Evaluation of Erythrocyte G6PD Activity Unit; It is Better Defined as a Function of RBC Count


Abstract views: 28 / PDF downloads: 36

Authors

  • Necat Yılmaz Department of Biochemistry and Clinical Biochemistry, Faculty of Medicine, University of Gaziantep, Turkey
  • Ayşe Binnur Erbağcı Department of Biochemistry and Clinical Biochemistry, Faculty of Medicine, University of Gaziantep, Turkey

DOI:

https://doi.org/10.58600/eurjther.1999-10-1-2-1520-arch

Keywords:

Erythrocyte G6PD, RBC, hemoglobin, MCV

Abstract

Glucose 6-phosphate dehydrogenase (G6PD) deficiency, one of the most common red celi abnormalities, is characterized by wide clinical, biochemical and molecular heterogeneity. in clinical laboratories erythrocyte ·G6PD activity is defined either as a function of hemoglobin (Hb) concentration or red blood celi (RBC) count and seldom hematocrit (Hct). These parameters are variable tor every individual and misinterpretation of the results cannot be avoided with reference interval establishment studies unless the best approach that define erythrocyte G6PD activity is selected. Hb concentration is frequently prone to the effects of genetic, physiological and environmental factors where G6PD activity should correlate with RBC count even when it is altered. in this study relations of the erythrocyte G6PD activity with RBC count, Hb concentration of the erythrocyte suspensions and RBC indices of 242 individuals were studied. Additionally, relations with platelet and white blood celi (WBC) counts were evaluated to determine possible interference. Erythrocyte G6PD activity was determined with kinetic spectrophotometric method according to the ICSH at 3o0 c. RBC, WBC, platelet counts, hemoglobin concentration of the erythrocyte suspensions and erythrocyte indices were determined with an automatic complete blood counter. Enzyme activity was correlated with RBC count (r: 0.53, p<0.001), there was no correlation with Hb (p>0.05). The negative correlation of the enzyme activity with MCV and MCH (r: -0.44 and r: -0.29, p<0.001 ), disappeared as a ratio of RBC count (p>0.05) and strengthened as a ratio of Hb concentration (r: -0.61 and r: -0.44, p<0.001 ). in this study a correlation of erythrocyte suspentions' platelet, leucocyte count and the enzyme activity as a ratio of Hb (r: 0.33 and r: 0.25, p<0.001) was observed. On the other hand enzyme activity as a ratio of RBC was only poorly correlated to WBC count (r: 0.15, p<0.01 ). Results of this study indicate that erythrocyte G6PD activity is related to RBC count and has several advantages over Hb in assessing G6PD status. it gives more reliable results in conditions that could affect erythrocyte morphology and Hb concentration.

Metrics

Metrics Loading ...

References

Naylor CE, Rowland P, Basak AK, Gover S, Mason PJ, Bautista JM, et al. Glucose 6- phosphate dehydrogenase mutations causing enzyme deficiency in a model of the tertiary structure of the human enzyme. Blood 1996; 87:2974-2982.

Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HR. Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood 1996; 87:1595-1599.

Martinez Cayuela M. Oxygen free radicals and human disease. Biochimie 1995; 77:147-161. 4. Nelson DA, Davey FR. Erythrocytic disorders. in: Henry JB (ed). Clinical Diagnosis and Management by Laboratory Methods (18th ed). Philadelphia, WB Saunders, 1991: 660-662.

Lehninger AL, Nelson DL, Cox MM. Principles of Biochemistry (2nd ed). New York, Worth Publishers, 1993: 436-437.

Luzzatto L, Mehta A. Glucose 6-phosphate dehydrogenase deficiency. in: Scriver CR, Beaudet AL, Siy WS, Valle D (eds). The metabolic and molecular bases of inherited disease ( ed). USA, 1995: 3367-3398.

Yüreğir GT, Aksoy K, Arpacı A, Ünlükurt İ, Tuli A. Studies on red celi glucose 6-phosphate dehydrogenase: evaluation of reference values. Ann Clin Biochem 1994; 31:50-55.

Luzzatto L. Investigation of hereditary haemolytic anaemias: membrane and enzyme abnormalities. in: Dacia JV, Lewis SM (eds). Practical Haematology (fh ed). Singapore, Longman Publishers, 1993: 204-214.

Scopes DA, Bautista JM, Naylor CE, Adams MJ, Mason PJ. Amino acid substitutions at the dimer interface of human glucose 6-phosphate dehydrogenase that increase thermostability and reduce the stabilising effect of NADPH. Eur J Biochem 1998; 251:382-388.

Bauer JD. Clinical Laboratory Methods (9th ed). USA, C V Mosby Company, 1982: 96-100, 220-221.

Fairbanks VF, Klee GG. Biocheınical aspects of hematology. In: Burtis CA, Ashwood ER (eds). Tietz Textbook of Clinical Chemistry (2nd ed). Philadelphia, WB Saunders Company, 1994: 1977-1986.

Löhr GW, Waller HD. Glucose 6 Phosphate Dehydrogenase. In: Bergmeyer HU (ed). Methods of Enzymatic Analysis. New York and London, 1974: 636.

Travis SF, Kumar SP, Paez PC, DelivoriaPapadopoulos M. Red cell metabolic alterations in postnatal life in term infants: glycolytic enzymes and glucose 6-phosphate dehydrogenase. Pediatr Res 1980; 14:1349-1352.

Vetrella M, Barthelman W: Enzyme activities in the erythrocytes of human fetuses. Z Kinderheilk 1971; 110: 99-103.

Kahn SE, Jandreski MA. Laboratory Statistics. In: Kaplan LA, Pesce AJ, (eds). Clinical Chemistry Theory, Analysis, Correlation (3rd ed). USA, Mosby Company 1996: 342-364.

Kingle O. Statistical procedures. In: Burtis CA, Ashwood ER (eds). Tietz Textbook of Clinical Chemistry (2nd ed). Phiadelphia, 1994:384-484.

Martini G, Ursini MW. A new lease of life for an old enzyme. Bioassays 1996; 18:631-637.

Tian WN, Braunstein LD, Phang J, Stuhlmeier KM, Xi OC, Tian X, et al. Importance of glucose-6-phosphate dehydrogenase activity for celi growth. J Biol Chem 1998; 273:10609- 10617.

Devi GS, Prasad MH, Reddy PP, Rao DN. Leukocyte glucose 6-phosphate dehydrogenase as a prognostic indicator in children with acute lymphocytic leukemia. Indian J Exp Biol 1997; 33:829-832.

Devi GS, Prasad MH, Reddy PP, Rao DN. Leukocyte glucose 6-phosphate dehydrogenase as a prognostic indicator in ANLL and CML. lndian J Exp Biol 1997; 35:155-158.

Cocco P, Todde P, Fornera S, Manca MB, Manca P, Sias AR. Mortality in a cohort of men expressing the glucose-6-phosphate dehydrogenase defıciency. Blood 1998; 91 :706-709.

Adediran SA. Kinetic and thermodynamic properties of two electrophoretically similar genetic variants of human erythrocyte glucose-6- phosphate dehydrogenase. Biochimie 1996; 78:165-170.

Beutler E, Kuhl W, Gelbart T, · Forman L. DNA sequence abnormalities of human glucose - 6- phosphate dehydrogenase variants. The Journal of Biological Chemistry 1991; 226:4145-4150.

Luzzatto L. Genetic heterogeneity and pathophysiology of G6PD deficiency. British Journal of Haematology 1974; 28:151-154.

Morelli A, Benatti U, Geatani GF, De Flora A. Biochemical mechanisms of glucose 6- phosphate dehydrogenase deficiency. Proc Natl Acad Sci 1978; 75:1979-1983.

Hodge DL, Salati LM. Nutritional regulation of the Glucose 6-phosphate dehydrogenase (G6PD) gene mediated by a nuclear posttranscriptional mechanism. Arch Biochem Biophys 1997; 348:303-312.

Spolarics Z. Endotoxemia, pentose cycle, and the oxidant/antioxidant balance in the hepatic sinusoid. J Leukoc Biol 1998; 63 :534-541.

De Flora A, Morelli A, Benatti U. Entrapment of normal and mutant glucose 6- phosphate dehydrogenase (G6PD) within G6PD deficient erythrocytes. Biblthca Haemat 1985; 51 :50-56.

Mamlock MR, Mills GC, Goldblum RM. Glucose 6-phosphate dehydrogenase Beaumont: A new variant with severe enzyme deficiency and CNSHA. Enzyme 1985; 34:15-21.

Downloads

Published

1999-01-01

How to Cite

Yılmaz, N., & Erbağcı, A. B. (1999). Evaluation of Erythrocyte G6PD Activity Unit; It is Better Defined as a Function of RBC Count. European Journal of Therapeutics, 10(1, 2), 58–63. https://doi.org/10.58600/eurjther.1999-10-1-2-1520-arch

Issue

Section

Review Articles