. Peptide mapping with N-chlorosuccinimide revealed that SCc1 and SCc2 have similar cleavage patterns, suggesting a common primary amino acid sequence that is modified posttranslationally. Metabolic labeling with [32P]orthophosphate provided direct evidence that SCc1 and SCc2 are phosphoproteins. A shift in mobility of SCc1 and SCc2 toward the basic region of the gel to positions designated SCc1' and SCc2' occurred when cell lysates were treated with alkaline phosphatase before electrophoresis, providing additional evidence that SCc1 and SCc2 are phosphoproteins. SCc1 and SCc2 are also shown to be mitochondrially-associated in the Sertoli cell. Peptide maps of SCc1, SCc2, SCc1', and SCc2' obtained by treatment with alpha-chymotrypsin, are identical to proteolytic maps of proteins pp30', p30, and pp30 from adrenocortical cells. SCc1, SCc2, SCc1', and SCc2' are homologous with regard to their regulated expression, electrophoretic mobility, and mitochondrial localization to the adrenal proteins pp30' and pp30 as well as a series of 30 kilodalton proteins from MA-10 Leydig tumor cells. Both the adrenal cell proteins and the Leydig tumor cell proteins are thought to participate in cholesterol transport to the inner mitochondrial membrane, providing substrate for the cholesterol side-chain cleavage enzyme complex, an activity which the Sertoli cell does not perform, suggesting that alternative functions must be sought for SCc1 and SCc2 in Sertoli cells.

Topics: Adrenal Cortex; Alkaline Phosphatase; Animals; Cells, Cultured; Chymotrypsin; Cyclic AMP; Electrophoresis, Polyacrylamide Gel; Female; Follicle Stimulating Hormone; Granulosa Cells; Leydig Cell Tumor; Male; Mitochondria; Peptide Mapping; Phosphorus Radioisotopes; Phosphorylation; Proteins; Rats; Rats, Sprague-Dawley; Seminiferous Tubules; Sequence Homology, Amino Acid; Sertoli Cells; Subcellular Fractions; Succinimides; Sulfur Radioisotopes; Testicular Neoplasms; Tumor Cells, Cultured

DNA was extracted from [(3)H]thymidine-labeled Marek's disease virus (MDV) and purified by two cycles of CsCl gradient centrifugation in a fixed-angle rotor. The DNA was transcribed in vitro into (32)P-labeled complementary RNA (cRNA). MDV cRNA did not hybridize with DNA from chicken embryo fibroblast cultures or from chicken spleen, but hybridized efficiently with DNA from MDV particles or MDV-infected cell cultures. Five Marek's disease tumors from different chickens and different organs (ovary, liver, testis) were all found to contain MDV DNA sequences. The relative amount of MDV DNA varied from tumor to tumor and was between 3 and 15 virus genome equivalents per cell. The content of virus DNA per cell in spleens from tumor-bearing chickens was much lower than in tumors from the same animals. MDV-infected cell cultures contained a large proportion (28-59%) of virus antigen-positive cells, as measured by immunofluorescence, but tumor cells were negative in this respect (<0.02% positive cells). These data indicate that MDV is present in a provirus form in tumor cells.

Topics: Animals; Base Sequence; Centrifugation, Density Gradient; Chick Embryo; DNA, Viral; Ducks; Embryo, Nonmammalian; Female; Fibroblasts; Fluorescent Antibody Technique; Herpesviridae; Liver Neoplasms; Male; Marek Disease; Microscopy, Electron; Neoplasms, Experimental; Nucleic Acid Hybridization; Ovarian Neoplasms; Phosphorus Radioisotopes; RNA, Viral; Testicular Neoplasms; Tritium; Virus Cultivation

Topics: Humans; Male; Phosphorus; Phosphorus Radioisotopes; Testicular Neoplasms; Testis