Glycation alters collagen fibril organization.
Incubation of rat tail tendon in 0.2M ribose results in accelerated non-enzymatic glycosylation of collagen, with the formation of fluorescent cross-links between molecules and decreased solubility. Electron micrographs of tendon cross-sections show an increased fibril packing density with increasing degrees of glycation. After a one-week incubation in ribose, every fibril appears in close contact with all of its neighbors, and the packing density has increased to 76%, from a value of 62% in controls. Irregular diameters and fusion of fibrils also are seen. All of the fibrils in a bundle appear to become cross-linked together, creating a larger stress bearing unit. This model is consistent with stress-strain curves showing a large increase in tensile stress and stiffness after a one-week incubation period in ribose. The diameters of the collagen fibrils increase in size in glycated tendon. We hypothesize larger diameters result from an increased resistance to shrinkage during the specimen preparation process, as a result of the rigid sugar derived cross-links. Closer fibril packing, increased fibril diameters, and irregular diameters have been reported in diabetic tissues, and may result from decades of glycation induced cross-link accumulation.
Bai
P
P
Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway 08854.
Phua
K
K
Hardt
T
T
Cernadas
M
M
Brodsky
B
B
D000818:Animals; D003094:Collagen / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D005260:Female; D006031:Glycosylation; D008854:Microscopy, Electron; D051381:Rats; D011919:Rats, Inbred Strains; D013710:Tendons / Q000378:metabolism / Q000648:ultrastructure
D003094:Collagen