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兔角膜裂伤后的胶原代谢

Collagen metabolism following corneal laceration in rabbits.

作者信息

Cionni R J, Katakami C, Lavrich J B, Kao W W

出版信息

Curr Eye Res. 1986 Aug;5(8):549-58. doi: 10.3109/02713688609015118.

Abstract

We investigated the synthesis and degradation of collagen in lacerated rabbit corneas. The rate of collagen synthesis was measured by the incorporation and hydroxylation of [14C]proline up to 5 weeks after a penetrating laceration. Our results indicate that protein and collagen synthesis is initially reduced during the 24 h period after laceration and then increases in two phases. A moderate increase in protein and collagen synthesis occurs up to day 5 after laceration. Synthesis then decreases to a low level through the 10th day after injury. A second wave of increase in protein and collagen synthesis takes place reaching a new peak of approximately twice the activity as found in control corneas after 5 weeks of healing. Afterwards, the rate of protein and collagen synthesis declines and reaches the basal level after 7 weeks of healing. In a separate set of experiments, rabbit corneas were lacerated and allowed to heal for one or three weeks at which point 100 microCi of [14C]proline was injected into each anterior chamber. The corneas were excised 1 to 17 days later and subjected to collagen analysis. Our data indicates that the degradation of collagen synthesized by the cornea 1 week after laceration followed biphasic kinetics. In the first phase, the half-life of newly-synthesized collagen is 20 days, whereas it is approximately 4 days in the second phase. It is of particular interest that the accelerated degradation of the newly-synthesized [14C]collagen is concomitant with the increased rate of collagen synthesis during the wound healing process. The degradation of collagen synthesized 3 weeks after injury was slower and followed monophasic kinetics having a half-life of 14 days. The degradation of non-collagenous 14C-proteins follow a monophasic kinetics having a half-life of 6-7 days. Polyacrylamide gel electrophoresis of newly-synthesized collagen indicated that the collagen(I) and collagen(V) were the main collagenous components synthesized by the lacerated corneas.

摘要

我们研究了兔角膜裂伤后胶原蛋白的合成与降解。通过在穿透性裂伤后长达5周的时间内,观察[14C]脯氨酸的掺入和羟化情况来测定胶原蛋白的合成速率。我们的结果表明,蛋白质和胶原蛋白的合成在裂伤后的24小时内最初会减少,然后分两个阶段增加。在裂伤后第5天之前,蛋白质和胶原蛋白的合成会适度增加。然后,合成在损伤后第10天降至低水平。蛋白质和胶原蛋白合成的第二波增加发生在愈合5周后,达到一个新的峰值,其活性约为对照角膜的两倍。此后,蛋白质和胶原蛋白的合成速率下降,在愈合7周后达到基础水平。在另一组实验中,将兔角膜裂伤并使其愈合1周或3周,此时向每个前房注射100微居里的[14C]脯氨酸。1至17天后切除角膜并进行胶原蛋白分析。我们的数据表明,裂伤后1周角膜合成的胶原蛋白降解遵循双相动力学。在第一阶段,新合成胶原蛋白的半衰期为20天,而在第二阶段约为4天。特别有趣的是,新合成的[14C]胶原蛋白加速降解与伤口愈合过程中胶原蛋白合成速率增加同时发生。损伤后3周合成的胶原蛋白降解较慢,遵循单相动力学,半衰期为14天。非胶原蛋白14C蛋白的降解遵循单相动力学,半衰期为6 - 7天。新合成胶原蛋白的聚丙烯酰胺凝胶电泳表明,胶原蛋白(I)和胶原蛋白(V)是裂伤角膜合成的主要胶原成分。

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