CHANGES IN GLYCOSYLATED PROTEINS IN TYPE-2 DIABETIC PATIENTS WITH AND WITHOUT COMPLICATIONS
AbstractBackground: Diabetes mellitus constitutes one of the most important problems in developing anddeveloped countries. Increased glycosylation of various proteins in diabetic patients has beenreported by many authors. The present study describes the changes in protein glycosylation indiabetic patients with and without diabetic complication. Methods: The study included onehundred and three subjects. Among them 21 were type 2 diabetic patients without any clinicalevidence of chronic diabetic complications, 21 were type 2 diabetic patients with cardiovascularcomplications, 20 were type 2 diabetic patients with cataract, 20 were type 2 diabetic patients withretinopathy and 21 apparently normal, age, sex and weight matched controls. The patients wereselected from Ziauddin Medical University Hospital, Karachi and Jinnah Postgraduate MedicalCentre, Karachi. Results: Fasting plasma glucose was increased in all diabetic patients andcorrelated significantly with glycosylated hemoglobin, glycosylated plasma proteins and serumfructosamine concentrations. There was no significant difference in the levels of fasting plasmaglucose, glycosylated plasma proteins, glycosylated hemoglobin, serum fructosamine, hexosamineor sialic acid between diabetic patients with or without chronic complications. Alpha-1 and alpha-2 globulin fraction were significantly increased in diabetic patients without complications, diabeticpatients with cardiovascular complications and diabetic patients with cataract. Albumin was foundto be decreased in diabetic patients with cataract while gamma globulin was increased in diabeticpatients with cardiovascular complications and diabetic patients with cataract. Conclusions: Inuncomplicated diabetic patients alpha-1 and alpha-2 glycoproteins were increased. In diabeticpatients with cardiovascular complications alpha-1, alpha-2 and gamma globulin were increasedwhile in diabetic patients with cataract alpha-1, alpha-2 and gamma globulin were increased butserum albumin was significantly decreased.Key words: glycosylated hemoglobin, glycosylated plasma protein, serum fructosamine, sialicacid, hexosamine and total serum proteins.
Wilson JD, Braunwald E, Isselbacher KJ, Petersdorf RG,
Martin JB, Facuci AS, et al. Harrison’s “Principles of Internal
Medicine”.12th Edition, New York: McGraw-Hill; 1991. vol:
Alberti KGMM, Zimmet PZ. Defination, diagnosis and
classification of diabetes mellitus and its complication.
Provisional report of WHO consultations. Diabetic Med. 1998;
Shera S. Prevalence and prevention. Diabetes Digest 1998;12:
Ahmed N. Glycation and diabetic complications. J Pak Med
Brownlee M, Vlassara H, Cerami A. Advanced glycosylation
end products in tissue and the biochemical basis of
complications. New Engl J Med 1998;318:1315-21.
Mandarino LJ. Current hypothesis for the biochemical basis of
diabetic retinopathy. Diabetes Care 1992;15: 1892-1900.
Singleton JR, Smith AG, Russell JW, Feldman EL.
Microvascular Complications of Impaired Glucose Tolerance.
Diabetes. 2003;52: 2867-73.
DCCT (diabetes control and complications trial research
group). The effect of intensive treatment of diabetes on the
development and progression of long-term complications of
insulin-dependent diabetes mellitus. N Engl J Med
Forbes JM, Yee LTL, Thallas V, Lassila M, Candido R, Dahm
KAJ, et al. Advanced Glycation End Product Interventions
Reduce Diabetes-Accelerated Atherosclerosis. Diabetes 2004;
Brownlee M. Biochemistry and Molecular Cell Biology of
diabetic complications. Nature. 2001; 414: 813-20.
Spiro RG. Glycoproteins: Structure, Metabolism and Biology.
N Engl J Med. 1963; 269: 616-21.
Khan IA, Rahman MA. Variation of saccharoid fraction in
diabetes mellitus. Nature 1967; 215: 979-80.
Kennedy L, Mehl TD, Elder E, Varghese M, Merimee Tj.
Nonenzymatic glycosylation of serum and plasma proteins.
Johnson RN, Metcalf PA, Baker JR. Fructosamine, a new
approach to the estimation of serum glycosylprotein, an index
of diabetic control. Clin Chim Acta 1982;127:87-95.
Gabir MM, Roumain J, Hanson RL, Bennett PH, Dabelea D,
Knowler WC, et al. The 1997 American Diabetes Association
and 1999 World Health Organization criteria for
hyperglycemia in the diagnosis and prediction of diabetes.
Diabetes Care 2000;23:1108-12.
Cessi C, Pilliego F. The determination of amino sugars in the
presence of amino acids and glucose. Biochem J1960;77:508-
Varley H, Gowenlock AH, Bell M. Biuret method for protein
estimation, in Practical Clinical Biochemistry. 5th edition.
London, William Heinemann Medical Books Ltd. 1980:545-7.
Natelson S. Microtechniques of clinical chemistry for the
routine laboratory. 2nd edition. Charles C. Thomos, Springfield
III, 1961: 378-80.
Ma A, Naughton MA, Cameron DP. Glycosylated plasma
proteins: a simple method for the elimination of interference
by glucose in its estimation. Clin Chim Acta. 1981;115:111-7.
Ralli EP, Barbosa X, Beck EM, Laken B. Serum
electrophoretic patterns in normal and diabetic subjects.
Stratton IM, Adler AI, Neil HA, Mathew DR, Manely SE,
Cull CA, et al. Association of glycemia with macrovascular
and microvascular complication of type 2 diabetes (UKPDS
. Brit Med J 2000;321:405-12.
Mclellan AC, Thornalley PJ, Benn J, Sonksen PH. Glyoxalase
system in clinical diabetes mellitus and correlation with
diabetic complications. Clin Sci 1994;87:21-29.
Rahman MA, Zafar G, Shera AS. Changes in glycosylated
proteins in log-term complications of diabetes mellitus.
Biomed and Pharmacother 1990; 44: 229-34.
Odetti P, Garibaldi S, Noberasco G, Aragno I, Valentini S,
Traverso N, et al. Levels of carbonyl groups in plasma proteins
of type 2 diabetes mellitus subjects. Acta Diabetol
J Ayub Med Coll Abbottabad 2005;17(3)
Mandarino LJ. Current hypothesis for the biochemical basis of
diabetic retinopathy. Diabetes Care. 1992; 15: 1892-1900.
Skeie S, Thue G, Sandberg S. Interpretation of hemoglobin
A1C (HbA1C) values among diabetic patients: Implication for
quality specifications for HbA1C. Clincal Chemistry. 2001; 47:
Malik M, Gill GV, Pugh RN, Bakir A, Hossain M. Can plasma
fructosamine substitute for glycated haemoglobin (HbA1C)
estimation in the assessment of diabetic control? Trop Doct.
; 30: 74-6.
Henricsson M, Gottsater A, JeppssonJO, Fernlund P,
Sundkvist G. The frequency and severity of retinopathy are
related to HbA1C values after, but not at, the diagnosis of
NIDDM. J Intern Med. 1998; 244: 149-54.
Lis H, Sharon N. Protein glycosylation. Structural and
functional aspects. Eur J Biochem. 1993; 218: 1-27.
Yarema KJ, Bertozzi CR. Characterizing glycosylation
pathway. Genome Biology. 2001; 2(5): 1-10.
Matie L. Plasma protein glycosylation and its alteration in
disease. Rom J Intern Med. 1997; 35: 3-11.
Opdenakker G, Rudd PM, Ponting CP, Dwek RA. Concepts
and principles of glycobiology . FASEB J 1993; 7: 1330-7.
Davis BJ. Synthesis of glycoproteins. Chem Rev, 2002; 102:
Frankl WS. Glycoproteins in diabetes mellitus and
atherosclerosis. Am J Med Sci. 1964; 248: 588-94.
Berkman J, Rifkin H, Ross G. The serum polysaccharides in
diabetic patients with and without degenerative vascular
disease. J Clin Invest. 1953; 32: 415-21.
Journal of Ayub Medical College, Abbottabad is an OPEN ACCESS JOURNAL which means that all content is FREELY available without charge to all users whether registered with the journal or not. The work published by J Ayub Med Coll Abbottabad is licensed and distributed under the creative commons License CC BY ND Attribution-NoDerivs. Material printed in this journal is OPEN to access, and are FREE for use in academic and research work with proper citation. J Ayub Med Coll Abbottabad accepts only original material for publication with the understanding that except for abstracts, no part of the data has been published or will be submitted for publication elsewhere before appearing in J Ayub Med Coll Abbottabad. The Editorial Board of J Ayub Med Coll Abbottabad makes every effort to ensure the accuracy and authenticity of material printed in J Ayub Med Coll Abbottabad. However, conclusions and statements expressed are views of the authors and do not reflect the opinion/policy of J Ayub Med Coll Abbottabad or the Editorial Board.
USERS are allowed to read, download, copy, distribute, print, search, or link to the full texts of the articles, or use them for any other lawful purpose, without asking prior permission from the publisher or the author. This is in accordance with the BOAI definition of open access.
AUTHORS retain the rights of free downloading/unlimited e-print of full text and sharing/disseminating the article without any restriction, by any means including twitter, scholarly collaboration networks such as ResearchGate, Academia.eu, and social media sites such as Twitter, LinkedIn, Google Scholar and any other professional or academic networking site.