Abstract
Extracellular glycoproteins play an important role in wound healing; yet little is known about glycoprotein biosynthesis and its regulation by insulin in inflammation. Using [1-14C] fucose as a marker, glycoprotein biosynthesis was studied in carrageenan-induced granuloma from diabetic and control rats. Fucose incorporation into glycoproteins was followed for 24 h after an intraperitoneal injection of the label. Radioactivity in trichloroacetic acid precipitable serum glycopoteins and saline-soluble and insoluble glycoproteins was assessed in five-, seven-, and ten-day-old granuloma tissues. Fucose incorporation was higher in soluble glycoproteins (P < 0.01) at all points in controls than in diabetic granulomas, and peak incorporation was reached in both groups on the seventh day. Incorporation of fucose into insoluble glycoproteins was higher in normals on the seventh day than in diabetics. Liver-, kidney-, and intestine-soluble glycoproteins showed a maximum incorporation on the seventh day, but no difference was noted between diabetic and normal rats. Incorporation of fucose in insoluble glycoproteins showed a gradual decline with the age of granuloma in all tissues from both groups, with the exception of the kidney. In the kidney, fucosylation of insoluble glycoproteins was decreased (P < 0.01) in diabetics compared to controls. These results indicate an active phase of biosynthesis, with an increase in glycosylation during inflammation that is probably insulin dependent.
Similar content being viewed by others
References
Vane, J. R., andS. H. Ferreira, editors. 1978. Handbook of Experimental Pharmacology, Vol. 50, Part 1, Inflammation. Springer Verlag, New York, 1–784.
Nicoletis, C., S. Bazin, andL. M. Lous. 1977. Clinical and biochemical features of normal, defective, and pathologic scars.Clin. Plast. Surg. 4:347–359.
Peacock, E. E. 1984. Wound Repair, 3rd ed. W. B. Saunders, Philadelphia. 56–140.
Cohen, I. K., C. D. Moore, andR. F. Diegelmann 1979. Onset and localization of collegan synthesis during wound healing in open rat skin wounds.Proc. Soc. Exp. Biol. Med. 160:458–462.
Ivaska, K. 1981. Effect of extracellular glycosaminoglycans on the synthesis of collagen and proteoglycans by granulation tissue cells. A study with freshly isolated experimental granulation tissue cells of rat.Acta Physiol. Scand. Suppl. 494:1–53.
Borel, J. P. 1982. Clinical biochemistry of inflammation and the role of connective tissue.In XI International Congress of Clinical Chemistry. E. Kaiser, F. Gabe, M. M. Muller, M. Bayer, editors, W. Gruyter, Berlin. 673–685.
Viljanto, J., R. Penttinen, andJ. Raekallio. 1981. Fibronectin in early phases of wound healing in children.Acta Chir. Scand. 147:7–13.
Dolynchuk, K. N., andJ.M. Bowness. 1981. The early metabolism of noncollagenous glycoproteins during wound healing.J. Surg. Res. 31:218–224.
Koj, A., H. Kasperczyk, J. Bereta, andA. H. Gordon. 1982. Changes in the blood level and affinity to concanavalin A of rat plasma glycoproteins during acute inflammation and hepatoma growth.Biochem. J. 206:545–553.
Koj, A. 1974.In Structure and Function of Plasma Proteins, Vol. 1. A. C. Allison, editor. Plenum Press, New York. 73–131.
Gordon A. H. 1976.In Plasma Protein Turnover. R. Bianchir, G. Mariani, and A. S. McFarlane, editors. University Park Press, Baltimore. 381–394.
Miller, L. L. 1976. The definitive role of known hormones in the regulation of net biosynthesis of five acute-phase proteins (APPP) by the isolated perfused rat liver: Corticosera.In Protides of the Biological Fluids, Vol. 23. H. Peters, editor. Pergamon, Oxford. 461–471.
Bhandaru, R., S. R. Srinivasan, B. Radhakrishnamurthy, andG. S. Berenson. 1982. Effects of high fat-high cholesterol diet on plasma lipid levels and on erythrocyte membrane composition.Atherosclerosis 42:263–272.
Dalferes, E. R., Jr., B. Radhakrishnamurthy, andG. S. Berenson. 1980. Studies on glycoproteins from bovine aorta.Artery 7:85–98.
Lowry, O. H., N. J. Rosebrough, A. L. Farr, andR. J. Randall 1951. Protein measurement with the Folin phenol reagent.J. Biol. Chem. 193:265–275.
Bekesi, J. G., andR. J. Winzler. 1967. The metabolism of plasma proteins: Studies on the incorporation ofl-Fucose-1-14C into tissue and serum in the normal rat.J. Biol. Chem. 242:3873–3879.
Srinivasan, S. R., G. S. Berenson, andB. Radhakrishnamurthy. 1970. Glycoprotein changes in diabetic kidneys.Diabetes 19:171–175.
Berenson, G. S., B. Radhakrishnamurthy, E. R. Dalferes, Jr., H. Ruiz, S. R. Srinivasan, F. Plavidal, andF. Brickman. 1972. Connective tissue macromolecular changes in rats with experimentally induced diabetes and hyperinsulinism.Diabetes 21:733–743.
Coffey, J. W., O. N. Miller, andO. Z. Sellinoer. 1964. The metabolism of L-fucose in the rat.J. Biol. Chem. 293:4011–4017.
Manchester, K.L., andF. G. Young. 1961. Insulin and protein metabolism.Vitam. Horm. 19:95–132.
Alhadeff, J. A., andP. Watkins. 1983. Dolichyl phosphate-mannosyltransferase and dolichyl phosphate-n-acetylglucosaminyltransferase activities in liver preparations from normal controls and patients with cystic fibrosis and diabetes mellitus.Clin. Chim. Acta 134:1–9.
Urban, J., D. Chan, G. Schreiber 1979. A rat serum glycoprotein whose synthesis rate increases greatly during inflammation.J. Biol. Chem. 254:10565–10568.
Stout, R. W., E. L. Bierman, andR. Ross. 1975. The effect of insulin on the proliferation of cultered primate arterial smooth muscle cells.Circ. Res. 36:319–327.
Author information
Authors and Affiliations
Additional information
This research was supported by funds from the National Heart, Lung and Blood Institute of the U.S. Public Health Service, HL-21649 and HL-02942, and the National Research and Demonstration Center-Arteriosclerosis (HL-15103).
Rights and permissions
About this article
Cite this article
Sharma, C., Dalferes, E.R., Radhakrishnamurthy, B. et al. Glycoprotein biosynthesis during inflammation in normal and streptozotocin-induced diabetic rats. Inflammation 9, 273–283 (1985). https://doi.org/10.1007/BF00916276
Issue Date:
DOI: https://doi.org/10.1007/BF00916276