Developmental expression of dermatan sulfate proteoglycans in the elastic bovine nuchal ligament

Reinboth, Betty; Finnis, Merran; Gibson, Mark; Sandberg, Lawrence B.; Cleary, Eimear

doi:10.1016/s0945-053x(00)00060-3

Cited by 21 publications

(23 citation statements)

References 53 publications

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“…Biglycan, decorin, tropoelastin, and MAGPs 1 and 2 were purified from the nuchal ligament of 230-day-old fetal calves as described previously (14,16). Bovine pepsin-treated type VI collagen was prepared as described elsewhere (17).…”

Section: Methodsmentioning

confidence: 99%

“…We have previously shown that a specific glucuronate-rich glycoform of biglycan is expressed in nuchal ligament during elastinogenesis, which is very distinct from glycoforms from earlier or later stages in development of the tissue (14). To determine whether biglycan isoforms with different glycosaminoglycan side chains had any influence on binding to tropoelastin, biglycan from the nuchal ligament of 230-day-old fetuses was compared with biglycan derived from adult bovines, which has a much higher iduronate content (Fig.…”

Section: Binding Of Biglycan and Decorin To Elastic Fibermentioning

confidence: 99%

“…Decorin expression was found to peak early in this tissue. However, the expression of a specific glycoform of biglycan correlated with the elastinogenic phase of elastic fiber formation, suggesting a role for biglycan in this stage of the process (14). In the present study we have investigated the interaction of decorin and biglycan glycoforms with the elastin precursor tropoelastin, MAGPs, and isolated fibrillin-containing, elastinassociated microfibrils.…”

mentioning

confidence: 92%

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Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components

Reinboth

Hanssen

Cleary

et al. 2002

Journal of Biological Chemistry

146

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The interactions of the dermatan sulfate proteoglycans biglycan and decorin have been investigated with the elastic fiber components, tropoelastin, fibrillin-containing microfibrils, and microfibril-associated glycoproteins (MAGP) 1 and 2. Both proteoglycans were found to bind tropoelastin and fibrillin-containing microfibrils but not MAGPs 1 and 2 in solid phase binding assays. The specificity of the binding of biglycan and decorin to tropoelastin was confirmed by co-immunoprecipitation experiments and by the blocking of the interactions with elastin-derived peptides. Isolated core proteins from biglycan and decorin bound to tropoelastin more strongly than the intact proteoglycans, and there were no differences in the tropoelastin binding characteristics of distinct glucuronate-rich and iduronate-rich glycoforms of biglycan. These findings indicated that the binding sites were contained in the protein cores of the proteoglycans rather than the glycosaminoglycan side chains. Scatchard analysis showed that biglycan bound more avidly than decorin to tropoelastin with K d values estimated as 1.95 ؋ 10 ؊7 M and 5.3 ؋ 10 ؊7 M, respectively. In blocking experiments each proteoglycan showed extensive inhibition of binding of the other to tropoelastin but was most effective at blocking its own binding. This result suggested that biglycan and decorin had closely spaced but distinct binding sites on tropoelastin. Addition of the elastin-binding protein MAGP-1 to the assays enhanced the binding of biglycan to tropoelastin but had no effect on the decorin-tropoelastin interaction. Co-immunoprecipitation experiments showed that MAGP-1 interacted with biglycan but not decorin in the solution phase. The results indicated that biglycan specifically formed a ternary complex with tropoelastin and MAGP-1. Overall the study supports the concept that biglycan may have a specific role in the elastinogenic phase of elastic fiber formation.

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Section: Methodsmentioning

confidence: 99%

Section: Binding Of Biglycan and Decorin To Elastic Fibermentioning

confidence: 99%

mentioning

confidence: 92%

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Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components

Reinboth

Hanssen

Cleary

et al. 2002

Journal of Biological Chemistry

146

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“…Second, tenascin-X could regulate deposition of elastic fiber components in a more indirect manner. It is thought that proteoglycans play an important role in guiding elastogenesis (75)(76)(77). Proteoglycans are present in the elastic fiber (78), and recent studies have shown binding of tenascin-X to the dermatan sulfate chains of decorin (68) and to heparan sulfate (79).…”

Section: Tenascin-x Deficiency and Elastic Fiber Abnormalitiesmentioning

confidence: 99%

Joint hypermobility syndromes: The pathophysiologic role of tenascin‐X gene defects

Zweers¹,

Hakim²,

Grahame³

et al. 2004

Arthritis & Rheumatism

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“…Specifically, hyaluronan (HA), a non-sulfated GAG, has been implicated in the synthesis and organization of microfibrils (fibrillin), a precursor for elastic fiber deposition [13] and has also been indirectly linked to elastin synthesis through its intimate binding of versican [14]. Via these interactions, HA may associate with microfibrillar proteins (fibulin-1, 2) and elastinassociated proteins to form higher-order macromolecular structures important for elastic fiber assembly [15].…”

Section: Introductionmentioning

confidence: 99%

Impact of delivery mode of hyaluronan oligomers on elastogenic responses of adult vascular smooth muscle cells

2007

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Our prior studies demonstrated that exogenous supplements of pure hyaluronan (HA) tetramers (HA4) dramatically upregulate elastin matrix synthesis by adult vascular smooth muscle cells (SMCs). Some studies suggest that exogenous HA likely only transiently contacts and signals cells, and may elicit different cell responses when presented on a substrate (e.g., scaffold surface). To clarify such differences, we used a carbodiimide-based chemistry to tether HA4 onto glass, and compared elastin matrix synthesis by SMCs cultured on these substrates, with those cultured with equivalent amounts of exogenous HA4. Tethered HA4-layers were first characterized for homogeneity, topography, and hydrolytic stability using SEM, XPS, AFM, and FACE. In general, mode of HA4 presentation did not influence its impact on SMC proliferation, or cell synthesis of tropoelastin and matrix elastin, relative to non-HA controls; however, surface-tethered HA4 stimulated SMCs to generate significantly greater amounts of elastin-stabilizing desmosine crosslinks, which partially accounts for the greater resistance to enzymatic breakdown of elastin derived from these cultures. Elastin derived from both sets of cultures contained peptide masses that correspond to the predominant peptides present in rat aortic elastin. SEM and TEM showed that HA4 stimulated fibrillin-mediated elastin matrix deposition, and organization into fibrils. Surfaceimmobilized HA4 was particularly conducive to organization of elastin into aggregating fibrils, and their networking to form closely-woven sheets of elastin fibers, as seen in cardiovascular tissues. The results suggest that incorporation of elastogenic HA4 mers onto cell culture substrates or scaffolds is a better approach than exogenous supplementation for in vitro or in vivo regeneration of architecturally and compositionally faithful-, and more stable mimics of native vascular elastin matrices.

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Developmental expression of dermatan sulfate proteoglycans in the elastic bovine nuchal ligament

Cited by 21 publications

References 53 publications

Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components

Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components

Joint hypermobility syndromes: The pathophysiologic role of tenascin‐X gene defects

Impact of delivery mode of hyaluronan oligomers on elastogenic responses of adult vascular smooth muscle cells

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