Proteoglycans of cartilage: An assessment of their structure

Tsiganos, Constantine P.; Hardingham, Timothy E.; Muir, Helen

doi:10.1016/0005-2795(71)90216-9

Cited by 68 publications

(32 citation statements)

References 10 publications

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“…Some of the proteoglycans in cartilage exist as aggregates ; these would be Vol. 130 present amongst the proteoglycans prepared by the procedure used here and would be excluded from Sepharose 4B since they are excluded from Sepharose 2B (Tsiganos et al, 1971). The diminished proportions of proteoglycans excluded from Sepharose 4B in the cartilages of the lame groups (Table 4), particularly at 10 weeks of age, suggest that fewer aggregates were present, either because there was less of the aggregating component or because there was a greater proportion of smaller proteoglycans, which appear to be unable to form aggregates (Hardingham & Muir, 1972).…”

Section: Discussionmentioning

confidence: 99%

Proteoglycans of the knee-joint cartilage of young normal and lame pigs

Šimůnek¹,

Muir²

1972

Biochemical Journal

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Intensive rearing, and restricted activity, induce rapid growth in pigs, but they often become lame. Groups of normal and lame pigs reared intensively were killed when 10 or 25 weeks old. Although there were no differences in the overall composition of the knee-joint cartilage of lame and sound animals, the proteoglycans in the cartilage of the lame pigs were extracted more easily by a standardized sequential procedure and contained a higher proportion of molecules of smaller size as assessed by gel chromatography on 6% agarose and Sepharose 4B. These increased at the expense of both the larger and mediumsized molecules. Differences were most evident at 10 weeks of age, when there was twice as much of the smaller proteoglycans in the cartilage of lame pigs. Despite these size-differences, the compositions of the proteoglycans in corresponding sequential extracts of cartilage of lame and normal groups were the same, as were the changes in chemical composition that accompany development. Proteoglycans from lame animals may have undergone limited proteolysis, thus decreasing their size without changing their composition detectably. As the differences between normal and lame groups were greater at 10 weeks than at 25 weeks of age, the first weeks after birth (when the greatest changes occur in the proteoglycans and in the cartilage) may be a critical period in the maturation of articular cartilage in this species. At this time, rapid gain in weight produced by intensive rearing may be too great for the immature cartilage to bear.

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Section: Discussionmentioning

confidence: 99%

Proteoglycans of the knee-joint cartilage of young normal and lame pigs

Šimůnek¹,

Muir²

1972

Biochemical Journal

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“…The range of densities obtained in several representative experiments is shown in the last column of the table. The relative concentrations of protein and uronate in BCC-SPG in both associative and dissociative gradients follow the general pattern established in severn other studies for cartilage [17,[21][22][23]; the concentration of uronate is greatest in the higher density fractions, and the ratio of uronate to protein decreases with decreasing buoyant densities. This pattern is found for SPG and for the RPG derived from the residue.…”

Section: Resultsmentioning

confidence: 50%

Studies on extractable and resistant proteoglycans from metaphyseal and cortical bone and cartilage

Campo

1981

Calcif Tissue Int

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Soluble proteoglycans (SPG) were extracted from bovine (BCC) and human (HCC) costal cartilages by the dissociative method using 4 M guanidinium chloride (GuHCl). Proteoglycans which are resistant to extraction (RPG) were obtained following collagenase digestion or hydroxylamine treatment of the cartilage residues. Similarly, SPG were extracted from bovine metaphyseal and cortical bone using EDTA. The RPG were extracted from the bones using hydroxylamine. Density gradient fractionation under dissociative conditions of cartilage SPG and RPG followed by chromatography on Sepharose 2B revealed that A1D1 RPG are smaller than the SPG. SPG reacted with either collagenase or hydroxylamine are also smaller than the parent SPG. A1D1 fractions obtained from BCC-SPG and RPG or from mixtures of SPG and acid-soluble collagen are free of hydroxyproline. Hydroxyproline is not completely separated from HCC-RPG. Density gradient fractionation of bone proteoglycans and Sepharose chromatography of the A1 and A1D1 fractions showed that those obtained from metaphysis are larger than those from cortical bone. This was attributed to the presence of calcified cartilage in metaphyseal bone. The A1D1 fractions of the metaphyseal proteoglycans seemed to undergo self-association since this fraction is larger than the A1 fraction from which it is derived. Cortical bone proteoglycans do not behave similarly. Density gradient purification under dissociative conditions failed to separate hydroxyproline from the proteoglycans obtained from bone. It is hypothesized that in bone proteoglycans and collagen might be linked.

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“…However, this sort of argument is almost certainly too simple. Tsiganos et al (1970) report that there is not only an increase of protein, but also of keratan sulphate, towards the top of a caesium chloride gradient of starting density 1.5g/ml. In our case, the small content of hexuronic acid in the glycoproteins may be due to some chondroitin sulphate associated with keratan sulphate.…”

Section: Discussionmentioning

confidence: 96%

The isolation of glycoproteins from bovine achilles tendon and their interaction with collagen

Anderson

Jackson

1972

Biochemical Journal

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Two glycoprotein fractions, A and B, were isolated from bovine achilles tendon. Glycoprotein A was prepared from a 0.2m-sodium chloride extract and glycoprotein B was isolated from a 3m-magnesium chloride extract. They were free from serum proteins. Glycoprotein A was essentially free of collagen, but glycoprotein B contained about 8% collagen. Both glycoproteins gave several bands on isoelectric focusing. This technique was also used to demonstrate that both glycoprotein fractions interacted strongly with acid-soluble calf skin tropocollagen. It is concluded that these fractions are true components of tendon, and that they may have some function in the macromolecular organization of the tissue.

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Proteoglycans of cartilage: An assessment of their structure

Cited by 68 publications

References 10 publications

Proteoglycans of the knee-joint cartilage of young normal and lame pigs

Proteoglycans of the knee-joint cartilage of young normal and lame pigs

Studies on extractable and resistant proteoglycans from metaphyseal and cortical bone and cartilage

The isolation of glycoproteins from bovine achilles tendon and their interaction with collagen

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