Morphological Comparison Of In Vitro Collagen Fibrosis In Young And Old Rat Tails
Keywords
Young Mice, Old Mice, Collagen Fibrosis In Vitro, Young Mice, Old Mice, Collagen Fibrosis In Vitro
Abstract
Objective: To explore the effect of age on collagen fibrosis by observing the fibrosis process of tail collagen in young and old rats in vitro and the morphological changes of collagen fibers in lumbar cancellous bone of young and old rats. Method: Take 5g each of rat tail tendons at 2 weeks and 20 months, extract collagen using dilute acetic acid, and freeze-dry the extracted collagen. Take 15 mg of rat tail collagen from 2-week-old and 20-month-old rats, divide it into 3 groups, 5 mg in each group, and dissolve them in 10 mmol/L acetic acid solution at 4¡ãC; infiltrate the titanium metal screws into the acetic acid solution, and add buffer solution , collagen fibrosis was performed at 37¡ãC, the screws were taken out at three time points: 2, 4, and 8 hours, and the collagen morphology on the screw surface was observed under a scanning electron microscope. Take 10 mice each at 2 weeks and 20 months. After sacrifice, the L3 vertebral bodies are taken out and made into regular specimens. After repeated washing with physiological saline, they are dehydrated, sprayed with gold, and observed under a scanning electron microscope. Results: After 2 hours of fibrosis, the collagen fibers in the rat tails of the 2-week-old and 20-month-old groups did not undergo microfibrillation on the screw surface. After 4 hours of fibrosis, 20-month-old rat tail collagen fibrils aggregated into irregular clumps of collagen polymers on the surface of the screw, and no collagen fibers were formed; 2-week-old rat tail collagen formed microfibrils on the surface of the screw with a width of 0.07¡«0.20? ¦Ìm criss-crossing collagen fibers. After 8 hours of fibrosis, the 20-month-old rat tail collagen gathered on the surface of the screw to form collagen polymers of varying sizes and shapes, and no collagen fibers were formed. The 2-week-old rat tail collagen fibrils further fibrillated, forming a width of 0.65 to 0.65 mm. 1.35? ¦Ìm collagen fibers. Scanning electron microscopy of trabecular bone showed that: the collagen of 2-week-old mouse bone was cross-linked into collagen fibers of uniform thickness, and the fibers were arranged closely together with consistent orientation; the collagen fibrils of trabecular bone of 20-month-old mouse were of varying thicknesses and were loosely, sparsely, and sparsely arranged. Disorganization, in which the orientation of finer collagen fibrils connecting adjacent thicker fibrils is disordered. Conclusion: As age increases, the fibrosis ability of type I collagen gradually decreases, leading to changes in the morphology of bone collagen fibers and abnormal mineral deposition. This may be one of the very important reasons for the increased risk of osteoporosis and fractures in the elderly.
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Original research was done by Liu Guomin|Sun Honghui|Zhang Yanqiu|Zhang Yongli|Kong Ning
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