title: Compression of cartilage results in differential effects on biosynthetic pathways for aggrecan, link protein, and hyaluronan.
abstract: The differential effects of static compression and recovery from compression on biosynthesis and biosynthetic pathways of aggrecan, link protein, and hyaluronan were assessed. During compression, biosynthesis of aggrecan and link protein were inhibited to approximately 25 and approximately 40%, respectively, of free-swelling control levels. In marked contrast, hyaluronan synthesis was unaffected by static compression. After release from 12-h 50% static compression, aggrecan synthesis remained inhibited for up to 2.5 days; however, link protein synthesis completely recovered to free-swelling control levels within 8 h after release. Hyaluronan synthesis remained at control levels after release of compression. During compression, aggrecan core protein pool size was decreased, whereas the rate of processing into the proteoglycan form remained essentially the same as in free swelling control tissue. Four hours after release from compression, aggrecan core protein pool size remained small and the rate of intracellular processing of aggrecan had become slower than that of free swelling control tissue. Due to the altered core-protein processing kinetics, fewer but longer chondroitin sulfate chains were added to the core proteins. Sulfation was not markedly altered. The differential effects of static compression and release on the biosynthesis of aggrecan, link protein, and hyaluronan are similar to the changes in the biosynthetic pathways that are affected in response to IL-1 treatment, suggesting that the response to static compression is not a general inhibition of cellular activity, but appears to be part of a specific transduction mechanism.
authors.affiliation: Continuum Electromechanics Group, Laboratory for Electromagnetic and Electronic Systems, Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology, Cambridge, 02139, USA.
authors.forename: Y J
authors.initials: YJ
authors.lastname: Kim
authors.forename: A J
authors.initials: AJ
authors.lastname: Grodzinsky
authors.forename: A H
authors.initials: AH
authors.lastname: Plaas
mesh_terms: D053674:Aggrecans; D000818:Animals; D002358:Cartilage, Articular / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D002417:Cattle; D003513:Cycloheximide / Q000494:pharmacology; D016326:Extracellular Matrix Proteins; D006820:Hyaluronic Acid / Q000096:biosynthesis*; D007700:Kinetics; D037181:Lectins, C-Type; D007930:Leucine / Q000378:metabolism; D009924:Organ Culture Techniques; D014176:Protein Biosynthesis; D011509:Proteoglycans / Q000096:biosynthesis*; D013314:Stress, Mechanical; D013431:Sulfates / Q000378:metabolism; D013462:Sulfur Radioisotopes; D013997:Time Factors; D014316:Tritium; D000099249:Proteoglycan Link Protein
chemical_list: D053674:Aggrecans; D003513:Cycloheximide; D016326:Extracellular Matrix Proteins; D006820:Hyaluronic Acid; D037181:Lectins, C-Type; D007930:Leucine; D011509:Proteoglycans; D013431:Sulfates; D013462:Sulfur Radioisotopes; D014316:Tritium; D000099249:Proteoglycan Link Protein