Effects of compression on the loss of newly synthesized proteoglycans and proteins from cartilage explants.
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 of 35S- and 3H-labeled macromolecules from tissue into medium. In contrast, prolonged static compression induced matrix consolidation and appeared to hinder the diffusional transport and loss of 35S- and 3H-labeled macromolecules. Since high amplitude cyclic compression led to a sustained increase in the rate of loss of 3H- and 35S-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. The 35S-labeled proteoglycans lost during such cyclic compression were of smaller average size than those from controls, but contained a similarly low proportion (approximately 15%) that could form aggregates with excess hyaluronate and link protein. The size distribution and aggregability of the remaining tissue proteoglycans and 35S-labeled proteoglycans were not markedly affected. The loss of tissue proteoglycan paralleled the loss of 35S-labeled macromolecules. This study provides a framework for elucidating the biophysical mechanisms involved in the redistribution, catabolism, and loss of macromolecules during cartilage compression.
Sah
R L
RL
Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology & Harvard-M.I.T., Cambridge.
Doong
J Y
JY
Grodzinsky
A J
AJ
Plaas
A H
AH
Sandy
J D
JD
D000818:Animals; D002358:Cartilage, Articular / Q000378:metabolism*; D002417:Cattle; D006909:Hydroxyproline / Q000032:analysis; D007700:Kinetics; D009924:Organ Culture Techniques; D011312:Pressure; D011392:Proline / Q000378:metabolism; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification; D011509:Proteoglycans / Q000096:biosynthesis* / Q000302:isolation & purification; D013314:Stress, Mechanical; D013431:Sulfates / Q000378:metabolism; D013462:Sulfur Radioisotopes; D014316:Tritium
D011506:Proteins; D011509:Proteoglycans; D013431:Sulfates; D013462:Sulfur Radioisotopes; D014316:Tritium; D011392:Proline; D006909:Hydroxyproline