Ukr.Biochem.J. 2014; Том 86, №6, листопад-грудень, c. 39-49

doi: http://dx.doi.org/10.15407/ubj86.06.039

Ідентифікація ензимів гідролізу тіамінмонофосфату в печінці курей

12.03.2016   Без категорії   No comments

І. К. Колос, О. Ф. Макарчиков

Гродненський державний аграрний університет;
Інститут біохімії біологічно активних сполук НАН Білорусі, Гродно;
e-mail: a_makarchikov@yahoo.com

У тварин тіамінмонофосфат (TMP) є інтермедіатом на шляху деградації коензимної форми вітаміну В1 – тіаміндифосфату. Натепер ензими, що беруть участь у метаболізмі TMP в тканинах тварин, не ідентифіковані. Мета роботи полягала в дослідженні гідролізу TMP в печінці курей. В гомогенаті печінки виявлені два ензими з активністю TMPази – розчинний, що виявляє рН-оптимум в кислому середовищі (рН 6,0), і мембранозв’язаний, активність якого максимальна при рН 9,0. Мембранозв’язана фосфатаза активується в 1,7 раза в присутності 5 мМ Mg2+. Уявна Km цього ензиму для TMP, розрахована в координатах Хейнса, становить 0,6 мМ. Левамізол інгібує мембранну TMPазу за безконкурентним шляхом з Ki = 53 мкМ. Активність розчинного ензиму не залежить від іонів Mg2+ і не інгібується левамізолом, уявна Km для TMP дорівнює 0,7 мМ. За даними гель-фільтрації на колонці з тойоперлом HW-55 молекулярна маса розчинної TMPази становить 17,8 кДа, при цьому пік активності TMPази збігається з піками флавінмононуклеотид- і п-нітрофенілфосфатазної активності. Одер­жані результати вказують на те, що TMP є фізіологічним субстратом низькомолекулярної кислої фосфатази, відомої також як низькомолекулярна протеїн-фосфотирозин-фосфатаза. Гідроліз TMP, який спостерігається в гомогенаті печінки курей за лужних рН, обумовлено дією лужної фосфатази.

Ключові слова: , , , , ,

Посилання:

  1. Makarchikov AF. Thiamine triphosphate: a new view on non-coenzyme function of vitamin B1. Mn: Belorusskaya nauka, 2008. 433 p. (in Russian).
  2. Bettendorff L, Wins P. Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors. FEBS J. 2009 Jun;276(11):2917-25. Review. PubMed, CrossRef
  3. Spenser ID, White RL. Biosynthesis of vitamin B1 (thiamin): an instance of biochemical diversity. Angew Chem Int Ed Engl. 1997 May;36(10):1032-46. CrossRef
  4. Vovk AI, Babiy LV, Murav’eva IV. Relative reactivity of thiamine monophosphate and thiamine diphosphate upon interaction with alkaline phosphatase. Ukr Biokhim Zhurn. 2002 Jan-Feb;74(1):93-6. Russian. PubMed
  5. Zylka MJ, Sowa NA, Taylor-Blake B, Twomey MA, Herrala A, Voikar V, Vihko P. Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine. Neuron. 2008 Oct 9;60(1):111-22. PubMed, PubMedCentral, CrossRef
  6. Ogawa K, Sakai M, Inomata K. Recent findings on ultracytochemistry of thiamin phosphatases. Ann N Y Acad Sci. 1982 Mar;378(1):188-214. Review. PubMed, CrossRef
  7. Knyihár-Csillik E, Bezzegh A, Böti S, Csillik B. Thiamine monophosphatase: a genuine marker for transganglionic regulation of primary sensory neurons. J Histochem Cytochem. 1986 Mar;34(3):363-71. PubMed, CrossRef
  8. Taylor-Blake B, Zylka MJ. Prostatic acid phosphatase is expressed in peptidergic and nonpeptidergic nociceptive neurons of mice and rats. PLoS One. 2010 Jan 13;5(1):e8674. PubMed, PubMedCentral, CrossRef
  9. Silverman JD, Kruger L. Acid phosphatase as a selective marker for a class of small sensory ganglion cells in several mammals: spinal cord distribution, histochemical properties, and relation to fluoride-resistant acid phosphatase (FRAP) of rodents. Somatosens Res. 1988;5(3):219-46. Review. PubMed, CrossRef
  10. Lanzetta PA, Alvarez LJ, Reinach PS, Candia OA. An improved assay for nanomole amounts of inorganic phosphate. Anal Biochem. 1979 Nov 15;100(1):95-7. PubMed, CrossRef
  11.  Sapru MK, Geetha H, Shetty KT. A single reagent method of phosphate estimation in phosphatase(s) assay. Indian J Biochem Biophys. 1987 Dec;24(6):340-3. PubMed
  12. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72(1-2):248-54. PubMed, CrossRef
  13. Kiessling K. H. Thiamine phosphatases in liver, kidney, and brain of the rat. Acta Chem. Scand. 1960;14:1669-70. CrossRef
  14. Scopes R. Protein Purification: Principles and Practice. Springer, 1994. 380 p. CrossRef
  15. McComb R. B., Bowers G. N. Jr., Posen S. Alkaline phosphatase. New York: Plenum, 1979. 986 p. CrossRef
  16. Millán JL. Alkaline Phosphatases : Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes. Purinergic Signal. 2006 Jun;2(2):335-41. Epub 2006 Jun 17. PubMed, PubMedCentral, CrossRef
  17. Zimmermann H, Zebisch M, Sträter N. Cellular function and molecular structure of ecto-nucleotidases. Purinergic Signal. 2012 Sep;8(3):437-502. Epub 2012 May 4. Review. PubMed, PubMedCentral, CrossRef
  18. Neal M J. Medical Pharmacology at a Glance. Wiley-Blackwell, 2012. 115 p.
  19. McDougall K, Plumb C, King WA, Hahnel A. Inhibitor profiles of alkaline phosphatases in bovine preattachment embryos and adult tissues. J Histochem Cytochem. 2002 Mar;50(3):415-22. PubMed, CrossRef
  20. Van Belle H. Kinetics and inhibition of alkaline phosphatases from canine tissues. Biochim Biophys Acta. 1972 Nov 10;289(1):158-68. PubMed, CrossRef
  21. Goldstein DJ, Rogers CE, Harris H. Expression of alkaline phosphatase loci in mammalian tissues. Proc Natl Acad Sci U S A. 1980 May;77(5):2857-60. PubMed, PubMedCentral, CrossRef
  22. Goldstein DJ, Rogers C, Harris H. Evolution of alkaline phosphatases in primates. Proc Natl Acad Sci U S A. 1982 Feb;79(3):879-83. PubMed, PubMedCentral, CrossRef
  23. Delomenède M, Buchet R, Mebarek S. Lansoprazole is an uncompetitive inhibitor of tissue-nonspecific alkaline phosphatase. Acta Biochim Pol. 2009;56(2):301-5. Epub 2009 Jun 18. PubMed
  24. Krupyanko V. I. A vector method for representation of enzyme reactions. M.: Nauka, 1990. 144 p. (in Russian).
  25. Cyboron GW, Wuthier RE. Purification and initial characterization of intrinsic membrane-bound alkaline phosphatase from chicken epiphyseal cartilage. J Biol Chem. 1981 Jul 25;256(14):7262-8. PubMed
  26. Khodaparast-Sharifi SH, Snow LD. Levamisole inhibition of alkaline phosphatase and 5′-nucleotidase of bovine milk fat globule membranes. Int J Biochem. 1989 Jan;21(4):401-5. PubMed, CrossRef
  27. Kozlenkov A, Le Du MH, Cuniasse P, Ny T, Hoylaerts MF, Millán JL. Residues determining the binding specificity of uncompetitive inhibitors to tissue-nonspecific alkaline phosphatase. J Bone Miner Res. 2004 Nov;19(11):1862-72. Epub 2004 Jun 28. PubMed, CrossRef
  28. Wang H, Gilles-Baillien M. Alkaline phosphatase and ATPases in brush-border membranes of rat jejunum: distinct effects of divalent cations and of some inhibitors. Arch Physiol Biochim. 1992 May-Jun;100(3):289-94. PubMed, CrossRef
  29. Dean RL. Kinetic studies with alkaline phosphatase in the presence and absence of inhibitors and divalent cations. Biochem Mol Biol Educ. 2002;3(6):401-7. CrossRef
  30. Hiwada K, Wachsmuth ED. Catalytic properties of alkaline phosphatase from pig kidney. Biochem J. 1974 Jul;141(1):283-91. PubMed, PubMedCentral, CrossRef
  31. Cathala G, Brunel C. Bovine kidney alkaline phosphatase. Purification, subunit structure, and metalloenzyme properties. J Biol Chem. 1975 Aug 10;250(15):6040-5. PubMed
  32. Stec B, Holtz KM, Kantrowitz ER. A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J Mol Biol. 2000 Jun 23;299(5):1303-11. PubMed, CrossRef
  33. Leone FA, Ciancaglini P, Pizauro JM. Effect of calcium ions on rat osseous plate alkaline phosphatase activity. J Inorg Biochem. 1997 Nov 1;68(2):123-7. PubMed, CrossRef
  34. Rindi G, Ricci V, Gastaldi G, Patrini C. Intestinal alkaline phosphatase can transphosphorylate thiamin to thiamin monophosphate during intestinal transport in the rat. Arch Physiol Biochem. 1995 Apr;103(1):33-8. PubMed, CrossRef
  35. Goldfarb DA, Stein BS, Shamszadeh M, Petersen RO. Age-related changes in tissue levels of prostatic acid phosphatase and prostate specific antigen. J Urol. 1986 Dec;136(6):1266-9. PubMed
  36. Rönnberg L, Vihko P, Sajanti E, Vihko R. Clomiphene citrate administration to normogonadotropic subfertile men: blood hormone changes and activation of acid phosphatase in seminal fluid. Int J Androl. 1981 Jun;4(1-6):372-8. PubMed, CrossRef
  37. Muniyan S, Chaturvedi NK, Dwyer JG, Lagrange CA, Chaney WG, Lin MF. Human prostatic Acid phosphatase: structure, function and regulation. Int J Mol Sci. 2013 May 21;14(5):10438-64. PubMed, PubMedCentral, CrossRef
  38. Quintero IB, Araujo CL, Pulkka AE, Wirkkala RS, Herrala AM, Eskelinen EL, Jokitalo E, Hellström PA, Tuominen HJ, Hirvikoski PP, Vihko PT. Prostatic acid phosphatase is not a prostate specific target. Cancer Res. 2007 Jul 15;67(14):6549-54. PubMed, CrossRef
  39. Graddis TJ, McMahan CJ, Tamman J, Page KJ, Trager JB. Prostatic acid phosphatase expression in human tissues. Int J Clin Exp Pathol. 2011 Mar;4(3):295-306. Epub 2011 Mar 22. PubMed, PubMedCentral
  40. Laforenza U, Patrini C, Rindi G. Distribution of thiamine, thiamine phosphates, and thiamine metabolizing enzymes in neuronal and glial cell enriched fractions of rat brain. J Neurochem. 1988 Sep;51(3):730-5. PubMed, CrossRef
  41. Bull H, Murray PG, Thomas D, Fraser AM, Nelson PN. Acid phosphatases. Mol Pathol. 2002 Apr;55(2):65-72. Review. PubMed, PubMedCentral, CrossRef
  42. Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS. Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. PubMed, CrossRef
  43. Pohlmann R, Krentler C, Schmidt B, Schröder W, Lorkowski G, Culley J, Mersmann G, Geier C, Waheed A, Gottschalk S. Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. EMBO J. 1988 Aug;7(8):2343-50. PubMed, PubMedCentral
  44. Wo YY, McCormack AL, Shabanowitz J, Hunt DF, Davis JP, Mitchell GL, Van Etten RL. Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase. J Biol Chem. 1992 May 25;267(15):10856-65. PubMed
  45. Bryson GL, Massa H, Trask BJ, Van Etten RL. Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1. Genomics. 1995 Nov 20;30(2):133-40. PubMed, CrossRef
  46. Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM. Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93.  PubMed, CrossRef
  47. Hayman AR, Bune AJ, Bradley JR, Rashbass J, Cox TM. Osteoclastic tartrate-resistant acid phosphatase (Acp 5): its localization to dendritic cells and diverse murine tissues. J Histochem Cytochem. 2000 Feb;48(2):219-27. PubMed, CrossRef
  48. Schindelmeiser J, Münstermann D. Immuno­histochemical characterization of purple acid phosphatase-containing leucocytes in the human placenta. Histochem J. 1991 Jan;23(1):38-42. PubMed, CrossRef
  49. Drexler HG, Gignac SM. Characterization and expression of tartrate-resistant acid phosphatase (TRAP) in hematopoietic cells. Leukemia. 1994 Mar;8(3):359-68. Review. PubMed
  50. Haider S., Naz R., Khan A. R., Saeed A. Acid phosphatases in chicken’s liver. J. Chem. Soc. Pak. 1993;15:64-71.
  51. de Araujo PS, Mies V, Miranda O. Subcellular distribution of low- and high-molecular-weight acid phosphatases. Biochim Biophys Acta. 1976 Nov 8;452(1):121-30. PubMed, CrossRef
  52. Panara F, Mileti A. Subcellular localization of high- and low-molecular weight acid phosphatases from chicken liver. Int J Biochem. 1986 Jan;18(11):1057-9. PubMed, CrossRef
  53. Helwig JJ, Farooqui AA, Bollack C, Mandel P. Purification and some properties of tartrate-sensitive acid phosphatase from rabbit kidney cortex. Biochem J. 1978 Oct 1;175(1):321-9. PubMed, PubMedCentral, CrossRef
  54. Fujimoto S, Urata Y, Nakagawa T, Ohara A. Characterization of intermediate-molecular-weight acid phosphatase from bovine kidney cortex. J Biochem. 1984 Oct;96(4):1079-88. PubMed
  55. Siddiqua A, Rehmat M, Saeed A, Amin S, Naz R, Sherazi M, Khan GM, Saeed A. Acid phosphatases from the liver of Labeo rohita: purification and characterization.
    Biol Pharm Bull. 2008 May;31(5):802-8. PubMed, CrossRef
  56. Taga EM, Van Etten RL. Human liver acid phosphatases: purification and properties of a low-molecular-weight isoenzyme.  Arch Biochem Biophys. 1982 Apr 1;214(2):505-15. PubMed, CrossRef
  57. Chernoff J, Li HC. A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase.
    Arch Biochem Biophys. 1985 Jul;240(1):135-45. PubMed, CrossRef
  58. Boivin P, Galand C. The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3.
    Biochem Biophys Res Commun. 1986 Jan 29;134(2):557-64. PubMed, CrossRef
  59. Bottini N, Bottini E, Gloria-Bottini F, Mustelin T. Low-molecular-weight protein tyrosine phosphatase and human disease: in search of biochemical mechanisms. Arch Immunol Ther Exp (Warsz). 2002;50(2):95-104. Review. PubMed
Creative CommonsThis work is licensed under a Creative Commons Attribution 4.0 International License.