The British Journal of Rheumatology, Vol 37, 532-538, Copyright © 1998 by British Society for Rheumatology
BA Hills and K Thomas
It was proposed some years ago that, in osteoarthritis, one source of joint
stiffness arises from 'articular gelling', but, if so, why does this not
occur in the normal joint? In a preliminary experiment using agar gels, it
is shown how such fusion of gel surfaces can be inhibited by surface-active
phospholipid (SAPL)--both synthetic and human--as quantified by the shear
stress needed to cause cleavage between samples after prolonged contact. On
the other hand, normal bovine articular cartilage (BAC) does not fuse to
itself, but can be made to do so if rinsed with a powerful lipid solvent
known to remove the outermost layer of adsorbed SAPL along with the
hydrophobicity so characteristic of the normal 'waxy' surface it imparts.
It is then shown how the inhibition of gel fusion can be restored by
treating both bovine and human articular surfaces with exogenous SAPL
derived from human AC and with synthetic SAPL. Samples of human articular
cartilage excised from osteoarthritic hips and knees during total joint
replacement showed a 55% greater tendency to fuse together than normal BAC.
This was exacerbated by solvent rinsing and can be attributed to a
deficiency in the outermost lining of SAPL previously studied as a
load-bearing boundary lubricant capable of reducing friction and wear to
the remarkably low levels observed physiologically. Hence, joint stiffness
can be attributed, in part, to a deficiency in the lubricating layer of
SAPL lining the normal articular surface where it can inhibit articular
gelling/gel fusion, possibly imparting other desirable physiological
functions. The possibility of clinical replenishment of SAPL in the
osteoarthritic joint is discussed.
ORIGINAL PAPERS
Joint stiffness and 'articular gelling': inhibition of the fusion of articular surfaces by surfactant
Paediatric Respiratory Research Centre, Mater Children's Hospital, Brisbane, Queensland, Australia.
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