Lectin Stainning of Extensor Digitorum Longus Muscle Cell Membranes in Alloxan Diabetic Rats

Nursel GÜL, Suna CEBESOY, Nesrin ÖZSOY


Extensor digitorum longus (EDL) muscle of alloxan-diabetic rats were observed by lectin staining techniques in light microscope. Samples of muscles were obtained from control and diabetic rats. The muscle samples sections were cutted by cryostat microtome and stained by four biotinylated lectins [Wheat Germ Agglutinin (WGA), Pea Nut Agglutinin (PNA), Concavalin A (ConA), Griffonia simplicifolia I (GS-I)]. The lectins were detected by avidin-peroxidase complex.  All lectins were bounded to EDL muscle cell membranes of control and diabetic rats. GS-I and WGA lectins were strongly stained extensor digitorum muscle cell membranes of alloxan-diabetic rats. Not only cell membranes but also cytoplasmic miyofibrills of diabetic muscle cells were stained by GS-I lectin. PNA was moderate stained diabetic muscle cell membranes. Con A was weakly stained diabetic muscle cell membranes with respect to control cell membranes. We suggested that there were changes in carbohydrate-containing constituents of the alloxan-diabetic muscle cell membranes.

Anahtar Kelimeler

Extensor Digitorum Longus Muscle Cell Membrane, Lectin Stainning, Diabetes mellitus, Alloxan, Wistar rat.

Tam Metin:



WHO (World of Health Organisation) 1999. Consultation. Definition, diagnosis and classification of diabetes mellitus and its complication. WHO Department of Noncommnicable Disease Surveillance Geneva.

Low Wang CC, Hess CN, Hiatt WR, Goldfine AB. 2016. Atherosclerotic cardiovascular disease and heart failure in type 2 diabetes-mechanism, management, and clinical considerations. Circulation, 133(24):2459-2502.

Grossıe J. 1982. Contractile and electrical characteristic of extensor muscle from alloxan –diabetic rats. An in vitro study. Diabetes, 31:194-202.

Paulus SF, Grossıe J. 1983. Skeletal muscle in alloxan-diabetes . A comparison of isometric contractions in fast and slow muscles. Diabetes, 32:1035-1039.

Cotter MA, Cameron NE, Lean DR, Robertson S. 1989. Effect of long-term streptozotocin diabetes on the contractile and histochemical properties of rat muscles. J Exper Physiol, 74:65-74.

McGuire M and MacDermott M(1999). The influence of streptozotocin diabetes and metformin on erythrocyte volume and on the membrane potential and the contractile characteristics of the extensor digitorum longus and soleus muscles in rats. J Exp Physiol, 84: 1051–1058.

D’Souza DM, Al-Sajee D, Hawke TJ. 2013. Diabetic myopathy:impact of diabetes mellitus on skeletal muscle progenitor cells. Front Physiol, 4:379.

Krause MP, Al-Sajee D, D’Souza DM, Rebalka IA, Moradi J, Riddell MC, Hawke TJ. 2013. Impaired macrophage and satellite cell infiltration occurs in a muscle-spesific fashion following injury in diabetic skeletal muscle. PLoS One, 8(8):e70971.

Kristensen JM, Treebak JT, Schjerling P, Goodyear L, Wojtaszewski JFP. 2014. Two week of metformin treatment induces AMPK-dependent enhancement of insulin-stimulated glucose uptake in mouse soleus muscle. Am J Physiol Endocrinol Metab, 306(10):1099-1199.

Ostler JE, Maurya SK, Dials J, Roof SR, Devor ST, Ziolo MT, Periasamy M. 2014. Effects of insulin resistance on skeletal muscle growth and exercise capacity in type 2 diabetic mouse models. Am J Physiol Endocrinol Metab, 306(6):E592-E605.

Green S, Egaña M, Baldi JC, Lamberts R, Regensteiner JG. 2015. Cardiovascular control during exercise in type 2 diabetes mellitus. J Diabetes Res, 2015:654204.

Fortes MAS, Pinherio CHJ, Guimarães- Ferreira L, Vitzel KF, Vasconceolos DAA, Curi R. 2015. Overload-induced skeletal muscle hypertrophy is not impaired in STZ-diabetic rats. Physiol Rep, 3(7):e12457.

Mimata Y, Sato K, Tokunaga K, Tsukimura I, Tada H, Doita M. 2015. Diabetic Muscle Infarction of the Tibialis Anterior and Extensor Hallucis Longus Muscles Mimicking the Malignant Soft-Tissue Tumor. Case Rep Orthop, 2015: 656307.

Almurdhi MM, Reeves ND, Bowling FL, Boulton AJ, Jeziorska M, Malik RA. 2016. Reduced lower-limb muscle strength and volume in patients with type 2 diabetes in relation to neuropathy, ıntramuscular fat, and vitamin D levels. Diabetes Care. 39(3):441-447.

Alpui C, Ramos K, Tenner TE (1993). Alterations of rabbit aortic smooth muscle cell proliferation in diabetes mellitus : spotlight on growth regulation in the cardiovascular system. Cardiovasc. Res. 27:1229-1232.

Kawano M, Koshikawa T, Kanzaki T, Morisaki N, Saito Y, Yoshida S (1993). Diabetes mellitus induced accelerated growth of aortic smooth muscle cells: association with overexpression of PDGF beta-receptors. EUR J Clin. Invest. 23:84-90.

Thorburn AW, Gumbiner B, Bulacan F, Brechtel G, Henry RR (1991) Multiple defects in muscle glycogen synthase activity contribute to reduced glycogen synthesis in non-insulin dependent diabetes mellitus. J Clin. Invest. 87:489-495.

Kjeldsen K, Braendgaard H, Sıdenıus P, Larsen JS, Norgaard A (1987). Diabetes decreases Na+-K+ pumb concerntration in skeletal muscles, heart ventricular muscle, and peripheral nerves of rat. Diabetes 31: 194-202

Cebesoy S, Ozsoy N, Gül N, Ayvalı C, Kutlu I (2000). Histochemical properties of skeletal muscle fibers in alloxan-diabetic rats. J Inst. Sci. Technol. Gazi Uni. 13:599-611.

Sharon, N (1977). Lectin. Sci. Amer. 236:108-119.

Lis H, Sharon N (1986) Lectins as molecules and as tools. Ann. Rev. Biochem. 55:35-67.

Sharon N, Lis H (1989). Lectins. Chapman and Hall Ltd., New York.

Vierbuchen M (1991) Lectin receptors. In Current Topics in Pathology. (Ed. Seifert, G.) Springer-Verlag, Berlin 83:1-522.

Jagannathan M, McDonnell M, Liang Y, Hasturk H, Hetzel J, Rubin D, Kantarci A, Van Dyke T E, Ganley-Leal L M, Nikolajczyk B S. 2010. Toll-like receptors regulate B cell cytokine production in patients with diabetes. Diabetologia, 53(7):1461-1471.

Lawrenson JG, Glyn MCP, Ward BJ (2002). Ultrastructural and morphometric comparison of retinal and myocardial capillaries following acute ischaemia. Microvasc. Res. 64:65-74.

Schaumburg-Lever G, Alroy J, Ucci A, Lever WF (1984). Distribution of carbohydrate residues in normal skin. Arch. Dermatol. Res. 276:216-223.

Pena SDJ, Gordon BB, Karpati G, Carpenter S (1981). Lectin histochemistry of human skeletal muscle. J Histochem. Cytochem. 29:542-546.

Dunn MJ, Sewry CA, Dubowitz V (1982). Cytochemical studies of lectin binding by diseased human muscle. J Neurol. Sci. 55:147-159.

Capaldi MJ, Dunn MJ, Sewry CA, Dubawitz V (1984). Binding of Ricinus communis 1 lectin to the muscle cell plasma membrane in diseased muscle. J Neurol. Sci. 64:315-324

Zaccone G, Fasulo S, Lo Cascio P, Licata A, Ainis L, and Affronte R (1987). Lectin-binding pattern on the surface epidermis of Ambystoma tigrinım larvae. Histochem. 87:431-438.

Helliwell TR, Gunhan O, Edwards RH (1989). Lectin binding and desmin expression during necrosis, regeneration, and neurogenic atrophy of human skeletal muscle. J Path. 159:43-51.

Kirkeby S., Moe D., Bøg-Hansen TC (1993). Fucose expression in skeletal muscle: a lectin histochemical study. Histochem. J. 25:619-627.

Reuterwing CO, Hogg E, Holm J (1987). Salivary glands in long-term alloxan-diabetic rats. A quantitative light and electron microscopic study. Acta Pathol. Microbiol. Immunol. Scand. Sect. A; 95:131-136.

Capaldi MJ, Dunn MJ, Sewry CA and Dubowitz V (1985). Lectin binding in human skeletal muscle: a comparison of 15 different lectins. Histochem. J. 17:81-92.

Yamagami T, Hosaka M and Mori M (1985). Classification of skeletal muscle fibers by comparison of enzyme histochemistry with lectin binding. Cell Mol. Biol. 31:241-249.


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