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

Eble, Johannes A.; Kassner, Anja; Niland, Stephan; Mörgelin, Matthias; Grifka, Joachim; Grässel, Susanne

doi:10.1074/jbc.m509942200

Cited by 50 publications

(42 citation statements)

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“…In vitro studies have, furthermore, suggested that α1β1 prefers the monomeric form of collagen I to the fibrillar forms that are present in mature connective tissues (Jokinen et al, 2004). It is possible that contacts with mature fibrillar collagen I matrices are enabled through binding to fibril associated collagens with interrupted triple helices (FACIT) collagens, such as collagen XVI (Eble et al, 2006). Various laminin isoforms also serve as good ligands for α1β1 (Barczyk et al, 2010).…”

Section: Integrin α1β1mentioning

confidence: 99%

The integrin–collagen connection – a glue for tissue repair?

Zeltz

Gullberg

2016

Journal of Cell Science

177

126

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There was an error published in J. Cell Sci. 129, 653-664.In Fig. 2A, the fibroblasts were incorrectly labelled. The correct annotation should have been α11 −/− fibroblast (left) and α11 +/+ fibroblast (right). The correct Fig. 2 is shown below. We apologise to the readers for any confusion that this error might have caused. Journal of Cell Science COMMENTARYThe integrin-collagen connection -a glue for tissue repair?Cedric Zeltz and Donald Gullberg* ABSTRACTThe α1β1, α2β1, α10β1 and α11β1 integrins constitute a subset of the integrin family with affinity for GFOGER-like sequences in collagens.Integrins α1β1 and α2β1 were originally identified on a subset of activated T-cells, and have since been found to be expressed on a number of cell types including platelets (α2β1), vascular cells (α1β1, α2β1), epithelial cells (α1β1, α2β1) and fibroblasts (α1β1, α2β1).Integrin α10β1 shows a distribution that is restricted to mesenchymal stem cells and chondrocytes, whereas integrin α11β1 appears restricted to mesenchymal stem cells and subsets of fibroblasts. The bulk of the current literature suggests that collagen-binding integrins only have a limited role in adult connective tissue homeostasis, partly due to a limited availability of cell-binding sites in the mature fibrillar collagen matrices. However, some recent data suggest that, instead, they are more crucial for dynamic connective tissue remodeling events -such as wound healing -where they might act specifically to remodel and restore the tissue architecture. This Commentary discusses the recent development in the field of collagen-binding integrins, their roles in physiological and pathological settings with special emphasis on wound healing, fibrosis and tumor-stroma interactions, and include a discussion of the most recently identified newcomers to this subfamilyintegrins α10β1 and α11β1.

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Section: Integrin α1β1mentioning

confidence: 99%

The integrin–collagen connection – a glue for tissue repair?

Zeltz

Gullberg

2016

Journal of Cell Science

177

126

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“…Collagen XVI, which was the most highly expressed transcript, is a member of the fibril-associated collagens with interrupted triple helices (FACIT-collagens) (Myers et al, 1994). Of potential physiological relevance, collagen XVI and collagen-binding integrin interactions may connect cells with specialized fibrils, contributing to the organization of fibrillar and cellular components within connective tissues (Eble et al, 2006). Collagen types I and III represent the major fibrillar collagen types in skin, and are possibly regulated by transforming growth factor (TGF)-β1, which is known to be the prototype of a large super family of proteins that control various aspects of differentiation (Heine et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

De-novo characterization of the soft-shelled turtle Pelodiscus sinensis transcriptome using Illumina RNA-Seq technology

Wang

et al. 2013

J. Zhejiang Univ. Sci. B

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Abstract:The soft-shelled turtle Pelodiscus sinensis is a high-profile turtle species because of its nutritional and medicinal value in Asian countries. However, little is known about the genes that are involved in formation of their nutritional quality traits, especially the molecular mechanisms responsible for unsaturated fatty acid and collagen biosynthesis. In the present study, the transcriptomes from six tissues from Pelodiscus sinensis were sequenced using an Illumina paired-end sequencing platform. We obtained more than 47 million sequencing reads and 73 954 unigenes with an average size of 754 bp by de-novo assembly. In total, 55.19% of the unigenes (40 814) had significant similarity with proteins in the National Center of Biotechnology Information (NCBI) non-redundant protein database and Swiss-Prot database (E-value <10 −5 ). Of these annotated unigenes, 9 156 and 11 947 unigenes were assigned to 52 gene ontology categories (GO) and 25 clusters of orthologous groups (COG), respectively. In total, 26 496 (35.83%) unigenes were assigned to 242 pathways using the Kyoto Encyclopedia of Genes and Genomes pathway database (KEGG). In addition, we found a number of highly expressed genes involved in the regulation of P. sinensis unsaturated fatty acid biosynthesis and collagen formation, including desaturases, growth factors, transcription factors, and extracellular matrix components. Our data represent the most comprehensive sequence resource available for the Chinese soft-shelled turtle and could provide a basis for new research on this turtle as well as the molecular genetics and functional genomics of other terrapins. To our knowledge, we report for the first time, the large-scale RNA sequencing (RNA-Seq) of terrapin animals and would enrich the knowledge of turtles for future research.

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“…Cell Spreading and Formation of Focal Contacts-Focal contact formation analysis was performed as described previously (34). Briefly, glass chamber slides (Nunc) were coated with collagen XXIII ectodomain or bovine collagen I (both 40 g/ml) overnight at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Collagen XXIII, Novel Ligand for Integrin α2β1 in the Epidermis

Veit

Zwolanek

Eckes

et al. 2011

Journal of Biological Chemistry

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Cellular receptors for collagens belong to the family of ␤ 1 integrins. In the epidermis, integrin ␣ 2 ␤ 1 is the only collagenbinding integrin present. Its expression is restricted to basal keratinocytes with uniform distribution on the cell surface of those cells. Although ␣ 2 ␤ 1 receptors localized at the basal surface interact with basement membrane proteins collagen IV and laminin 111 and 332, no interaction partners have been reported for these integrin molecules at the lateral and apical membranes of basal keratinocytes. Solid phase binding and surface plasmon resonance spectroscopy demonstrate that collagen XXIII, a member of the transmembrane collagens, directly interacts with integrin ␣ 2 ␤ 1 in an ion-and conformation-dependent manner. The two proteins co-localize on the surface of basal keratinocytes. Furthermore, collagen XXIII is sufficient to induce adhesion and spreading of keratinocytes, a process that is significantly reduced in the absence of functional integrin ␣ 2 ␤ 1 .Collagen XXIII belongs to the class of transmembrane collagens in type II orientation, which comprises the collagens XIII, XVII, XXIII, and XXV and other related proteins such as ectodysplasin A, class A macrophage scavenger receptors, and the colmedins (1, 2). Collagen XXIII forms homotrimers consisting of a short intracellular domain, a single-pass transmembrane domain and three extracellular collagen domains interrupted by short noncollagenous sequences (3, 4). It exists either as a full-length, membrane-anchored protein or as a soluble ectodomain. The proteolytic processing releasing the ectodomain is mediated by furin and is regulated by the plasma membrane microenvironment (5). Collagen XXIII is expressed in the epidermis and other epithelia such as those in the tongue, gut, and lung but also in the brain and kidney (4). In prostate, collagen XXIII expression was shown to correlate with tumor progression (6).Four integrins, ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , ␣ 10 ␤ 1 , and ␣ 11 ␤ 1 bind native collagens (7). This ␤ 1 subunit-containing subclass of integrins is characterized by the presence of an inserted domain (I domain) with homology to von Willebrand factor A domains in their ␣-subunit, which harbors the ligand-binding site (8, 9). The integrins ␣ 10 ␤ 1 and ␣ 11 ␤ 1 have a restricted expression pattern on differentiated chondrocytes and developing muscle cells (10, 11), whereas ␣ 1 ␤ 1 and ␣ 2 ␤ 1 show a broader distribution, with integrin ␣ 1 ␤ 1 being predominantly expressed by cells of mesenchymal origin and integrin ␣ 2 ␤ 1 by epithelial cells and platelets. In vitro studies suggested an implication of integrin ␣ 2 ␤ 1 in cell attachment and migration (12, 13), generation of mechanical forces and contraction of collagen matrices (14), induction of collagenase activity and matrix remodeling (15, 16), as well as angiogenesis (17) and epithelial branching morphogenesis (18). Mice lacking the integrin ␣ 2 subunit exhibit defects in mammary gland branching morphogenesis (19), delayed platelet aggregation and formation of unstable t...

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

Cited by 50 publications

References 43 publications

The integrin–collagen connection – a glue for tissue repair?

The integrin–collagen connection – a glue for tissue repair?

De-novo characterization of the soft-shelled turtle Pelodiscus sinensis transcriptome using Illumina RNA-Seq technology

Collagen XXIII, Novel Ligand for Integrin α2β1 in the Epidermis

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