1984
DOI: 10.2337/diabetes.33.10.970
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Inhibition of fibronectin binding to matrix components by nonenzymatic glycosylation

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Cited by 17 publications
(11 citation statements)
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“…51 AGE-modified fibronectin has reduced ability to support cell adhesion, spreading, and migration, 52,53 and to bind to collagen and heparin. 54 As such, the fibronectin fibrils observed in uninjured human diabetic skin may have reduced function. Fibronectin matrix mimetics promote adhesion, spreading, and migration, 24 suggesting that they may be used to overcome the irregularities in cell adhesion and migration associated with AGE-modified fibronectin from diabetic humans.…”
Section: Discussionmentioning
confidence: 99%
“…51 AGE-modified fibronectin has reduced ability to support cell adhesion, spreading, and migration, 52,53 and to bind to collagen and heparin. 54 As such, the fibronectin fibrils observed in uninjured human diabetic skin may have reduced function. Fibronectin matrix mimetics promote adhesion, spreading, and migration, 24 suggesting that they may be used to overcome the irregularities in cell adhesion and migration associated with AGE-modified fibronectin from diabetic humans.…”
Section: Discussionmentioning
confidence: 99%
“…It is possible that enhanced nonenzymatic glycation of extracellular matrix proteins such as fibronectin and laminin may interfere with the synthesis and function of HSPG. It has been shown that increased nonenzymatic glycation of either fibronectin (23) or laminin (24) reduces heparin or heparan sulfate binding to these matrix proteins and thus alters macromolecular assembly of basement membranes. During this rearrangement of macromolecular assembly, it is possible that HSPG synthesis is decreased.…”
Section: Discussionmentioning
confidence: 99%
“…In our study a high fibronectin concentration may be the effect of widespread endothelial injury to small vessels. Although a recent study showed no modulation of PF function in diabetic patients receiving insulin treatment [30], some studies showed that glycated fibronectin is characterized by altered properties, especially by decreased binding to collagen and endothelial cells [9,11]. This may contribute to disturbed vessel wall integrity.…”
Section: Resultsmentioning
confidence: 99%
“…Glycated fibronectin Received: June 14, 1994 Accepted: November 26, 1994 Correspondence to: Dr. Mehmet Ali GUNDOGAN, Dept. of Endocrinology Gulhane School of Medicine, 06018 EtlikAnkara, Turkey is characterized by altered properties, especially by decreased binding to collagen and endothelial cells [7][8][9][10][11]. This may contribute to disturbed vessel wall integrity [9,11].…”
mentioning
confidence: 99%