Properties of a collagen molecule containing three identical components extracted from bovine articular cartilage

Strawich, E.; Nimni, Marcel E.

doi:10.1021/bi00797a017

Cited by 146 publications

(61 citation statements)

References 33 publications

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“…Likewise, since the proteoglycans were the major components removed by the guanidinium chloride treatment, it is reasonable to consider that their loss was a major cause of the decreased wear resistance. The proteoglycans in vivo are thought to function as a "shock absorber" and as a "filler" that reinforces the fibrous collagen network (17). The results obtained in this study are compatible with this view and indicate that the nonfibrillar matrix constituents contribute to the wear resistance of the tissue by "strengthening" the collagen network.…”

Section: Discussionsupporting

confidence: 83%

Factors influencing articular cartilage wear in vitro

Radin

Swann

Paul

et al. 1982

Arthritis & Rheumatism

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The in vitro wear of articular cartilage in oscillating and impulsively loaded bovine metatarsophalangeal joints was studied. Articular cartilage scarification had little effect on cartilage wear, but stiffening of the subchondral bone with methyl methacrylate greatly increased the rate of cartilage loss, whether or not it had previously been scarified. Glutaraldehyde treatment of articular cartilage for 30 minutes decreased its wear rate. Guanidinium chloride extraction of the cartilage before wear testing caused it to peel off its subchondral bed. This effect could be spared by prior glutaraldehyde fixation.In vivo cartilage fibrillation has been presumed to be one of the first stages of a process that eventually leads to a total loss of cartilage substance, the exposure of the bony subchondral plate, and, finally, an articular surface made up of eburnated bone (1). However, Byers et a1 (2) necessarily progressive, and Bullough et a1 (4) have suggested that the loading characteristics within the joint are important determinants of the pattern of articular cartilage loss. It has also been established that relative stiffness of the underlying subchondral bone plays an important role in determining the behavior of its overlying cartilage (5).Oscillating joints can be worn out in vitro by being subjected to repetitive impulsive loads superimposed upon a static one (6). We previously reported preliminary experiments in which bovine metatarsophalangeal articular cartilage was subjected to glutaraldehyde fixation and wear tested in vitro (7). In these inital tests, we found that glutaraldehyde increased the stiffness of the cartilage and apparently the in vitro cartilage wear as well. In contrast to this, studies by Lipshitz et a1 (8), which used another in vitro wear method in which they rubbed cartilage plugs on glass under static load, showed that formaldehyde fixation decreased cartilage wear. With this new information in mind, we undertook a new series of experiments for 2 reasons: 1) to restudy the effect of glutaraldehyde fixation of articular cartilage on the in vitro wear rate of articular cartilage, and 2) to study the effects of proteoglycan loss, subchondral bone stiffening, and scarification of cartilage as well as the role of synovial fluid on cartilage wear. MATERIALS AND METHODSMetatarsophalangeal joints of adult cows were obtained at the slaughter house and frozen. Such treatment does not affect the mechanical or chemical properties of these tissues (6). When needed, paired joints from each animal were thawed, dissected free of all soft tissue, mounted with methyl methacrylate in metal holders, and subjected

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Section: Discussionsupporting

confidence: 83%

Factors influencing articular cartilage wear in vitro

Radin

Swann

Paul

et al. 1982

Arthritis & Rheumatism

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“…This would tend to support the thesis advanced by Ehrlich et al (12) that autolytic collagen degradation is a major component of the osteoarthritic process, particularly in more severe phases of the disease. Miller and Matukas (26,27) and several subsequent investigators (28,29) have demonstrated that cartilage contains a different genetic species of collagen than that found in skin and bone. The collagen of cartilage (type II) has a number of differences from that found in skin and bone (type I), including an in- Of greater importance than the absolute number, however, is the fact that the hydroxylysine/hydroxyproline ratio does not change with advancing severity of the disease.…”

Section: Discussionmentioning

confidence: 99%

Collagen synthesis in normal and osteoarthritic human cartilage.

Lippiello¹,

Hall²,

Mankin³

1977

J. Clin. Invest.

230

102

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A B S T R A C T Collagen metabolism in osteoarthritic human articular cartilage was compared to that in normal cartilage and was also correlated with the degree of severity of the osteoarthritic lesion as determined by a histological-histochemical grading system.No correlation was apparent between the concentrations of DNA, hydroxyproline, and hydroxylysine and the degree of severity of the osteoarthritic lesion (except in far-advanced lesions). Similarly, there was no correlation in levels of these components in tissues from the normal vs. osteoarthritic group. The similarity of the values of the ratio hydroxylysine/hydroxyproline in osteoarthritic tissue compared with normal, and the lack of variation in these with increasing severity ofthe disease process argues against the possibility that osteoarthritis is associated with a major shift in the synthesis of type II collagen to type I.[3H] Proline incorporation into osteoarthritic cartilage was increased fourfold as compared to normal cartilage and varied with advancing histological-histochemical grade. Measurement of the specific activity of insolubilized hydroxyproline-containing material of the cartilage matrix, as an index of the turnover of collagen, showed a sixfold increase in osteoarthritic cartilage which also varied with grade. These data suggest that collagen synthesis in these tissues is substantially greater than in nonosteoarthritic tissues and varies directly with the severity of the disease process up to a point and then varies inversely as the lesion becomes more severe.

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“…Extraction with 5M guanidine-HCI (Miller, van der Korst, and Sokoloff, 1969), 2M CaCI2, 2M MgCI2 or 6M Urea (Strawich and Nimni, 1971) brought into solution less than 3 per cent. of the collagen of the tissue.…”

Section: Collagenmentioning

confidence: 99%

Biochemistry of articular cartilage. Nature of proteoglycans and collagen of articular cartilage and their role in ageing and in osteoarthrosis.

McDevitt¹

1973

Annals of the Rheumatic Diseases

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Properties of a collagen molecule containing three identical components extracted from bovine articular cartilage

Cited by 146 publications

References 33 publications

Factors influencing articular cartilage wear in vitro

Factors influencing articular cartilage wear in vitro

Collagen synthesis in normal and osteoarthritic human cartilage.

Biochemistry of articular cartilage. Nature of proteoglycans and collagen of articular cartilage and their role in ageing and in osteoarthrosis.

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