[17] Isolation and characterization of proteoglycans

Heinegård, Dick; Sommarin, Yngve

doi:10.1016/0076-6879(87)44186-4

Cited by 160 publications

(86 citation statements)

References 107 publications

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“…To investigate the effect of non-covalent intermolecular bonds among the extracellular matrix molecules on the tensile integrity of articular cartilage, the specimens were extracted with 4M guanidine HCl (Gnd), a strong chaotrophic agent [47]. The maximum amount of GAG, as measured by hexuronate content, that can be extract with Gnd is ∼85% of total, while the residual ∼15% remains behind with the insoluble matrix [48].…”

Section: Methodsmentioning

confidence: 99%

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

Asanbaeva

Tam

Schumacher

et al. 2008

Archives of Biochemistry and Biophysics

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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.

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Section: Methodsmentioning

confidence: 99%

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

Asanbaeva

Tam

Schumacher

et al. 2008

Archives of Biochemistry and Biophysics

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“…The proteolyzed homogenates were placed in a boiling water bath for 15 min to deactivate the protease and then centrifuged (2500 × g) for 30 min at 4°C. The recovered supernatant was next β-eliminated (modified method from [20]) using sodium borohydride (1% w/v) under mild alkaline conditions (0.2M NaOH at 4°C overnight). After neutralization (with 0.2 M HCl) perchloric acid (75%) was added to obtain a final concentration of 5% v/v.…”

Section: Tissues Processing Isolation and Purification Of Heparan Sumentioning

confidence: 99%

Isolation and characterization of heparan sulfate from various murine tissues

et al. 2006

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Heparan sulfate (HS), is a proteoglycan (PG) found both in the extracellular matrix and on cell surface. It may represent one of the most biologically important glycoconjugates, playing an essential role in a variety of different events at molecular level. The publication of the mouse genome, and the intensive investigations aimed at understanding the proteome it encodes, has motivated us to initiate studies in mouse glycomics focused on HS. The current study is aimed at determining the quantitative and qualitative organ distribution of HS in mice. HS from brain, eyes, heart, lung, liver, kidney, spleen, intestine and skin was purified from 6-8 week old male and female mice. The recovered yield of HS from these organs is compared with the recovered whole body yield of HS. Structural characterization of the resulting HS relied on disaccharide analysis and 1 H-NMR spectroscopy. Different organs revealed a characteristic HS structure. These data begin to provide a structural understanding of the role of HS in cell-cell interactions, cell signaling

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“…A large proportion of the proteoglycans are present as aggregates formed by the non-covalent interaction between proteoglycan monomers and hyaluronate ( Figure 1). The resulting polyanionic supramolecular assemblies have high charge densities and attract large amounts of water, this being crucial for the biomechanical properties of cartilage such as resilience to load (for reviews see [1][2][3][4]). …”

Section: Introductionmentioning

confidence: 99%

Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates

Mörgelin

Paulsson

Aebi

et al. 1995

Biochemical Journal

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Aggregates of proteoglycans from the Swarm rat chondrosarcoma reassembled in vitro have been studied by rotary-shadowing electron microscopy, and shown to be similar to native structures that have never been dissociated [Mörgelin, Engel, Heinegård and Paulsson (1992) J. Biol. Chem. 267, 14275-14284]. A hyaluronate with defined chain length (HAshort) has now been prepared by autoclaving high-Mr hyaluronate and fractionation to a narrow size distribution by gel filtration. Proteoglycan monomers, core protein, hyaluronate-binding region and link protein were combined with HAshort. Free chains of HAshort and reconstituted complexes with proteoglycan, link protein and aggrecan fragments were examined by electron microscopy after rotary shadowing. Length measurements showed that the hyaluronate was condensed to about half of its original length on binding intact aggrecan monomers, any aggrecan fragment or link protein alone. This strongly implies that hyaluronate adopts a defined spatial arrangement within the central filament of the aggregate, probably different from its secondary structure in solution. No differences in length were observed between link-free and link-stabilized aggregates.

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[17] Isolation and characterization of proteoglycans

Cited by 160 publications

References 107 publications

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

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

Isolation and characterization of heparan sulfate from various murine tissues

Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates

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