The tensile properties of the cartilage of human femoral condyles related to the content of collagen and glycosaminoglycans

Kempson, G. E.; Muir, Helen; Pollard, Christine D.; Tuke, M A

doi:10.1016/0304-4165(73)90093-7

Cited by 402 publications

(245 citation statements)

References 10 publications

Supporting

Mentioning

221

Contrasting

Unclassified

Order By: Relevance

“…While aggrecan contains most of the chondroitinase ABC-susceptible material of the tissue, depletion of GAG with chondroitinase ABC may alter or displace some of these other chondroitin sulfate-or dermatan sulfate-containing molecules and allow new interactions between collagen fibrils that enhance the tensile integrity of the collagen network. Thus, although the tensile behavior of cartilage in the high-strain region is generally attributed to the tensile response of the collagen network (15,26), these results demonstrate an indirect, but dramatic, contribution of the GAG component.…”

Section: Discussionmentioning

confidence: 77%

“…Chondroitinase ABC specifically depolymerizes chondroitin and dermatan sulfate (22), while collagen, the collagen network arrangement, keratan sulfate, and link protein remain unaffected by the enzyme (23)(24)(25). In response to chondroitinase ABC treatment, altered mechanical properties include a reduction of the initial slope of the stress-strain curve (26,27) and an increase in the overall tensile modulus (28,29). The biologic response of chondrocytes to chondroitinase ABC treatment appears to be minimal; no changes were detected in cell density and volume (30) or in gene expression of certain collagens, aggrecan, and decorin (31).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Mechanisms of cartilage growth: Modulation of balance between proteoglycan and collagen in vitro using chondroitinase ABC

Asanbaeva¹,

Masuda²,

Thonar³

et al. 2007

Arthritis & Rheumatism

View full text Add to dashboard Cite

Objective. To examine the cartilage growthassociated effects of a disruption in the balance between the swelling pressure of glycosaminoglycans (GAGs) and the restraining function of the collagen network, by diminishing GAG content prior to culture using enzymatic treatment with chondroitinase ABC.Methods. Immature bovine articular cartilage explants from the superficial and middle layers were analyzed immediately or after incubation in serumsupplemented medium for 13 days. Other explants were treated with chondroitinase ABC to deplete tissue GAG and also either analyzed immediately or after incubation in serum-supplemented medium for 13 days. Treatment-and incubation-associated variations in tissue volume, contents of proteoglycan and collagen network components, and tensile mechanical properties were assessed.

show abstract

Section: Discussionmentioning

confidence: 77%

mentioning

confidence: 99%

Mechanisms of cartilage growth: Modulation of balance between proteoglycan and collagen in vitro using chondroitinase ABC

Asanbaeva¹,

Masuda²,

Thonar³

et al. 2007

Arthritis & Rheumatism

View full text Add to dashboard Cite

show abstract

“…An indirect, but dramatic contribution of the proteoglycan component to the tensile properties or cartilage has also been demonstrated. Chondroitinase ABC (C-ABC) treatment, which specifically depolymerizes chondroitin and dermatan sulfate GAG chains [10], resulted in a reduction of the initial slope of the stress-strain curve [11,12] and an increase in the overall tensile modulus of cartilage [13][14][15] and tensile strength in tendon [16]. In addition, collagen to proteoglycan ratio correlated strongly with equilibrium tensile modulus of cartilage [17].…”

Section: Introductionmentioning

confidence: 99%

Articular cartilage tensile integrity: Modulation by matrix depletion is maturation-dependent

Asanbaeva

Tam

Schumacher

et al. 2008

Archives of Biochemistry and Biophysics

View full text Add to dashboard Cite

Articular cartilage function depends on the molecular composition and structure of its extracellular matrix (ECM). The collagen network (CN) provides cartilage with tensile integrity, but must also remodel during growth. Such remodeling may depend on matrix molecules interacting with the CN to modulate the tensile behavior of cartilage. The objective of this study was to determine the effects of increasingly selective matrix depletion on tensile properties of immature and mature articular cartilage, and thereby establish a framework for identifying molecules involved in CN remodeling. Depletion of immature cartilage with guanidine, chondroitinase ABC, chondroitinase AC, and Streptomyces hyaluronidase markedly increased tensile integrity, while the integrity of mature cartilage remained unaltered after depletion with guanidine. The enhanced tensile integrity after matrix depletion suggests that certain ECM components of immature matrix serve to inhibit CN interactions and may act as modulators of physiological alterations of cartilage geometry and tensile properties during growth/maturation.

show abstract

“…Articular cartilage is composed of 2 primary matrix proteins, type II collagen and aggrecan, as well as a number of other matrix proteins that provide structural functions such as rigidity, flexibility, and compression damping. In addition, the cartilage matrix influences chondrocyte function through integrin receptor signaling, initiated via ligation of either intact matrix molecules or peptide fragments resulting from proteolytic activity (3).…”

mentioning

confidence: 99%

Characterization of metalloprotease cleavage products of human articular cartilage

Zhen¹,

Brittain²,

Laska³

et al. 2008

Arthritis & Rheumatism

141

130

View full text Add to dashboard Cite

Objective. To identify, characterize, and compare proteolysis peptide products generated by metalloprotease digests of human articular cartilage.Methods. Human articular cartilage was digested by the addition of exogenous metalloproteases, including matrix metalloproteinases 2, 3, 8, 9, 12, and 13 and aggrecanases ADAMTS-4 and ADAMTS-5. Proteolyzed peptide products were identified by proteomics methods using mass spectrometry.Results. Complete sequences of the peptides proteolyzed from human articular cartilage, including Nand C-termini and hydroxylated posttranslational modifications, were determined. A wide variety of peptides, originating from types I, II, and III collagen, biglycan, prolargin, fibromodulin, fibronectin, decorin, cartilage oligomeric matrix protein, cartilage intermediate-layer protein, megakaryocyte-stimulating factor, mimecan, aggrecan, and lumican, was analyzed following metalloprotease digestion. Release of peptides varied as a function of time, enzyme specificity, and abundance. Specific type II collagen peptide biomarkers, including those containing the three-quarter-length fragment cleavage site and those containing the domains for helical peptide of type II collagen and C-telopeptide of type II collagen, were observed after release by selected proteases.Conclusion. The use of intact cartilage instead of purified protein substrates in the assay allowed for the identification of novel potential substrates and cleavage sites for individual enzymes under more physiologically relevant conditions. Characterization of these cartilage matrix peptides may help in the development of pharmacodynamic biomarkers of cartilage degradation, and also may contribute to an understanding of the bioactive peptides important in chondrocyte signaling.Osteoarthritis (OA) and rheumatoid arthritis (RA) are typified by biologic changes in the articular cartilage that lead to cartilage degradation and joint space narrowing (1,2). Articular cartilage is composed of 2 primary matrix proteins, type II collagen and aggrecan, as well as a number of other matrix proteins that provide structural functions such as rigidity, flexibility, and compression damping. In addition, the cartilage matrix influences chondrocyte function through integrin receptor signaling, initiated via ligation of either intact matrix molecules or peptide fragments resulting from proteolytic activity (3).In arthritis, an imbalance of chondrocyte matrix synthesis and degradation leads to a net loss of matrix, and eventually to joint impairment. In OA, the excessive degradation is primarily due to the action of proteases released by chondrocytes, synovial cells, and macrophages (4). Numerous serine proteases and metalloproteases are overexpressed by these cells during the disease process, but specific metalloproteases, including the collagenase matrix metalloproteinase 13 (MMP-13) and the aggrecanase ADAMTS-5, are thought to be especially important for initiating and promoting cartilage matrix degradation in OA (5,6). MMP-13 cleaves type II collage...

show abstract

The tensile properties of the cartilage of human femoral condyles related to the content of collagen and glycosaminoglycans

Cited by 402 publications

References 10 publications

Mechanisms of cartilage growth: Modulation of balance between proteoglycan and collagen in vitro using chondroitinase ABC

Mechanisms of cartilage growth: Modulation of balance between proteoglycan and collagen in vitro using chondroitinase ABC

Articular cartilage tensile integrity: Modulation by matrix depletion is maturation-dependent

Characterization of metalloprotease cleavage products of human articular cartilage

Contact Info

Product

Resources

About