Corrigendum to “Molecular Structure and Interaction of Recombinant Human Type XVI Collagen” [J. Mol. Biol. (2004) 339, 835–853]

Kassner, Anja; Tiedemann, Kerstin; Notbohm, Holger; Ludwig, Thomas; Mörgelin, Matthias; Reinhardt, Dieter P.; Chu, Mon‐Li; Brückner, Peter; Grässel, Susanne

doi:10.1016/j.jmb.2004.08.015

Cited by 4 publications

(10 citation statements)

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“…7), in accordance to previously published data on the structure of the entire recombinant collagen XVI (Fig. 8A) (22). In no other eluate fractions, but the one containing the complex of collagen XVI fragment and ␣1␤1 integrin, were tadpole-like structures visualized with a globular head in the size of the ␣1␤1 integrin heterodimer, from which a tail-like rod representing the tryptic collagen XVI fragment protruded (Fig.…”

Section: Resultssupporting

confidence: 91%

“…In contrast, ␣1␤1 integrin binding to homotrimeric collagen I strongly depends on the 4-hydroxyproline content of the collagen ligand (28). In recombinant collagen XVI, about half of the available proline residues in the Y position of the collagenous GXY repeats were hydroxylated (22). Hence, we anticipate a significantly higher affinity for ␣1␤1 integrin binding to authentic collagen XVI in vivo.…”

Section: Discussionmentioning

confidence: 85%

“…By using highly purified recombinant integrins and recombinant collagen XVI (22,23,36), we proved in a cell-free binding assay that integrins ␣1␤1 and ␣2␤1 interact directly with collagen XVI. Furthermore, inhibitory monoclonal antibodies demonstrated that the two integrins utilize the A domains of their ␣ (NC1-11, indicated by boxes).…”

Section: Discussionmentioning

confidence: 94%

“…Hybridoma cells producing mAb 9EG7 against the human integrin ␤1 subunit were provided by Dr. D. Vestweber (University of Münster, Münster, Germany). Generation of antibodies directed against recombinant collagen XVI is described elsewhere (22). Antibodies were purified by affinity chromatography on protein A and G columns according to standard procedures.…”

Section: Methodsmentioning

confidence: 99%

“…The antibody JA221 was biotinylated with a 500-fold molar excess of biotin-hexanoic-N-(hydroxysuccinimidyl) ester (Pierce). Recombinant expression and purification of human collagen XVI and of soluble ␣2␤1 integrin have been described previously (22,23).…”

Section: Methodsmentioning

confidence: 99%

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Collagen XVI Harbors an Integrin α1β1 Recognition Site in Its C-terminal Domains

Eble

Kassner

Niland

et al. 2006

Journal of Biological Chemistry

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Collagen XVI is integrated tissue-dependently into distinct fibrillar aggregates, such as D-banded cartilage fibrils and fibrillin-1-containing microfibrils. In skin, the distribution of collagen XVI overlaps that of the collagen-binding integrins ␣1␤1 and ␣2␤1. Basal layer keratinocytes express integrin ␣2␤1, whereas integrin ␣1␤1 occurs in smooth muscle cells surrounding blood vessels, in hair follicles, and on adipocytes. Cells bearing the integrins ␣1␤1 and ␣2␤1 attach and spread on recombinant collagen XVI. Furthermore, collagen XVI induces the recruitment of these integrins into focal adhesion plaques, a principal step in integrin signaling. Of potential physiological relevance, these integrin-collagen XVI interactions may connect cells with specialized fibrils, thus contributing to the organization of fibrillar and cellular components within connective tissues. In cell-free binding assays, collagen XVI is more avidly bound by ␣1␤1 integrin than by ␣2␤1 integrin. Both integrins interact with collagen XVI via the A domain of their ␣ subunits. A tryptic collagen XVI fragment comprising the collagenous domains 1-3 is recognized by ␣1␤1 integrin. Electron microscopy of complexes of ␣1␤1 integrin with this tryptic collagen XVI fragment or with full-length collagen XVI revealed a unique ␣1␤1 integrin-binding site within collagen XVI located close to its C-terminal end.Collagen XVI belongs to the fibril-associated collagens with interrupted triple helices (FACIT) 3 family of collagens (1, 2) and is composed of 10 collagenous domains, designated as COL1-10, which are flanked by 11 noncollagenous (NC) regions (3). It constitutes a minor component of the extracellular matrices (ECM) of skin and cartilage. Despite its integration into small heterotypic D-banded fibrils of cartilage, collagen XVI is not generally a component of D-banded fibrils, which contain several types of collagens and further constituents, i.e. small leucine-rich proteoglycans and noncollagenous glycoproteins, in an alloy-like mixture (4, 5). In a tissue-specific manner, collagen XVI is incorporated into structurally and functionally discrete matrix aggregates, such as in specialized fibrillin-1-rich microfibrils in skin. Collagen XVI preferentially associates with that part of the microfibrillar apparatus lacking an amorphous elastin core and is localized in the dermal epidermal junction (DEJ) zone of the papillary dermis (4). Here the microfibrils insert perpendicularly into the basement membrane. This location suggests that collagen XVI plays an active role in anchoring microfibrils to basement membranes. Despite its occurrence in the dermis, it is not only produced by fibroblasts but also by keratinocytes, similarly to type VII collagen (6, 7). However, the mechanism by which these collagens are transported across the basement membrane and incorporated into the mesenchymal stroma is yet unknown. Although many matrix proteins self-assemble and thus contribute to the organization of supramolecular networks, cells also affect the architecture ...

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Section: Resultssupporting

confidence: 91%

Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 94%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Collagen XVI Harbors an Integrin α1β1 Recognition Site in Its C-terminal Domains

Eble

Kassner

Niland

et al. 2006

Journal of Biological Chemistry

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Microfibrils at Basement Membrane Zones Interact with Perlecan via Fibrillin-1

Tiedemann

Sasaki

Gustafsson

et al. 2005

Journal of Biological Chemistry

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Mutational defects in fibrillin-rich microfibrils give rise to a number of heritable connective tissue disorders, generally termed microfibrillopathies. To understand the pathogenesis of these microfibrillopathies, it is important to elucidate the supramolecular composition of microfibrils and their interaction properties with extracellular matrix components. Here we demonstrate that the proteoglycan perlecan is an associated component of microfibrils typically close to basement membrane zones. Double immunofluorescence studies demonstrate colocalization of fibrillin-1, the major backbone component of microfibrils, with perlecan in fibroblast cultures as well as in dermal and ocular tissues. Double immunogold labeling further confirms colocalization of perlecan to microfibrils in various tissues at the ultrastructural level. Extraction studies revealed that perlecan is not covalently associated with microfibrils. High affinity interactions between fibrillin-1 and perlecan were found by kinetic binding studies with dissociation constants in the low nanomolar range. A detailed mapping study of the interaction epitopes by solid phase binding assays primarily revealed interactions of perlecan domains I and II with a central region of fibrillin-1. Analysis of perlecan null embryos showed less microfibrils at the dermal-epidermal junction as compared with wild-type littermates. The data presented indicate a functional significance for perlecan in anchoring microfibrils to basement membranes and in the biogenesis of microfibrils.

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Epidermolysis bullosa – a group of skin diseases with different causes but commonalities in gene expression

Knaup

Verwanger

Gruber

et al. 2012

Experimental Dermatology

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Epidermolysis bullosa (EB) is a group of hereditary skin disorders. Although each subtype is caused by mutations in genes encoding differentially located components of the skin, the resulting phenotype is similar. In this study, we investigated similarities in the gene expression profiles of each subtype on mRNA level. Type XVI collagen (COL16A1), G0/G1 switch 2 (G0S2), fibronectin (FN1), ribosomal protein S27A (RPS27A) and low density lipoprotein receptor (LDLR) were shown to exhibit corresponding changes in gene expression in all three EB subtypes. While COL16A1, G0S2 and FN1 are up-regulated, LDLR and RPS27A mRNA levels are decreased. These data indicate that EB cells seem to take measures increasing their mechanical stability. Apoptosis is likely to be exacerbated, and migratory potential appears to be elevated. Protein degradation is hampered, and the release of fatty acids and glycerol is restricted, probably to save energy. These commonalities might benefit existing EB treatment strategies or could help to reveal new starting points for the treatment of EB in the future.

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Corrigendum to “Molecular Structure and Interaction of Recombinant Human Type XVI Collagen” [J. Mol. Biol. (2004) 339, 835–853]

Cited by 4 publications

References 0 publications

Collagen XVI Harbors an Integrin α1β1 Recognition Site in Its C-terminal Domains

Collagen XVI Harbors an Integrin α1β1 Recognition Site in Its C-terminal Domains

Microfibrils at Basement Membrane Zones Interact with Perlecan via Fibrillin-1

Epidermolysis bullosa – a group of skin diseases with different causes but commonalities in gene expression

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