Millard C B, Tripathi B J, Tripathi R C
Eye Research Laboratories, University of Chicago, IL.
Exp Eye Res. 1987 Oct;45(4):623-31. doi: 10.1016/s0014-4835(87)80071-4.
The protein profile of the trabecular meshwork from 44 normal human eyes of various ages, ranging from 5 months to 87 years, was investigated by using sodium dodecyl sulfate-polyacrylamide-gel (SDS-PAGE) electrophoresis and a highly sensitive silver-stain technique. Samples from each eye were analysed individually to avoid anomalies that may occur with tissue pooling. More than 20 protein bands were consistently visible at all ages and varied in molecular weight from 20,000 to 290,000 MW. The shifts which occurred in band prominence with increasing age included a consistent decrease in the intensity of bands at MWs 42,000 (tentatively identified as G-actin) and 58,000; a noticeable increase in the intensity of the bands at MWs 140,000 and 160,000 that correspond to alpha I and II components of type IV collagen; and a gradual disappearance of a faint band at MW 68,000 in eyes older than 31 years. Our study shows that molecular aging does occur in the trabecular meshwork. The data presented also provides a basis for comparison of the polypeptide alterations that may occur in primary open-angle glaucoma and in other disease processes.
采用十二烷基硫酸钠 - 聚丙烯酰胺凝胶（SDS - PAGE）电泳和高灵敏度银染技术，对44只年龄从5个月到87岁不等的正常人眼小梁网的蛋白质谱进行了研究。对每只眼睛的样本单独进行分析，以避免组织合并可能出现的异常情况。所有年龄段均始终可见20多条蛋白带，分子量在20,000至290,000道尔顿之间。随着年龄增长，蛋白带突出程度发生的变化包括：分子量为42,000（暂定为G - 肌动蛋白）和58,000的条带强度持续下降；分子量为140,000和160,000的条带强度显著增加，这两条带对应于IV型胶原的αI和αII成分；以及在31岁以上的眼睛中，分子量为68,000的一条 faint 带逐渐消失。我们的研究表明小梁网中确实发生了分子老化。所呈现的数据也为比较原发性开角型青光眼和其他疾病过程中可能发生的多肽变化提供了基础。
