Age-related changes in the chemical composition of bovine articular cartilage. The structure of high-density proteoglycans

Garg, Hari G.; Swann, David A.

doi:10.1042/bj1930459

Cited by 46 publications

(11 citation statements)

References 39 publications

(31 reference statements)

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“…The amount of link protein in A1 samples was determined by RIA following severe pretreatment in SDS and the molar content calculated assuming a Mw of 40,000 for link protein. Samples from 5 , 8,16,20,50, and 100 week old rabbits contained 10.2, 11.8, 7.1, 16.8, 14.1, and 12.4 nmol of LP/g of wet weight of cartilage, respectively, in good agreement with data shown in Table 1.…”

Section: Molar Ratio Of Proteoglycan and Link Protein Content In Rabbsupporting

confidence: 85%

“…Samples from 5 , 8,16,20,50, and 100 week old rabbits contained 10.2, 11.8, 7.1, 16.8, 14.1, and 12.4 nmol of LP/g of wet weight of cartilage, respectively, in good agreement with data shown in Table 1.…”

Section: Molar Ratio Of Proteoglycan and Link Protein Content In Rabbsupporting

confidence: 81%

“…Finally, the molar ratio (nmol of LP:nmol of aggregating monomer) was calculated as 0.94, 1.05, 0.59, 1.12, 0.90, and 0.81 at 5 , 8,16,20,50, and 100 weeks, respectively.…”

Section: Molar Ratio Of Proteoglycan and Link Protein Content In Rabbmentioning

confidence: 99%

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The effect of maturation and aging on the structure and content of link proteins in rabbit articular cartilage

Flannery

Urbanek

Sandy

1990

Journal Orthopaedic Research

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We have examined extracts of articular cartilage from rabbits aged 3-100 weeks for evidence of age-related changes in the structure and content of link protein (LP) in this tissue, with the following findings: (a) Two major molecular weight forms of LP were seen on SDS-PAGE (41 and 48 kDa) and the proportion of these changed markedly with age. The 48 kDa species was predominant in young animals (representing about 78% of the total LP at 5 weeks) whereas the 41 kDa species increased in amount with age (representing 35% of the total LP at 100 weeks). A minor form of about 43 kDa, representing less than 20% of the total, was present only during the growth phase. A small amount of fragmented link protein (less than 5% of the total) of about 25-30 kDa was present in samples from mature and aged rabbits only. (b) The quantitation of LP in guanidinium: HCl extracts of cartilage, by radioimmunoassay with monoclonal antibody 8-A-4, was markedly influenced by the conditions of preparation and pretreatment of samples. Assays of dialyzed guanidine extracts following treatment at 80 degrees C for 15 min in 0.025% (w/v) SDS indicated that immature and mature cartilage contains about 50 and 180 micrograms of LP/g of tissue, respectively. On the other hand, assays following treatment at 100 degrees C for 20 min in 0.1% (w/v) SDS suggested that rabbit cartilage contains about 300 micrograms of LP/g of tissue at all ages; finally, assay of CsCl purified proteoglycan samples under these conditions indicated a content of about 500 micrograms of LP/g at all ages. (c) Calculations based on the analysis of proteoglycan preparations for aggregating monomer and link protein suggest that a LP:aggregating monomer molar ratio of about 0.9 is maintained in the articular cartilage throughout maturation and aging in the rabbit.

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Section: Molar Ratio Of Proteoglycan and Link Protein Content In Rabbsupporting

confidence: 85%

Section: Molar Ratio Of Proteoglycan and Link Protein Content In Rabbsupporting

confidence: 81%

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The effect of maturation and aging on the structure and content of link proteins in rabbit articular cartilage

Flannery

Urbanek

Sandy

1990

Journal Orthopaedic Research

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“…Such changes in proteoglycan structure are not unique to the human, but have also been shown in a variety of animals (10)(11)(12)(13)(14)(15)(16). Again, the changes in glycosylation appear to be predominant between birth and the end of growth (17).…”

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confidence: 93%

The Structure and Abundance of Cartilage Proteoglycans during Early Development of the Human Fetus

Roughley

White

Glant³

1987

Pediatr Res

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ABSTRACT. Proteoglycan was isolated from the epiphyseal cartilage of the knee joint from human fetuses, ranging in age from 11 to 19 wk of gestation. The content of proteoglycan, per wet weight of cartilage, increased with gestational age, and structural changes were observed in the proteoglycan subunits, particularly with respect to hydrodynamic size and the position of sulfation of the chondroitin sulfate chains. While 6-sulfation remained fairly constant on about half the disaccharide residues during the age period examined, the proportion of nonsulfated residues decreased with gestational age and there was a corresponding increase in the proportion of 4-sulfated residues. Other structural parameters showed little change, and after 11 wk of gestation the majority of proteoglycan subunits were able to interact with hyaluronic acid to form aggregates. Link proteins were detected in the cartilage at all ages and their abundance increased with age relative to other cartilage proteins. They showed little change in structural heterogeneity, with the two larger molecular forms predominating. In contrast to the proteoglycans, cartilage proteins were in high abundance at 11 wk of gestation, but decreased considerably with time, although there was little change in the relative proportion of the majority of the components. (Pediatr Res 22: [409][410][411][412][413]1987) Abbreviation SDS, sodium dodecyl sulfateHyaline cartilage is best depicted as a solution of proteoglycan and matrix proteins entrapped within a network of collagen fibrils containing a sparse population of cells. The composition of the extracellular matrix is not constant throughout life, and this is particularly true for the proteoglycan, whose structure shows considerable variation. In the human the major changes after birth take place in the first two decades of life (I), representing the period of skeletal development. They are typified by a decrease in the size of the proteoglycan subunit, a decrease in both the size and number of chondroitin sulfate chains, and an increase in the size and number of keratan sulfate chains (2, 3). This latter change occurs concomitantly with a decrease in the number of 0-linked oligosaccharides (4, 5). Such changes in

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“…Mature and immature joints are compared to explore whether significant differences may arise due to the well-recognized evolution in material properties (Kempson, 1991; Williamson et al, 2003) and composition (Front et al, 1989; Garg and Swann, 1981; Wachtel et al, 1995) with age. The strain measurement method employed in this study, which uses digital image correlation, builds upon our earlier application in the study of cartilage explants under static loading (Wang et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Two-dimensional strain fields on the cross-section of the bovine humeral head under contact loading

Canal

Hung

Ateshian

2008

Journal of Biomechanics

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The objective of this study was to provide a detailed experimental assessment of the two-dimensional cartilage strain distribution on the cross-section of immature and mature bovine humeral heads subjected to contact loading at a relatively rapid physiological loading rate. Six immature and six mature humeral head specimens were loaded against glass and strains were measured at the end of a 5 s loading ramp on the textured articular cross-section using digital image correlation analysis. The primary findings indicate that elevated tensile and compressive strains occur near the articular surface, around the center of the contact region. Few qualitative or quantitative differences were observed between mature and immature joints. Under an average contact stress of ~1.7 MPa, the peak compressive strains averaged −0.131 ± 0.048, which was significantly less than the relative change in cartilage thickness, −0.104 ± 0.032 (p < 0.05). The peak tensile strains were significantly smaller in magnitude, at 0.0325 ± 0.013. These experimental findings differ from a previous finite element analysis of articular contact, which predicted peak strains at the cartilage-bone interface even when accounting for the porous-hydrated nature of the tissue, its depth-dependent inhomogeneity, and the disparity between its tensile and compressive properties. These experimental results yield new insights into the local mechanical environment of the tissue and cells, and suggest that further refinements are needed in the modeling of contacting articular layers.

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Age-related changes in the chemical composition of bovine articular cartilage. The structure of high-density proteoglycans

Cited by 46 publications

References 39 publications

The effect of maturation and aging on the structure and content of link proteins in rabbit articular cartilage

The effect of maturation and aging on the structure and content of link proteins in rabbit articular cartilage

The Structure and Abundance of Cartilage Proteoglycans during Early Development of the Human Fetus

Two-dimensional strain fields on the cross-section of the bovine humeral head under contact loading

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