OBJECTIVE: To study the proliferation change of tunica intima and smooth muscle in artery after hydrolic dilation for potential clinical use. METHODS: Sixten adult New Zealand rabbits were randomly divided into 4 groups, named group A, B, C and D. Right carotid arteries of rabbits of those 4 groups were dilated by hydrolic dilation with different pressures with 0 kPa, 40 kPa, 80 kPa, and 120 kPa respectively. The arterial calibers, thickness of tunica intima and smooth muscle were analyzed by automatic medical photograph analyzer immediately, 1 week and 2 weeks later respectively. RESULTS: The arterial calibers in the experimental group were larger than those in control group after immediate hydrolic dilation and 1 week later (P lt; 0.01). At 2 weeks, the arterial calibers in group B and D has no significant difference compared to group A (P gt; 0.05), and those in group C were larger than that of group A (P lt; 0.01). There were no significant difference in thickness of tunica intima and smooth muscle between the experimental group and control group (P gt; 0.05) after immediate hydrolic dilation. At 1 and 2 weeks after dilation, there were no significant difference between group A and group B (Pgt; 0.05), and those in group C and D were all larger than those in group A (P lt; 0.01). No obvious proliferation of tunica intima were observed in group B at 2 weeks after hydrolic dialation, but the proliferation of tunica intima could be observed in group C and D, especially in group D. CONCLUSION: Caliber of artery can be expanded by hydrolic dilation with higher pressure, but the proliferation of tunica intima and smooth muscle may be occurred in hydrolic dilation with higher pressure over 80 kPa, therefore it is safe to use hydrolic dilation with pressure no more than 40 kPa.
Objective To study the effects of advanced glycation end (AGEs) products induced by bovine serum albumin (BSA) on the survival and the morphology of bovine retinal endothelial cells (BREC) and pericytes (BRP). Methods BSA with the final concentration of 50 mg/ml was incubated in PBS, containing 500 mmol/L D-glucose, for 12 weeks under 37℃. AGEs-BSA was purified by Sephacryl S-300 column chromatography and was confirmed by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The concentration of AGEs-BSA was determined by the method of commassie protein assay. In order to detect the toxic effects of AGEs-BSA on cultured BREC and BRP, groups of AGEs-BSA and BSA with different concentration and untreated control were set up. Phase contrast microscope was used to observe the effect of AGEs-BSA and BSA (with the concentration of 500mu;g/ml and actuation duration of 48 hours) on morphology of BREC and BRP. Results As the dosage of AGEs-BSA increased, the number of inhibited cells increased. When the concentration of AGEs-BSA was 500mu;g/ml, the inhibited BREC in AGEs-BSA group was (72.8plusmn;15.9)% of which in untreated control group, and the inhibited BRP was (64.8plusmn;9) % of which in untreated control group. AGEs-BSA with low concentration promoted the proliferation of endothelial cells, but there was no significant difference between AGEs-BSA and the control group (P=0.231). Inhibited proliferation and abnormal morphology were seen under the phase contrast microscope while the normal morphology of cells was found in BSA and control group. Conclusion AGEs-BSA with the high concentration may inhibit the growth of both BREC and BRP, which leads the loss of BRP and damage of vascular function. These results suggest that nonenzymatic glycosylation plays a major role in diabetic complications. (Chin J Ocul Fundus Dis, 2006, 22: 11-15)