The matrilins: Modulators of extracellular matrix assembly

Klatt, Andreas R.; Becker, Ann-Kathrin A.; Neacsu, Cristian Dan; Paulsson, Mats; Wagener, Raimund

doi:10.1016/j.biocel.2010.12.010

Cited by 109 publications

(128 citation statements)

References 113 publications

Supporting

Mentioning

125

Contrasting

Unclassified

Order By: Relevance

“…It revealed two sequence stretches with homology to the group of von Willebrand factor type A (VWA) domains (Pfam PF00092) with B25% sequence identity andB50% homology to other members of this group, including the von Willebrand factor A3 domain or the I-domains of integrins. VWA domain containing proteins of the blood plasma or the extracellular matrix are often involved in protein-protein interactions including binding of collagen [12][13][14][15] . In case of the von Willebrand factor, binding to partner proteins like glycoprotein Ib or collagen is dependent on conformational changes upon shear forces 16,17 .…”

mentioning

confidence: 99%

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

et al. 2014

View full text Add to dashboard Cite

Blue mussels adhere to surfaces by the byssus, a holdfast structure composed of individual threads representing a collagen fibre reinforced composite. Here, we present the crystal structure and function of one of its matrix proteins, the proximal thread matrix protein 1, which is present in the proximal section of the byssus. The structure reveals two von Willebrand factor type A domains linked by a two-b-stranded linker yielding a novel structural arrangement. In vitro, the protein binds heterologous collagens with high affinity and affects collagen assembly, morphology and arrangement of its fibrils. By providing charged surface clusters as well as insufficiently coordinated metal ions, the proximal thread matrix protein 1 might interconnect other byssal proteins and thereby contribute to the integrity of the byssal threads in vivo. Moreover, the protein could be used for adjusting the mechanical properties of collagen materials, a function likely important in the natural byssus.

show abstract

mentioning

confidence: 99%

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

et al. 2014

View full text Add to dashboard Cite

show abstract

“…In agreement with this notion, we presented evidence here that the mostly non-collagenous components of collagen-containing fibrils in cartilage contain the relevant binding sites for integrins. Molecular candidates include collagen VI and microfibrils containing collagen VI [24], matrilins [11], COMP (thrombospondin 5) [13], and several SLRPs (decorin, fibromodulin, lumican) [44]. Many of these macromolecules have been associated also with a biomechanical role in cartilage (for review see [12]).…”

Section: Binding Of α1-or α2-integrin I-domains To Authentic Cartilagmentioning

confidence: 99%

“…Their properties strongly depend on their composition in terms of, both, collagens and non-collagenous molecules (e.g. COMP, matrilins, decorin, fibromodulin, lumican, perlecan, and collagen VI-containing microfibrils) [8][9][10][11][12][13]. In cartilage fibrils, for example, the inclusion of collagen XI as a fibrillar nucleus is vital for the incorporation of the main component, collagen II [14,15].…”

Section: Introductionmentioning

confidence: 99%

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

et al. 2017

View full text Add to dashboard Cite

Interactions of cells with supramolecular aggregates of the extracellular Matrix (ECM) are mediated, in part, by cell surface receptors of the integrin family. These are important molecular components of cell surfacesuprastructures regulating cellular activities in general. A subfamily of β1-integrins with von Willebrand-factor A-like domains (I-domains) in their α-chains can bind to collagen molecules and, therefore, are considered as important cellular mechano-receptors. Here we show that chondrocytes strongly bind to cartilage collagens in the form of individual triple helical molecules but very weakly to fibrils formed by the same molecules.We also find that chondrocyte integrins α1β1-, α2 β1-and α10β1-integrins and their I-domains have the same characteristics. Nevertheless we find integrin binding to mechanically generated cartilage fibril fragments, which also comprise peripheral non-collagenous material. We conclude that cell adhesion results from binding of integrin-containing adhesion suprastructures to the non-collagenous fibril periphery but not to the collagenous fibril cores. The biological importance of the well-investigated recognition of collagen molecules by integrins is unknown. Possible scenarios may include fibrillogenesis, fibril degradation and/orphagocytosis, recruitment of cells to remodeling sites, or molecular signaling across cytoplasmic membranes. In these circumstances, collagen molecules may lack a fibrillar organization. However, other processes requiring robust biomechanical functions, such as fibril organization in tissues, cell division, adhesion, or migration, do not involve direct integrin-collagen interactions.

show abstract

“…Major typical morphological changes are the progressive accumulation of extracellular matrix (ECM) proteins in mesangial interstitial space to lead to glomerular and tubular basement membrane thickening and increase of mesangial matrix, ultimately resulting in glomerulosclerosis and tubulointerstitial fibrosis. ECM is a potential protein source of diagnostic biomarkers for renal fibrosis [1,2], and among a large number of ECM proteins, Matrilin is a novel filamentous-forming adapter protein family, which can form collagen-dependent and -independent network of extracellular matrix [3][4][5]. Matrilin-2 is the largest member of the Matrilin family that shares von Willebrand factor A (vWFA) domains, epithelial growth factor (EGF) like repeats, and a series of heptad repeats at their C-terminal coiled-coil domain [6,7].…”

Section: Introductionmentioning

confidence: 99%

High glucose-induced Matrilin-2 expression in mouse mesangial cells was mediated by transforming growth factor beta 1 (TGF-β1)

Zhang

Huang

et al. 2016

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

The matrilins: Modulators of extracellular matrix assembly

Cited by 109 publications

References 113 publications

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils

High glucose-induced Matrilin-2 expression in mouse mesangial cells was mediated by transforming growth factor beta 1 (TGF-β1)

Contact Info

Product

Resources

About