Centrifugal characterization of proteoglycans from various depth layers and weight‐bearing areas of normal and abnormal human articular cartilage

Journal of Orthopaedic Research - Tập 7 Số 3 - Trang 326-334 - 1989
Francisco J. Müller1, Julio C. Pita1, Daniel Manicourt1, Theodore I. Malinin2, John M. Schoonbeck3, Van C. Mow3
1Veterans Administration Medical Center and Arthritis Division, University of Miami School of Medicine, Florida, U.S.A.
2Surgery Dept., University of Miami School of Medicine, Miami, Florida, U.S.A.
3Orthopaedic Research, Columbia University, New York, New York, U.S.A.

Tóm tắt

AbstractUltracentrifugal polydispersity differential [g(S)] distributions were determined for the proteoglycans of various postmortem human articular cartilage samples extracted from six lateral patellar grooves in nondissociative conditions after mild collagenase digestion of the tissue. The samples consisted of 53 slices (250 μm thick), from normal, mildly fibrillated, and extensively ulcerated knee joints. When statistically analyzed in various subgroupings, the obtained average sedimentation coefficients and polydispersity profiles supported the following conclusions: (a) loss of proteoglycan aggregation and sedimentability is confirmed to be a primary sign of cartilage matrix degradation; (b) higher S values for proteoglycans of the high weight (HW)‐bearing areas and lower values for those of the low weight (LW)‐bearing areas were a typical finding in normal cartilage samples; (c) inversion of this pattern was indicative of matrix degradation, suggesting that the HW regions are more affected than the LW‐bearing areas; (d) the average S value distribution across cartilage thickness tended to resemble the corresponding proteoglycan content versus distance from articular surface; and (e) the deepest cartilage layer had, in most cases, the smallest amount of aggregates while the highest average sedimentability was observed at the middle zone of the normal samples. In the discussion, a role of proteoglycan aggregation for providing a means to “pack” more proteoglycans within the collagen meshwork and to control the generation of osmotic pressure gradients is suggested.

Từ khóa


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Thông tin xuất bản

Journal of Orthopaedic Research

Tập 7 Số 3

326-334

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