A model of tenascin‐X integration within the collagenous network

Lethias, Claire; Carisey, Alexandre F.; Comte, Jane; Cluzel, Caroline; Exposito, Jean‐Yves

doi:10.1016/j.febslet.2006.10.037

Cited by 65 publications

(68 citation statements)

References 22 publications

(31 reference statements)

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“…It has been shown in vitro that decorin and tenascin-X interact with the fibrillar collagens (particularly type I) (Svensson et al, 1995;Lethias et al, 2006), and that type XIV collagen interacts with decorin (Font et al, 1996;Ehnis et al, 1997;Elefteriou et al, 2001). Tenascin-X and collagen XIV could modulate the flexibility of the ECM and, as a result, its mechanical properties.…”

Section: Discussionmentioning

confidence: 99%

“…Among them, we can mention collagen XIV, a minor collagen, decorin, a proteoglycan (PG) and tenascin-X, a noncollagenic glycoprotein (Velleman, 2002). They interact with structural collagens and each other (Font et al, 1993;Weber et al, 1996;Elefteriou et al, 2001;Lethias et al, 2006) and are co-localized in perimysium (Listrat). These interactions might have important biological implications on building of extracellular networks, alter flexibility of the ECM and, as a result, its mechanical properties (Nishiyama et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

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New insight of some extracellular matrix molecules in beef muscles. Relationships with sensory qualities

Dubost

Micol

Lethias

et al. 2016

Animal

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The aim of this study was to highlight the relationships between decorin, tenascin-X and type XIV collagen, three minor molecules of extracellular matrix (ECM), with some structural parameters of connective tissue and its content in total collagen, its cross-links (CLs) and its proteoglycans (PGs). In addition, we have evaluated impact of these minor molecules on beef quality traits. The relative abundance of these molecules was evaluated by western blot analysis in Longissimus thoracis (LT) and Biceps femoris (BF) muscles from Aberdeen Angus and Blond d'Aquitaine beef breeds. Decorin and tenascin-X were more abundant in BF than in LT (1.8 v. 0.5 arbitrary units (AU), respectively, P < 0.001, and 1.0 v. 0.6 AU, P < 0.05). There was no muscle effect for collagen XIV content. Decorin and tenascin-X relative abundance were positively correlated with perimysium and endomysium areas and with collagen characteristics (total, insoluble and CLs). Decorin was negatively correlated with total PG content and positively with tenascin-X. Collagen XIV was correlated with any of parameters measured. To assess the impact of decorin, tenascin-X and collagen XIV and of their ratios to total collagen and PGs on shear force and quality traits we realized, respectively, a multiple-linear regression analysis and a Pearson's correlation analysis. Decorin and tenascin-X relative abundance were, respectively, negatively and positively involved in juiciness. Decorin relative abundance was also negatively involved in abnormal flavour and positively in overall liking. The ratio of decorin to total collagen and PGs was negatively correlated to juiciness, together with collagen XIV ratio to total PGs. The ratios of decorin, tenascin-X and collagen XIV to total PGs were positively correlated to sensory tenderness, negatively to abnormal beef flavour and positively to overall liking. The ratio of decorin to total collagen was also negatively correlated to abnormal flavour and positively to overall liking while its ratio to total PGs was positively correlated to beef flavour and overall liking. Results of the present study highlighted for the first time the possible role of minor ECM molecules on beef quality traits. In addition, variations of meat texture and more generally of sensory qualities would depend not only to the quantity of total collagen and of its CLs, but also of components of ECM such as decorin, tenascin-X and collagen XIV and of their ratios to total collagen and PGs.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

New insight of some extracellular matrix molecules in beef muscles. Relationships with sensory qualities

Dubost

Micol

Lethias

et al. 2016

Animal

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“…They interact with other ECM molecules such as decorin (Font et al, 1998) or tenascin-X (Lethias et al, 2006), they promote collagen gel contraction in vitro (Nishiyama et al, 1994), but their respective roles are still unclear. Collagen XII could form flexible bridges between collagen fibrils by interacting with them both directly and indirectly by its binding partners.…”

Section: Collagen XII and Xivmentioning

confidence: 99%

Collagens XII and XIV: Two collagen types both associated with bovine muscle and intramuscular lipid metabolism

et al. 2016

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting galley proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. and CS activities) regardless of breed and muscle, whereas type XIV collagen is associated with the same parameters plus enzymes of glycolytic metabolism that discriminate breeds.

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“…Recombinant full length bovine TNX was produced in mammalian HEK293 cells as previously described [7,10]. TNX was further purified from the culture medium by two chromatographic steps: firstly on heparin-Sepharose (GE Healthcare), and secondly on Q-Sepharose (GE Healthcare) [7].…”

Section: Production and Purification Of Recombinant Tnxmentioning

confidence: 99%

“…This association might be explained by the interaction of TNX with several molecular components of these fibrils i.e. decorin, fibrillar and FACIT collagens [6,7,8]. More recently, it was shown that TNX has elastic properties, due to the extension/refolding of its constitutive FNIII modules [9].…”

Section: Introductionmentioning

confidence: 99%

Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis

Margaron

Bostan

Exposito

et al. 2010

Biophysical Chemistry

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Tenascin-X is an extracellular matrix protein whose absence leads to an Ehlers-Danlos Syndrome in humans, mainly characterised by connective tissue defects including the disorganisation of fibrillar networks, a reduced collagen deposition, and modifications in the mechanical properties of dense tissues. Here we tested the effect of tenascin-X on in vitro collagen fibril formation. We observed that the main parameters of fibrillogenesis were unchanged, and that the diameter of fibrils was not significantly different when they were formed in the presence of tenascin-X. Interestingly, mechanical analysis of collagen gels showed an increased compressive resistance of the gels containing tenascin-X, indicating that this protein might be directly involved in determinating the mechanical properties of collagen-rich tissues in vivo.

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A model of tenascin‐X integration within the collagenous network

Cited by 65 publications

References 22 publications

New insight of some extracellular matrix molecules in beef muscles. Relationships with sensory qualities

New insight of some extracellular matrix molecules in beef muscles. Relationships with sensory qualities

Collagens XII and XIV: Two collagen types both associated with bovine muscle and intramuscular lipid metabolism

Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis

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