Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
Tytuł artykułu

Serum glycoproteins in diabetic and non-diabetic patients with and without cataract

Wybrane pełne teksty z tego czasopisma
Warianty tytułu
Języki publikacji
This study describes the changes in serum glycoproteins from type 2 diabetic and non-diabetic patients with and without cataract. A total of 85 subjects were selected for the study and divided into four groups. The first group consisted of 21 healthy subjects, the second group consisted of 21 diabetic patients with no chronic complications, the third group consisted of 20 diabetic patients with cataract, and the fourth group had 23 non-diabetic patients with age related cataract. The patients with and without cataract were selected on clinical grounds from the Ziauddin University and Jinnah Postgraduate Medical Centre in Karachi, Pakistan. As expected diabetic patients with and without cataract had significantly higher levels of fasting plasma glucose, glycated haemoglobin, glycated plasma proteins and serum fructosamine. In addition to these parameters, the levels of hexosamine, sialic acid and serum total protein were higher in diabetic compared to non-diabetic subjects with age related cataract and healthy subjects. Analysis of the protein fractions showed that alpha-1-globulins and alpha-2-globulins were higher in diabetic patients without complications compared to non-diabetic subjects with age related cataract and healthy subjects. Serum alpha-1-globulin, alpha-2-globulin, beta globulins and gamma globulins were all significantly higher in diabetic patients with cataract compared to healthy subjects but not serum albumin. In conclusion, the levels of beta globulins and gamma globulins were significantly higher in diabetic patients with cataract and non-diabetic age related patients with cataract compared to healthy subjects. Thus, mechanisms other than hyperglycaemia are responsible for the development of cataract in these patients.
Opis fizyczny
Bibliogr. 29 poz.,
  • Department of Biochemistry, Ziauddin University, Shah rah-e- Ghalib, Clifton, Karachi-75600, Pakistan
  • [1] NATHAN D.M., Long-term complications of diabetes mellitus, New England Journal of Medicine 328(23), 1993, pp. 1676–85.
  • [2] ALBERTI K.G.M.M., ZIMMET P.Z., Defination, diagnosis and classification of diabetes mellitus and its complication. Part 1: diagnosis and classification of diabetes mellitus provisional report of a WHO consultation, Diabetic Medicine 15(7), 1998, pp. 539–53.
  • [3] SHERA A.S., RAFIQUE G., KHAWAJA I.A., ARA J., BAQAI S., KING H., Pakistan national diabetes survey: prevalence of glucose intolerance and associated factors in Shikarpur, Sindh Province, Diabetic Medicine 12(12), 1995, pp. 1116–21.
  • [4] The world health report 1998: life in the 21st century: a vision for all, World Health Organization, 1998.
  • [5] BLOEMENDAL H., DE JONG W., JAENICKE R., LUBSEN N.H., SLINGSBY C., TARDIEU A., Ageing and vision: structure, stability and function of lens crystallins, Progress in Biophysics and Molecular Biology 86(3), 2004, pp. 407–85.
  • [6] HORWITZ J., The function of -crystallin in vision, Seminars in Cell and Developmental Biology 11(1), 2000, pp. 53–60.
  • [7] MACRAE T.H., Structure and function of small heat shock/-crystallin proteins: established concepts and emerging ideas, Cellular and Molecular Life Sciences 57(6), 2000, pp. 899–913.
  • [8] MONNIER V.M., STEVENS V.J., CERAMI A., Nonenzymatic glycosylation, sulfhydryl oxidation and aggregation of lens proteins in experimental sugar cataracts, Journal of Experimental Medicine 150(5), 1979, pp. 1098–107.
  • [9] MONNIER V.M., Nonenzymatic glycosylation, the maillard reaction and the aging process, Journal of Gerontology 45(4), 1990, pp. B105–11.
  • [10] RAHMAN M.A., ZAFAR G., SHERA A.S., Changes in glycosylated proteins in log-term complications of diabetes mellitus, Biomedicine and Pharmacotherapy 44(4), 1990, pp. 229–34.
  • [11] GABIR M.M., ROUMAIN J., HANSON R.L., BENNETT P.H., DABELEA D., KNOWLER W.C., IMPERATORE G., The 1997 American Diabetes Association and 1999 World Health Organization criteria for hyperglycemia in the diagnosis and prediction of diabetes, Diabetes Care 23(8), 2000, pp. 1108–12.
  • [12] TIETZ N.W., Clinical Guide to Laboratory Tests, 3rd Ed., WB. Saunders Company, Philadelphia, PA, 1995, pp. 268–73.
  • [13] ROCHMAN H., Hemoglobin A1C and diabetes mellitus, Annals of Clinical and Laboratory Science 10(2), 1980, pp. 111–5.
  • [14] CESSI C., PILIEGOF., The determination of amino sugars in the presence of amino acids and glucose, Biochemical Journal 77, 1960, pp. 508–10.
  • [15] VARLEY H., GOWENLOCK A.H., BELL M., Practical Clinical Biochemistry, 5th Ed., William Heinemann Medical Books Ltd, London, 1980, pp. 545–7.
  • [16] NATELSON S., Microtechniques of Clinical Chemistry for the Routine Laboratory, 2nd Ed., Thomas Springfield, Illinois, 1961, pp. 378–80.
  • [17] MA A., NAUGHTON M.A., CAMERON D.P., Glycosylated plasma proteins: a simple method for the elimination of interference by glucose in its estimation, Clinica Chimica Acta 115(2), 1981, pp. 111–7.
  • [18] RALLI E.P., BARBOSA X., BECK E.M., LAKEN B., Serum electrophoretic patterns in normal and diabetic subjects, Metabolism 6(4), 1957, pp. 331–8.
  • [19] MCLELLAN A.C., THORNALLEY P.J., BENN J., SONKSEN P.H., Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications, Clinical Science 87(1), 1994, pp. 21–9.
  • [20] THORNALLEY P.J., The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life, Biochemical Journal 269(1), 1990, pp. 1–11.
  • [21] BROWNLEE M., CERAMI A., VLASSARA H., Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications, The New England Journal of Medicine 318(20), 1988, pp. 1315–21.
  • [22] SKEIE S., THUE G., SANDBERG S., Interpretation of hemoglobin A1C (HbA1C) values among diabetic patients: Implications for quality specifications for HbA1C, Clincal Chemistry 47(7), 2001, pp. 1212–7.
  • [23] STRATTON I.M., ADLER A.I., NEIL H.A., MATTHEWS D.R., MANLEY S.E., CULL C.A., HADDEN D., TURNER R.C., HOLMAN R.R., Association of glycaemia with macrovascular and microvascular complication of type 2 diabetes (UKPDS 35): prospective observational study, BMJ 321(7258), 2000, pp. 405–12.
  • [24] CROOK M., The determination of plasma or serum sialic acid, Clinical Biochemistry 26(1), 1993, pp. 31–8.
  • [25] MARSHALL S., BACOTE V., TRAXINGER R.R., Discovery of a metabolic pathway mediating glucose induced desensitization of the glucose transport system: Role of hexosamine biosynthesis in the induction of insulin resistance, Journal of Biological Chemistry 266(8), 1991, pp. 4706–12.
  • [26] HANGLOO V.K., KAUL I., ZARGARH.U., Serum sialic acid levels in healthy individuals, Journal of Postgraduate Medicine 36(3), 1990, pp. 140–2.
  • [27] LINDBERG G., EKLUND G.A., GULLBERG B., RASTAM L., Serum sialic acid concentration and cardiovascular mortality, BMJ 302(6769), 1991, pp. 143– 6.
  • [28] SPAN P.N., POUWELS M.J., OLTHAAR A.J., BOSCH R.R., HERMUS A.R., SWEEP C.G., Assay for hexosamine pathway intermediates (uridine diphosphate-N-acetyl amino sugars) in small samples of human muscle tissue, Clinical Chemistry 47(5), 2001, pp. 944–6.
  • [29] HAWKINS M., BARZILAI N., LIU R., HU M., CHEN W., ROSSETTI L., Role of the glucosamine pathway in fat-induced insulin resistance, Journal of Clinical Investigation 99(9), 1997, pp. 2173–82.
Typ dokumentu
Identyfikator YADDA
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.