Abstract
Hyperglycemia-induced protein glycation is thought to be implicated in the diabetic vasculopathy. In this study, we cultured vascular endothelial cells on native or glycated collagen matrix and compared their growth and functional characteristics. At lower plating density, the cells grew equally well on both substrata; however, at higher planting density, the cells plated on glycated collagen grew slower and reached a lower confluent density compared to that of the native collagen-based cultures. Confluent cell layers formed on glycated collagen exhibited a lower diffusion barrier function and a less response to epidermal growth factor stimulated prostacyclin production, compared to their native collagen-cultured counterparts.
Similar content being viewed by others
References
Ahmed, N., 2005. Advanced glycation endproducts—role in pathology of diabetic complications. Diabetes Research and Clinical Practice. 67(1), 3–21.
Al-Abed,Y., Bucala, R., 2000. Structure of a synthetic glucose derived advanced glycation endproduct that is immunologically cross-reactive with its naturally occurring counterparts. Bioconjugate Chemistry. 11, 39–45.
Bailey, A.J., Sims, T.J., Avery, N.C., Halligane, E.P., 1995. Non-enzymic glycation of fibrous collagen: reaction products of glucose and ribose. Biochemical Journal. 305, 385–390.
Brownlee, M., Vlassara, H., Cerami, A., 1985. Nonenzymatic glycosylation products on collagen covalently trap low-density lipoprotein. Diabetes. 34, 938–941.
Bucala, R., Makita, Z., Vega, G., Grundy, S., Koschinsky, T., Cerami, A., Vlassara, H., 1994. Modification of LDL by advanced glycation endproducts contribute to the dyslipidaemia of diabetes and renal insufficiency. Proceedings of the National Academy of Sciences of the United States of America. 91, 9441–9445.
Bunn, H.F., Haney, D.N., Kamin, S., Gabbay, K.H., Gallop, P.M., 1976. The biosynthesis of human hemoglobin A1c. Slow glycosylation of hemoglobin in vivo. Journal of Clinical Investigation. 57, 1652–1659.
Chen, J., Brodsky, S., Li, H., Hampel, D.J., Miyata, T., Weinstein, T., Gafter, U., Norman, J.T., Fine, L.G., Goligorsky, M.S., 2001. Delayed branching of Endothelial capillary-like cords in glycated collagen I is mediated by early induction of PAI-1. American Journal of Physiology: Renal Physiology. 281, F71–F80.
Chen, J., Brodsky, S.V., Goligorsky, D.M., Hample, D.J., Li, H., Gross, S.S., Goligorsky, M.S., 2002. Glycated collagen I induces premature senescence-like phenotypic changes in endothelial cells. Circulation Research. 90, 1290–1298.
Chen, S., Chen, M.P., Ziyadeh, F.N., 2000. Amadori-glycated albumin in diabetic nephropathy: pathophysiologic connections. Kidney International Suppl. 77, S40–S44.
Chow, S.E., Lee, R.S., Shih, S.H., Chen, J.K., 1998. Oxidized LDL promotes vascular endothelial cell pinocytosis via a prooxidation mechanism. FASEB Journal. 12, 823–830.
Dyer, D.G., Dunn, J.A., Thorpe, S.R., Bailie, K E., Lyons, T.J., McCance, D.R., Baynes, J.W., 1993. Accumulation of Maillard reaction products in skin collagen in diabetes and aging. Journal of Clinical Investigation. 91, 2463–2469.
Facchiano, F., Lentini, A., Fogliano, V., Mancarella, S., Rossi, C., Facchiano, A., Capogrossi M.C., 2002. Sugar-induced modification of fibroblast growth factor 2 reduces its angiogenic activity in vivo. American Journal of Pathology. 161, 531–541.
Frye, E.B., Degenhardt, T.P., Thorpe, S.R., and Baynes, J.W., 1998. Role of the Maillard reaction in aging of tissue proteins. Journal of Biological Chemistry. 273, 18714–18719.
Jakuš, V., Bauerová K., Michalková D., Èársky J., 2001. Serum levels of advanced glycation end products in poorly metabolically controlled children with diabetes mellitus: relation to HbA1c. Diabetes Nutrition and Metabolism. 14, 207–211.
Johnson, R.N., Metcalf, P.A., Baker, J.R. 1982. Fructosamine: a new approach to the estimation of serum glycosylprotein. An index of diabetic control. Clinica Chimica Acta. 127, 87–95.
Lopes-Virella, M.F., Klein, R.L., Lyons, T.J., Stevenson, H.C., Witztum, J.L., 1988. Glycosylation of LDL enhances cholesteryl ester synthesis in human monocyte-derived macrophages. Diabetes. 37, 550–557.
McCance, D.R., Dyer, D.G., Dunn, J.A., Bailie, K.E., Thorpe, S.R., Baynes, J.W., Lyons, T.J., 1993. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. Journal of Clinical Investigation. 91, 2470–2478.
Meli, M., Granouillet, R., Reynaud, E., Chamson, A., Frey, J., and Perier C., 2003. Changes in glycation of fibrous type I collagen during long-term in vitro incubation with glucose. Journal of Protein Chemistry 22 (6), 521–525.
Obayashi, H., Nakano, K., Shigeta, H., Yamaguchi, M., Yoshimori, K., Fukui, M., Fujii, M., Kitagawa, Y., Nakamura, N., Nakamura, K., Nakazawa, Y., Ienaga, K., Ohta, M., Nishimura, M., Fukui, I., Kondo, M., 1996. Formation of crossline as a fluorescent advanced glycation endproduct in vitro and in vivo. Biochemical and Biophysical Research Communications. 226, 37–41.
Paul, R.G., Avery, N.C., Slatter, D.A., Sims, T.J., Bailey, A.J., 1998. Isolation and characterization of advanced glycation end products derived from the in vitro reaction of ribose and collagen. Biochemical Journal. 330, 1241–1248.
Reddy, S., Bichler, J., Wells-Knecht, K. J., Thorpe, S. R., Baynes, J. W., 1995. Ne-(Carboxymethyl)lysine is a dominant advanced glycation endproduct (AGE) In tissue proteins. Biochemistry 34, 10872–10878.
Schleicher, E.D., Wagner, E., Nerlich, A.G., 1997. Increased accumulation of the glycoxidation product N (epsilon)—(carboxymethyl) lysine in human tissue in diabetes and aging. Journal of Clinical Investigation. 99, 457–468
Sell, D.R., Nagaraj, R.H., Grandhee, S.K., Odetti, P., Lapolla, A., Fogarty, J., Monnier, V.M., 1991. Pentosidine: a molecular marker for the cumulative damage to proteins in diabetes, aging, and uremia. Diabetes Metabolism Reviews. 7, 239–251.
Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S.-D., Stern, D., Sayre, L.M., Monnier, V.M., Perry, G., 1994. Advanced Maillar reaction product are associated with Alzheimer diaease. Proceedings of the National Academy of Sciences of the United States of America 91, 5710–5714.
Turk, Z., Mesic, R., Benko, B., 1998. Comparison of advanced glycation endproducts on haemoglobin (Hb-AGE) and haemoglobin A1c for the assessment of diabetic control. Clinica Chimica Acta, 272, 159–170.
Turk, Z., Ljubic, S., Turk, N., Benko, B., 2001. Detection of autoantibodies against advanced glycation endproducts and AGEimmune complexes in serum of patients with diabetes mellitus. Clinica Chimica Acta, 303, 105–115.
Vlassara, H., Palace, M.R., 2002. Diabetes and advanced glycation endproducts. Journal of Internal Medicine. 251, 87–101.
Wautier, J.L., Zoukourian, C., Chappey, O., Wautier, M.P., Guillausseau, P.J., Cao, R., Hori, O., Stern, D., Schmidt A.M., 1996. Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy. Soluble receptor for advanced glycation end products blocks hyperpermeability in diabetic rats. Journal of Clinical Investigation. 97, 238–243.
Westwood, M.E., Thimalley, P.J., 1995. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins. Journal of Protein Chemistry 14, 359–372.
Wolffenbuttel, B. H. R., Giordano, D., Founds, H.W., Bucala, R., 1996. Long-term assessment of glucose control by haemoglobin-AGE measurement. Lancet. 347, 513–515.
Wu, J.T., Tu, M.C., Zhung, P., 1996. Advanced glycation end product (AGE): characterization of the products from the reaction between d-glucose and serum albumin. Journal Clinical Laboratory Analysis. 10, 21–34.
Author information
Authors and Affiliations
Corresponding author
Additional information
Editor: J. Denry Sato
Rights and permissions
About this article
Cite this article
Kuo, PC., Kao, CH. & Chen, JK. Glycated type 1 collagen induces endothelial dysfunction in culture. In Vitro Cell.Dev.Biol.-Animal 43, 338–343 (2007). https://doi.org/10.1007/s11626-007-9058-9
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11626-007-9058-9