Protein- Polysaccharide Loss during Endochondral Ossification: Immunochemical Evidence

Hirschman, Albert O.; Dziewiatkowski, Dominic D.

doi:10.1126/science.154.3747.393

Cited by 133 publications

(26 citation statements)

References 18 publications

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“…Weinstein, Sachs, and Schubert (25) indicate that di- (27) indicate that the protein moiety of the protein-GAG complexes is indeed decreased or modified in calcifying tissues through the action of proteases (28). One would expect that these processes, and the release of "free" GAG into circulation, would be more evident in very young animals who undergo an almost constant process of remodeling and calcification.…”

Section: Discussionmentioning

confidence: 99%

The glycosaminoglycans of human plasma

Calatroni¹,

Donnelly²,

Ferrante³

1969

J. Clin. Invest.

133

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Section: Discussionmentioning

confidence: 99%

The glycosaminoglycans of human plasma

Calatroni¹,

Donnelly²,

Ferrante³

1969

J. Clin. Invest.

133

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“…There is evidence which suggests that sulfated proteoglycans and glycosaminoglycans inhibit mineralization (7-11). Because of this, it has been proposed that proteolytic degradation of proteoglycans is involved in the conversion of a noncalcifiable matrix into one that is capable of being mineralized (12)(13)(14). Alternatively, it may be that as chondrocytes hypertrophy, they cease to synthesize proteoglycans, or perhaps they synthesize distinct proteoglycans (15) and/or other matrix components with structural characteristics that permit calcification.…”

mentioning

confidence: 99%

Increased calcification of growth plate cartilage as a result of compressive force in vitro

Klein‐Nulend

Veldhuijzen

Burgér

1986

Arthritis & Rheumatism

135

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The influence of intermittent compressive force (ICE') and of continuous compressive force (CCF) on calcification of growth plate cartilage was investigated, using organ cultures of fetal mouse cartilaginous long bone rudiments. Sixteen-day-old metatarsal rudiments, still consisting of uncalcified cartilage, were isolated and cultured for 5 days. Initial calcification of hypertrophic Cartilage occurred under control conditions (atmospheric pressure), and under the influence of ICF or CCF by intermittently or continuously compressing the gas phase above the culture medium. Calcification was monitored by means of 45Ca and 32P incorporation into calcium-phosphate mineral and by morphometric methods. Both ICF and CCF increased cartilage calcification, but ICF was about twice as effective as CCF. Killed rudiiments did not calcify during the culture period, nor did ICF or CCF increase the incorporation of label. The effects of ICF and CCF on calcification could not be mimicked by increasing the Po, and Pcoz levels in the g s phase. The length of the central zone of calcified cartilage was significantly increased by ICF and CCF.W e conclude that hypertrophic chondrocytes respond directly to ICF and CCF by an increased deposition of calcium-phosphate mineral in the matrix. Discontinuous mechanical stimulation evokes a higher cellular response than does continuous stimulation.

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“…The finding of a lower proportion of aggregates in the EDTA-containing dissociative extract (4E) than in the previous extract (4) could possibly indicate a decreased proportion of proteoglycan aggregates in calcified parts of the guinea-pig costal cartilage, as compared to noncalcified parts. This may relate to the suggestions of proteoglycan breakdown in connection with the calcification process [33], and also to the recent reports that aggregate, but not non-aggregate, forms of proteoglycans are able to inhibit mineral growth…”

Section: Associative Gradient Cen Tnfuga Tionmentioning

confidence: 61%

Proteoglycans of Guinea‐Pig Costal Cartilage

Lohmander

1975

European Journal of Biochemistry

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Proteoglycans were extracted, in a yield of about 90%, from costal cartilage of young, growing guinea-pigs. Three solvents were used in sequence: 0.4 M guanidine . HC1, pH 5.8, 4 M guanidine . HCl, pH 5.8, and 4 M guanidine . HCl/O.l M EDTA, pH 5.8. The proteoglycans were purified and fractionated by cesium chloride density gradient ultracentrifugation under associative and dissociative conditions. Gel chromatography on Sepharose 2 B of proteoglycan fractions from associative centrifugations showed the presence of both aggregated and monomer proteoglycans. The ratio of aggregates to monomers was higher in the second extract than in the other two extracts. Dissociative gradient centrifugation gave a similar distribution for proteoglycans from all three extracts. Thus, with decreasing buoyant density there were decreasing ratios of polysaccharide to protein, and of chondroitin sulfate to keratan sulfate. In addition, there was with decreasing density an increasing ratio of chondroitin 4-sulfate to chondroitin 6-sulfate. Amino acid analyses of dissociative fractions were in accordance with previously published results. On comparing proteoglycan monomers of the three extracts, significant differences were found. Proteoglycans, extracted at low ionic strength, contained lower proportions of protein, keratan sulfate, chondroitin 6-sulfate and basic amino acids than those of the second extract. The proteoglycans of the third extract also differed from those of the other extracts.The results indicate that the proteoglycans of guinea-pig costal cartilage exist as a very polydisperse and heterogenous population of molecules, exhibiting variations in aggregation capacity, molecular size, composition of protein core, degree of substitution of the protein core, as well as variability in the type of polysaccharides substituted.The structure of the preoteoglycans of various bovine and porcine hyaline cartilages is rather well known [I -51. Recent work has also, to a large extent, elucidated the role of hyaluronic acid and linking proteins in the aggregation of these molecules [6-121. Since data on proteoglycans of hyaline cartilages of other animals are less abundant, it is, however, difficult to ascertain the more general applicability of the conclusions drawn from the research on bovine and porcine cartilages.This lack of information also makes it difficult to interpret in vivo metabolic studies on proteoglycans, which usually have to be made with smaller laboratory animals. Abbreviations.ECTEOLA-cellulose, epichlorohydrin-triethanolamine-cellulose; CPC-cellulose, cellulose trcatcd with cetyl pyridinium chloride.Enzymcs. Papain (EC 3.4.22.2); chondroittnase ABC (EC 4.2.2.4).The present work was undertaken as part of an investigation on the structure, metabolism, and function of the proteoglycans of guinea-pig hyaline cartilage [I3 -161. The fractionation and chemical characterization of the proteoglycans of guinea-pig costal cartilage are described. Our purpose was to obtain a basis for the subsequent investigation both of t...

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Protein- Polysaccharide Loss during Endochondral Ossification: Immunochemical Evidence

Cited by 133 publications

References 18 publications

The glycosaminoglycans of human plasma

The glycosaminoglycans of human plasma

Increased calcification of growth plate cartilage as a result of compressive force in vitro

Proteoglycans of Guinea‐Pig Costal Cartilage

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