Chondroitin Sulfate Perlecan Enhances Collagen Fibril Formation

Kvist, Alexander J.; Johnson, Anna E.; Mörgelin, Matthias; Gustafsson, Erika; Bengtsson, Eva; Lindblom, Karin; Aszódi, Attila; Fässler, Reinhard; Sasaki, Takako; Timpl, Rupert; Aspberg, Anders

doi:10.1074/jbc.m607892200

Cited by 95 publications

(74 citation statements)

References 48 publications

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“…Also, the concentration of Col I affects strongly fibril formation as found previously [40,41]. Presumably CS binds to collagen molecules and facilitates the organization of mature fibrils by increasing collagen concentration as it was found in the presence of 4,6-disulfated disaccharides structures, previously [38]. In line with this, here a pronounced fibril formation in both nCS and oCS-based PEMs was observed, when more Col I was adsorbed, which showed also a specific network-like organization as in connective tissue.…”

Section: Physicochemical Characterization Of Polyelectrolyte Multilaysupporting

confidence: 66%

“…Conversely, rather sparse and short fibrils were observed in both nHA and oHA-containing PEMs, where Col I seemed to form rather discrete aggregates than fibers. Col I fibrillogenesis is a sophisticated process highly affected by environmental factors, such as pH, electrolyte type and collagen concentration, but also on the presence of GAG like CS and other naturally occurring polyanions [37,38]. In general, at pH value <5.5 Col I forms more globular structures, while at pH value >5.5 normally fibrillogenesis is supported [39].…”

Section: Physicochemical Characterization Of Polyelectrolyte Multilaymentioning

confidence: 99%

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Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

et al. 2016

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T. (2016) Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells. Acta Biomaterialia, 41, pp. 86-99. (doi:10.1016Biomaterialia, 41, pp. 86-99. (doi:10. /j.actbio.2016 This is the author's final accepted version.There may be differences between this version and the published version. You are advised to consult the publisher's version if you wish to cite from it.http://eprints.gla.ac.uk/119626/ AbstractThe effect of molecular composition of multilayers, by pairing type I collagen (Col I) with either hyaluronic acid (HA) or chondroitin sulfate (CS) was studied regarding the osteogenic differentiation of adhering human adipose-derived stem cells (hADSCs). Multilayer (PEM)formation was based primarily on ion pairing and on additional intrinsic cross-linking through imine bond formation replacing native by oxidized HA (oHA) or CS (oCS) with Col I.Significant amounts of Col I fibrils were found on both native and oxidized CS-based PEMs, resulting in higher water contact angles and surface potential under physiological condition, while much less organized Col I was detected in either HA-based multilayers, which were more hydrophilic and negatively charged. An important finding was that hADSCs remodeled Col I at the terminal layers of PEMs by mechanical reorganization and pericellular proteolytic degradation, being more pronounced on CS-based PEMs. This was in accordance with the higher quantity of Col I deposition in this system, accompanied by more cell spreading, focal adhesions (FA) formation and significant α2β1 integrin recruitment compared to HA-based PEMs. Both CS-based PEMs caused also an increased fibronectin (FN) secretion and cell growth. Furthermore, significant calcium phosphate deposition, enhanced ALP, Col I and Runx2 expression were observed in hADSCs on CS-based PEMs, particularly on oCS-containing one. Overall, multilayer composition can be used to direct cell-matrix interactions, and hence stem cell fates showing for the first time that PEMs made of biogenic polyelectrolytes undergo significant remodeling of terminal protein layers, which enables cells to form a more adequate extracellular matrix-like environment.

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Section: Physicochemical Characterization Of Polyelectrolyte Multilaysupporting

confidence: 66%

Section: Physicochemical Characterization Of Polyelectrolyte Multilaymentioning

confidence: 99%

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

et al. 2016

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“…More recently, it has been shown that the chondroitin sulfate side chains of perlecan, but not its heparan sulfate chains, will promote collagen fibrillogenesis in vitro. These chondroitin sulfate chains differ from those found on aggrecan, which are inert with regard to fibrillogenesis and essentially lack the incorporation of chondroitin sulfate E type oversulfated disaccharides (25) as found in perlecan chondroitin sulfate chains.…”

mentioning

confidence: 77%

COMP Acts as a Catalyst in Collagen Fibrillogenesis

Halász

Kassner²,

Mörgelin

et al. 2007

Journal of Biological Chemistry

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273

220

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We have previously reported that COMP (cartilage oligomeric matrix protein) is prominent in cartilage but is also present in tendon and binds to collagens I and II with high affinity. Here we show that COMP influences the fibril formation of these collagens. Fibril formation in the presence of pentameric COMP was much faster, and the amount of collagen in fibrillar form was markedly increased. Monomeric COMP, lacking the N-terminal coiled-coil linker domain, decelerated fibrillogenesis. The data show that stimulation of collagen fibrillogenesis depends on the pentameric nature of COMP and not only on collagen binding. COMP interacts primarily with free collagen I and II molecules, bringing several molecules to close proximity, apparently promoting further assembly. These assemblies further join in discrete steps to a narrow distribution of completed fibril diameters of 149 ؎ 16 nm with a banding pattern of 67 nm. COMP is not found associated with the mature fibril and dissociates from the collagen molecules or their early assemblies. However, a few COMP molecules are found bound to more loosely associated molecules at the tip/end of the growing fibril. Thus, COMP appears to catalyze the fibril formation by promoting early association of collagen molecules leading to increased rate of fibrillogenesis and more distinct organization of the fibrils.

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“…Collagen Fibrillogenesis Assay-The assays were performed as described previously (29). Pepsin-extracted acid-solubilized collagen (Vitrogen) was neutralized and diluted (167 pM) in 150 mM NaCl, 20 mM HEPES, pH 7.4, with decorin or mutated decorins at 4°C.…”

Section: Methodsmentioning

confidence: 99%

The Decorin Sequence SYIRIADTNIT Binds Collagen Type I

Kalamajski

Aspberg

Oldberg

2007

Journal of Biological Chemistry

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Decorin belongs to the small leucine-rich repeat proteoglycan family, interacts with fibrillar collagens, and regulates the assembly, structure, and biomechanical properties of connective tissues. The decorin-collagen type I-binding region is located in leucine-rich repeats 5-6. Site-directed mutagenesis of this 54-residue-long collagen-binding sequence identifies Arg-207 and Asp-210 in leucine-rich repeat 6 as crucial for the binding to collagen. The synthetic peptide SYIRIADTNIT, which includes Arg-207 and Asp-210, inhibits the binding of full-length recombinant decorin to collagen in vitro. These collagen-binding amino acids are exposed on the exterior of the ␤-sheet-loop structure of the leucine-rich repeat. This resembles the location of interacting residues in other leucine-rich repeat proteins.Decorin is an extracellular matrix proteoglycan involved in collagen type I fibril formation and collagen matrix assembly in a wide range of connective tissues (1-3). Decorin belongs to the small leucine-rich repeat proteoglycan family (SLRPs) 2 (4), which also includes, for example, biglycan (5), fibromodulin (6), lumican (7), and asporin (8, 9). The decorin core protein is composed of 12 tandem leucine-rich repeats (LRRs), each containing an average of 24 amino acid residues. The decorin threedimensional structure, resolved by x-ray crystallography, reveals an arch-shaped molecule with LRRs composed of parallel ␤-sheets on the concave surface and short ␤-strands, 3 10 helices, and polyproline II helices on the convex face (10). Close to the N terminus, decorin is substituted with a single chondroitin or dermatan sulfate chain. Decorin also has three potential consensus sites for N-glycosylation in the LRR domain (4).Several SLRPs are involved in the regulation of collagen fibril formation and matrix assembly, as demonstrated in SLRP-deficient mice (11). Decorin deficiency causes skin fragility (12); biglycan-deficient mice suffer from reduced bone mass and osteoarthritis (13); lack of fibromodulin results in weaker tendons and ligaments, causing osteoarthritis (14); and lumican ablation correlates with corneal opacity (15). In all these cases, ultrastructural imaging reveals abnormally developed collagen fibrils.Decorin presumably affects the lateral association of collagen type I fibrils in vitro as it binds to collagen monomers and delays their accretion to the growing fibrils (1). Collagen fibrils in the skin of decorin-deficient mice are thicker and irregularly shaped, in contrast to smaller, uniform fibrils formed in wild type mice (12). Decorin binds near the C terminus of collagen, close to an intermolecular cross-linking site (16), and seems to have a tutelary function in collagen fibril assembly, which is important for the collagen cross-linking. In addition, decorin also binds collagen type VI (17), transforming growth factor-␤ (18), fibronectin (19), and epidermal growth factor receptor (20).The precise decorin-binding site for collagen has not been determined. An early study identified two collagen-bin...

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Chondroitin Sulfate Perlecan Enhances Collagen Fibril Formation

Cited by 95 publications

References 48 publications

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

COMP Acts as a Catalyst in Collagen Fibrillogenesis

The Decorin Sequence SYIRIADTNIT Binds Collagen Type I

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