The effect of phospholipase digestion upon the boundary lubricating ability of synovial fluid

Authors
Citation
Gd. Jay et Cj. Cha, The effect of phospholipase digestion upon the boundary lubricating ability of synovial fluid, J RHEUMATOL, 26(11), 1999, pp. 2454-2457
Citations number
21
Categorie Soggetti
Rheumatology,"da verificare
Journal title
JOURNAL OF RHEUMATOLOGY
ISSN journal
0315162X → ACNP
Volume
26
Issue
11
Year of publication
1999
Pages
2454 - 2457
Database
ISI
SICI code
0315-162X(199911)26:11<2454:TEOPDU>2.0.ZU;2-B
Abstract
Objective. To identify the boundary lubricant in synovial fluid (SF). Is sy novial lubrication mediated by surface active phospholipid as opposed to mu cinous glycoprotein? Methods. A sonicated preparation of phosphatidylcholine and bovine SF were tested in vitro in a bearing of latex oscillating against polished glass un der a load of 0.35 x 10(6) N/m(2). The friction apparatus isolates conditio ns of boundary lubrication and has been validated against a cartilaginous b earing. Coefficient of friction (mu) was measured and compared against mu f rom physiologic saline, which served as a control. Separate digestions were carried out upon the SF with trypsin, phospholipase C, and phospholipase A (2) in the presence and absence of proteolytic inhibitors. Results, Digestions of bovine SF by phospholipase C in the presence of prot ease inhibitors did not remove boundary lubricating ability compared to an undigested control (p = 0.89). Digestion of bovine SF with trypsin removed all lubricating ability and raised friction (p = 0.004). Commercial purifie d phospholipase C contained trypsin-like activity when activity was tested with N alpha-benzoyl-L-arginine ethyl ester as substrate. Similar results w ere observed for phospholipase A(2), which possesses a lower amount of tryp sin activity. Conclusion, The results indicate that phospholipid does not play a prominen t role in synovial fluid's ability to lubricate an artificial bearing. Rath er, the boundary lubricating ability of SF is attributable to lubricin, a m ucinous glycoprotein.