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Metabolism of Neoplastic Tissue II. a Survey of Enzymes of the Citric Acid Cycle in Transplanted Tumors*

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Metabolism of Neoplastic Tissue II. a Survey of Enzymes of the Citric Acid Cycle in Transplanted Tumors* Metabolism of Neoplastic Tissue II. A Survey of Enzymes of the Citric Acid Cycle in Transplanted Tumors* CHARLES E. WENNER,t MORRIS A. SPIRTES, AND SIDNEY WEINHOUSE (The Lankenau Hospital Research institute and the Instituiefor Cancer Research, and the Department of Chemistry, Temple University, Philadelphia, Pa.) Recent isotopic tracer studies of tumor metabo on homogenates of the whole tissue or on extracts lism indicated that the neoplastic cell can carry out of acetone powders. All assays were carried out in the complete oxidation of glucose and fatty acids the zero order range of substrate concentration via the citric acid cycle (84, 85). In view of a strong and with proportionality of enzyme activity and body of evidence against the occurrence of the tissue concentration—these conditions having Krebs cycle in tumors (18, 19), further information been established by preliminary experiments. De bearing on this problem seemed desirable. Accord tails of the procedures are given in the individual ingly, a survey was undertaken of various trans sections and in the table headings. The prepara planted neoplasms for their content of citric acid tions of homogenates will be described in the indi cycle enzymes. In order to obtain a “profile―of vidual assays. The acetone powder extracts were enzymatic activity, approximate assays were car prepared as follows : the freshly dissected tissue ned out of those enzymes for which straightfor (pooled from four to six animals) was homogenized ward methods were available; these included for 1 minute at 2°C. in a Waring Blendor with 2 malic, isocitric, and a-ketoglutaric dehydroge volumes of acetone. The homogenate was filtered nases, the “condensing―enzyme, and the hydrases, with suction, and the residue was resuspended in fumarase and aconitase. The peripheral enzymes, 10 volumes of acetone and refiltered with suction. lactic dehydrogenase and oxalacetic carboxylase, The tightly packed cake was powdered in a mor were also assayed, but succinic dehydrogenase, tar, air-dried on filter paper, then dried thoroughly having been thoroughly investigated and found to in a vacuum desiccator over sulfuric acid and par be present in tumors by others (24, 25), was affin, and stored at less than 5°.The extract was omitted from the present investigation. All the prepared bystirring 1 gm. of the acetone powder tumors were found to possess the enzymatic equip with 10 ml. of water for 10 minutes at 40°C. and ment for the citric acid cycle. by centrifuging at 3,000 r.p.m. for 20 minutes in the angle head of a No. 2 refrigerated Internation METHODS AND RESULTS al Centrifuge. The opalescent solution was used as Tumors.—The neoplasms employed in this such or was further diluted if necessary. study were described in previous papers (33, 35). Substrates and other materials.—Pyruvic, malic, They were implanted subcutaneously and used in citric, and a-ketoglutaric acids, and adenosine the experiments when they attained a diameter of triphosphate were comm€@cialproducts. Lithium approximately 1 cm. Assays were carried out either acetyl phosphate, 60 per cent pure, was obtained a This work was aided by grants from the American Cancer through the kindness of Drs. Stern and Ochoa. Society, on recommendation by the Committee on Growth of Oxalacetic acid, 90 per cent pure by aniline citrate the National Research Council; the National Cancer Institute assay (5), was prepared from the ester by the pro of the National Institutes of Health, Public Health Service; cedure of Krampitz and Werkman (9). Isocitric and the U.S. Atomic Energy Commission, Contract No. acid was prepared by catalytic reduction of tn AT(80-1)777. A preliminary report of a portion of this work has appeared ethyl oxalosuccinate, synthesized according to the (36). method of Wislicenus and Waldmtiller (38). The t This study will constitute part of a thesis to be presented reduction was carried out with platinum at room by C. E. Wenner to the Graduate School of Temple University temperature at 3—4atmospheres of hydrogen, and in partial fulfillment of the requirements for the Ph.D. degree. the reduced product was saponified with the cal Receivedfor publication September 24. culated quantity of sodium hydroxide. The final 44 Downloaded from cancerres.aacrjournals.org on September 29, 2021. © 1952 American Association for Cancer Research. WENNER et al.—Metabolism of Neoplastic Tissue. II 45 product consisted of a mixture of four isomers, D gm.) were intimately mixed with 0.5 gm. of alumi and t-isocitric and D- and fralloisocitric acids. As na (Alcoa No. A301, 325 mesh) by grinding to @ expected, only of the product was acted upon by gether in a mortar for a few minutes at room tem aconitase, the active isomer being presumably perature. The mixture was transferred to a Lus D-isocitric. teroid centrifuge tube of 10-ml. capacity and Reduced diphosphopyridine nucleotide was pre stirred with 0.5 ml. of M/50 phosphate buffer, pared according to the method of Ohlmeyer (17) pH 7. The suspension was centrifuged for 20 mm from commercial cozymase assaying 33 per cent utes in a Sorvall centrifuge at 12,000 r.p.m. The pure by the enzymatic method of Racker (22) em supernatant fluid, which contained the transacety . ployi@ alcohol dehydrogenase. Triphosphopyri lane, was kept refrigerated at all times and was S dine nucleotide, assaying 40 per cent pure by the freshly prepared each day of use. Sufficient co Zwischenferment assay (32), was prepared by the enzyme A is present in this extract so that no method of LePage and Mueller (11). further additions are required. Condensing enzyme.—Ofall the reactions of the Since only small quantities of some of the mate cycle, the one least understood until quite recently rials were available, only a few assays were per is the condensation leading to formation of the 6- formed. However, the data, given in Table 1, con carbon acid. Recent studies have clarified this process, however (16, 26, 29), and the reaction can TABLE 1 now be formulated, according to Stern and Ochoa CONDENSING ENZYME ASSAY (28), as follows: Thecomponentsoftbe auaysystemwere: Mphosphatebuffer, pH 7, 0.025 nil.; 0.08 K MgCI*, 0.05 ml.; 0.2 N cysteine (neutral. @ Acetyl-Coenzyme A + óxalacetate —+ ised), 0.05 nil.; 0.14 oxalacetic acid, 0.05 ml.; 0.1 synthetic I\ acetyl phosphate. 0.i nil.; E. Coli extract, 0.20 ml.; acetone pow. citrate + Coenzyme A. ‘%I) der extract of the 1@1hue and water to make a total volume of 1.00 ml. After incubation in small test tubes for 10 minutes at 25°the An impure concentrate of acetyl-CoA has been reactionlwas stopped by adding trichloroacetic acid to a final oon. ceutration of 5 per cent. An aliquot of the supernatant solution obtained by Lynen and Reichart (12); and Ochoa was removed for citric acid determination according to Natelaon and co-workers1 have found that this substance St of. (15). can condense with oxalacetate to yield citrate in pM citrate produced the presence of the crystalline condensing enzyme. Tissue 10 znin.X 100 mg. acetone powder For assay purposes the acetyl-CoA may be gener Normal mouse liver 1.63 ated in situ, either by an acetate-activating factor Mouse mammary carcinoma 8.30 Mouse hepatoma 2.90 which, according to the originalprocedure of Stern Mouse rhabdomyosarcoma 1.45 and Ochoa (27), catalyzes the formation of acetyl CoA from acetate, CoA and ATP; or, more con vincingly demonstrate the presence of the con veniently, by means of the following reaction densing enzyme in three mouse tumors in amounts catalyzed by a transacetylating enzyme present in at least as high as in mouse liver. The activities of E. Coli (26): these neoplastic tissues were of the same order as E. Ccli pigeon liver, reported by Stern and Ochoa (26), Acetyl phosphate + CoA —- Acetyl-CoA + and were of a magnitude similar to that obtained phosphate. (2) by these investigators for other normal tissues The latter procedure was used in the present (29). study. According to equation (3), representing a Aconilase and fumarase.—For assay of the summation of equations (1) and (2), citric acid, hydrases, advantage was taken of the recent spec trophotometric method described by Racker (21). Acetyl phosphate + (@oA+ E. Coli extract + With citrate or malate as the substrate, aconitase (conden4ng enzwn@) (3) or fumarase activity is measured by the appear oxalacetate -)@citrate + CoA + phosphate, ance of absorption at 240 m@&ofthe corresponding is formed in the presence of the condensing en unsaturated acids, cis-aconitic or fumaric. The zyme and E. Coli extract from a mixture of Acetyl test system contained, in a total volume of 3 ml., phosphate, coenzyme A, and oxalacetate. The 0.05 Mphosphate buffer, pH 7.4, an aliquot of the E. Coliextract was prepared,accordingto direc tissue, and the substrate. For aconitase assay the tions of Drs. Stern and Ochoa,2 from lyophilized enzyme was prepared by homogenizing the fresh cells supplied by these investigators. Cells (0.5 tissue with 20 volumes of 0.1 M phosphate buffer, pH 7.4, and centrifuging off the residue at 3,000 1 Private communication. r.p.m. Fumarase was assayed in an extract of an 2 We aregreatly indebtedto theseinvestigators for generous gifts of acetylphosphate, lyophilised E. Ccli, and details of the acetone powder prepared as described in the con condensing enzyme assay prior to publication. densing enzyme assay. The reactions were carried Downloaded from cancerres.aacrjournals.org on September 29, 2021. © 1952 American Association for Cancer Research. 46 Cancer Research out in quartz absorption cells, with the use of the The reactions were carried out in quartz micro Beckman DU spectrophotometer.
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