Advertisement
Research Article| Volume 78, ISSUE 2, P245-254, August 1971

Oxalate and glycolate synthesis by hemic cells

  • Lloyd H. Smith Jr.
    Correspondence
    Reprint requests: Dr. Lloyd H. Smith, Jr., Department of Medicine School of Medicine, University of California at San Francisco, San Francisco, Calif. 94122.
    Affiliations
    From the Department of Medicine, School of Medicine, University of California, San Francisco, Calif., USA

    From the Medical Services, San Francisco General Hospital, San Francisco, Calif., USA
    Search for articles by this author
  • Richard L. Bauer
    Affiliations
    From the Department of Medicine, School of Medicine, University of California, San Francisco, Calif., USA

    From the Medical Services, San Francisco General Hospital, San Francisco, Calif., USA
    Search for articles by this author
  • Hibbard E. Williams
    Affiliations
    From the Department of Medicine, School of Medicine, University of California, San Francisco, Calif., USA

    From the Medical Services, San Francisco General Hospital, San Francisco, Calif., USA
    Search for articles by this author
      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      Oxalate and glycolate were synthesized from 14C-glyoxylate by leukocytes, erythrocytes, and dialyzed hemolysate preparations. Oxalate decarboxylase was used in a convenient and reliable assay of oxalate produced. Leukocytes were approximately 10 to 20 times as active in oxalate and glycolate synthesis, respectively, as erythrocytes. Data submitted to indicate that the erythrocytic enzyme system is lactic dehydrogenase (LDH) include nicotinamide, adenine dinucleotide dependence, pH curve, simultaneous glycolate and oxalate synthesis, inhibition by oxalate and oxamate, and coincidence of isoenzyme activities for lactate and glyoxylate. Coincidence of glyoxylate and lactate oxidation by LDH isoenzymes was also shown in leukocyte preparations. These findings are discussed in terms of the implications of the coupling by LDH of glyoxylate oxidation to oxalate and its reduction to glycolate or the competitive reduction of another substrate. The implications for the development of a pharmacologic inhibitor of oxalate synthesis are also presented.
      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Translational Research
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect

      References

        • Hockaday TDR
        • Frederick EW
        • Clayton JE
        • et al.
        Studies on primary hyperoxaluria. II. Urinary oxalate, glycolate, and glyoxylate measurement by isotope dilution methods.
        J Lab Clin Med. 1965; 65: 677-687
        • Gibbs DA
        • Watts RWE
        The variation of urinary oxalate excretion with age.
        J Lab Clin Med. 1969; 73: 901-908
        • Elder TD
        • Wyngaarden JB
        The biosynthesis and turnover of oxalate in normal and hyperoxaluric subjects.
        J Clin Invest. 1960; 39: 1337-1344
      1. Williams HE, Johnson G, and Smith LH: Unpublished observations.

        • Cattell WR
        • Spencer AG
        • Taylor GW
        • et al.
        The mechanism of the renal excretion of oxalate in the dog.
        Clin Sci. 1962; 22: 43-52
        • Zarembski PM
        • Hodgkinson A
        The renal clearance of oxalic acid in normal subjects and in patients with primary hyperoxaluria.
        Invest Urol. 1963; 1: 87-93
        • Pierce EC
        • Appleman CO
        Role of ether-soluble organic acids in the cation-anion balance in plants.
        Plant Physiol. 1943; 18: 224-238
        • Hockaday TDR
        • Clayton JE
        • Frederick EW
        • et al.
        Primary hyperoxaluria.
        Medicine. 1964; 43: 315-345
        • Williams HE
        • Smith LH
        Primary hyperoxaluria.
        in: Stanbury JB Wyngaarden JB Frederickson DS The metabolic basis of inherited disease. ed. 3. McGraw-Hill Book Co., Inc, New York1971
        • Williams HE
        • Wilson M
        • Smith LH
        Studies on primary hyperoxaluria. III. Transamination reactions of glyoxylate in human tissue preparations.
        J Lab Clin Med. 1967; 70: 494-502
        • Fallon HJ
        • Frei E
        • Davidson JD
        • et al.
        Leukocyte preparations from human blood: evaluation of their morphologic and metabolic state.
        J Lab Clin Med. 1962; 59: 779-791
        • Fisher CL
        • Nixon JC
        The determination of lactate dehydrogenase isoenzymes using the microzone cellulose acetate system.
        Clin Biochem. 1967; 1: 34-41
        • Mayer GG
        • Markow D
        • Karp F
        Enzymatic oxalate determination in urine.
        Clin Chem. 1963; 9: 334-339
        • Cook DA
        • Henderson LM
        The formation of oxalic acid from the side chain of aromatic amino acids in the rat.
        Biochim Biophys Acta. 1969; 184: 404-411
        • Warren WA
        Catalysis of both oxidation and reduction of glyoxylate by pig heart lactate dehydrogenase isozyme 1.
        J Biol Chem. 1970; 245: 1675-1681
        • Fisher V
        • Watts RWE
        The metabolism of glyoxylate in blood from normal subjects and patients with primary hyperoxaluria.
        Clin Sci. 1968; 34: 97-110
        • Novoa WB
        • Winer AD
        • Glaid AJ
        • et al.
        Lactic dehydrogenase. V. Inhibition by oxamate and by oxalate.
        J Biol Chem. 1959; 234: 1143-1148
        • Frederick EW
        • Rabkin MT
        • Smith LH
        Primary hyperoxaluria: a defect in glyoxylate metabolism.
        J Clin Invest. 1962; 41 (Abst.): 1358
        • Vesell ES
        • Bearn AG
        Variations in the lactic dehydrogenase of vertebrate erythrocytes.
        J Gen Physiol. 1962; 45: 553-565
        • Karnovsky ML
        Metabolic basis of phagocytic activity.
        Physiol Rev. 1962; 42: 143-168
        • Nakada HI
        • Weinhouse S
        Studies of glycine oxidation in rat tissues.
        Arch Biochem Biophys. 1953; 42: 257-270
        • Romano M
        • Cerra M
        The action of crystalline lactate dehydrogenase from rabbit muscle on glyoxylate.
        Biochim Biophys Acta. 1969; 177: 421-426
        • Richardson KE
        • Tolbert NE
        Oxidation of glyoxylic acid to oxalic acid by glycolic acid oxidase.
        J Biol Chem. 1961; 236: 1280-1284
        • Williams HE
        • Smith LH
        L-glyceric aciduria: a new genetic variant of primary hyperoxaluria.
        N Engl J Med. 1968; 278: 233-239
        • Williams HE
        • Smith LH
        Hyperoxaluria in L-glyceric aciduria: a possible pathogenic mechanism.
        Science. 1971; 171: 390-391
        • Heck Hd'A
        Porcine heart lactate dehydrogenase: optical rotatory dispersion, thermodynamics, and kinetics of binding reactions.
        J Biol Chem. 1969; 244: 4375-4381
        • Anderson SR
        • Florini JR
        • Vestling CS
        Rat liver lactate dehydrogenase. III. Kinetics and specificity.
        J Biol Chem. 1964; 239: 2991-2997
        • Goldberg EB
        • Nitowsky HM
        • Colowick SP
        The role of glycolysis in the growth of tumor cells. IV. The basis of glucose toxicity in oxamate-treated, cultured cells.
        J Biol Chem. 1965; 240: 2791-2796
        • Coe EL
        • Strunk RC
        The effect of oxamate on glycolysis in intact ascites tumor cells. I. Kinetic evidence for a dual glycolytic system.
        Biochim Biophys Acta. 1970; 208: 189-202
        • Warburg O
        • Gawehn K
        • Geissler AW
        Stoffwechsel der weissen Blutzellen.
        Z Naturforsch. 1958; 13b: 515-516
        • Reynolds VH
        • Fleming JH
        • Richie RE
        • et al.
        Inhibition of lactic dehydrogenase: a new approach to cancer chemotherapy.
        in: 1st edition. Surg Forum. 14. 1963: 128-130