EFFECTS OF COMPRESSION ON THE LOSS OF NEWLY SYNTHESIZED PROTEOGLYCANS AND PROTEINS FROM CARTILAGE EXPLANTS
EFFECTS OF COMPRESSION ON THE LOSS OF NEWLY SYNTHESIZED PROTEOGLYCANS AND PROTEINS FROM CARTILAGE EXPLANTS
复制标题
DOI：
10.1016/0003-9861(91)90004-3
复制
发表时间：
1991-04-01
影响因子：
3.9
通讯作者：
SANDY, JD
中科院分区：
文献类型：
--
作者：
SAH, RLY;DOONG, JYH;SANDY, JD
研究了机械压缩小牛软骨外植体对蛋白聚糖和[35 S]硫酸盐和[3 H]脯氨酸放射性标记蛋白质的降解和损失的影响。直径为3 mm的软骨盘从1.25 mm至0.50 mm的单次2或12 h压缩，或从1.25 mm至1.00、0.75或0.50 mm的缓慢循环压缩（2 h开/2 h关）持续24 h，导致放射性标记大分子损失的一过性改变和/或持续增加。施加或移除载荷的影响与几种压缩引起的物理介质一致，包括流体流动、扩散和基质破坏。循环性压迫诱导对流性流体流动，并增加35 S-和3 H-标记的大分子从组织进入介质的损失。相反，长时间的静态压缩诱导基质固结，并出现阻碍扩散运输和损失的35 S-和3 H-标记的大分子。由于高幅度的周期性压缩导致3 H-和35 S-标记的大分子的损失率持续增加，伴随着[3 H]羟脯氨酸残基损失率的增加和组织水合作用的增加，这种压缩可能导致胶原网络的破坏。35 S标记的蛋白聚糖在这种循环压缩过程中损失的平均大小小于对照组，但含有类似的低比例（~15%），可以形成与过量透明质酸和连接蛋白的聚集体。剩余组织蛋白聚糖和35 S标记蛋白聚糖的尺寸分布和聚集性没有受到显着影响。组织蛋白多糖的丢失导致35 S标记大分子的丢失。这项研究提供了一个框架，阐明生物物理机制参与的再分配，catalysts，和损失的大分子在软骨压缩。
The effects of mechanical compression of calf cartilage explants on the catabolism and loss into the medium of proteoglycans and proteins radiolabeled with [35S]sulfate and [3H]proline were examined. A single 2- or 12-h compression of 3-mm diameter cartilage disks from a thickness of 1.25 to 0.50 mm, or slow cyclic compression (2 h on/2 h off) from 1.25 mm to 1.00, 0.75, or 0.50 mm for 24 h led to transient alterations and/or sustained increases in loss of radiolabeled macromolecules. The effects of imposing or removing loads were consistent with several compression-induced physical mediators including fluid flow, diffusion, and matrix disruption. Cyclic compression induced convective fluid flow and enhanced the loss of35S- and3H-labeled macromolecules from tissue into medium. In contrast, prolonged static compression induced matrix consolidation and appeared to hinder the diffusional transport and loss of35S- and3H-labeled macromolecules. Since high amplitude cyclic compression led to a sustained increase in the rate of loss of3H- and35S-labeled macromolecules that was accompanied by an increase in the rate of loss of [3H]hydroxyproline residues and an increase in tissue hydration, such compression may have caused disruption of the collagen meshwork. The35S-labeled proteoglycans lost during such cyclic compression were of smaller average size than those from controls, but contained a similarly low proportion (~15%) that could form aggregates with excess hyaluronate and link protein. The size distribution and aggregability of the remaining tissue proteoglycans and35S-labeled proteoglycans were not markedly affected. The loss of tissue proteoglycan paralleled the loss of35S-labeled macromolecules. This study provides a framework for elucidating the biophysical mechanisms involved in the redistribution, catabolism, and loss of macromolecules during cartilage compression.