Interaction of small dermatan sulfate proteoglycan from fibroblasts with fibronectin.

Schmidt, Gregory W.; Robenek, Horst; Harrach, B.; Glössl, Josef; Nolte,; Hörmann, Helmut; Richter, Hartmut; Kresse, Hans

doi:10.1083/jcb.104.6.1683

Cited by 164 publications

(99 citation statements)

References 62 publications

(60 reference statements)

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“…Chromogen was formed by incubation with 3 mM 4-chloro-l-naphtol in buffer B containing 0.003% H,O, and 17% (v/v) methanol. For staining with MAb against decorin (25). peroxidaseconjugated goat anti-mouse IgG was used in a 1 : 500 dilution.…”

Section: Methodsmentioning

confidence: 99%

Presence of small proteoglycan fragments in normal and arthritic human cartilage

Witsch‐Prehm

Miehlke

Kresse

1992

Arthritis & Rheumatism

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Objective. To characterize the small proteoglycans decorin and biglycan in normal human patellar cartilage and in cartilage from individuals with chronic polyarthritis.Methods. Cartilage extracts were chromatographed on DEAE-Trisacryl and further separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis before and after enzymatic degradation of the glycosaminoglycan chains. Decorin and biglycan were visualized after Western blotting, using core proteinspecific polyclonal and monoclonal antibodies.Results. Core protein fragments of both proteoglycans were observed even in normal cartilage. In the case of decorin they amounted to up to 15% of the immunoreactive material, and up to 5% of the core protein was glycosaminoglycan free. The quantity of decorin core protein was reduced in arthritic cartilage, but the core protein fragments represented up to 45% of the immunoreactive material. Different zones of cartilage differed in their content of the fragments. Evidence for an increased proportion of biglycan fragments was not obtained.

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Section: Methodsmentioning

confidence: 99%

Presence of small proteoglycan fragments in normal and arthritic human cartilage

Witsch‐Prehm

Miehlke

Kresse

1992

Arthritis & Rheumatism

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“…Extracellular matrix (ECM) proteins under TGF-␤ regulation include collagens, decorin, and fibronectin (Balza et al, 1988;Saed et al, 1999;Klein et al, 2002;Fu et al, 2005). Both decorin and fibronectin are capable of binding TGF-␤, presumably to regulate its activity (Schmidt et al, 1987;Mooradian et al, 1989;Yamaguchi et al, 1990;Hildebrand et al, 1994;Schonherr et al, 1998). Decorin, in particular, has been shown to possess independent binding sites for TGF-␤s and collagen type I (Schonherr et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Spatiotemporal protein distribution of TGF‐βs, their receptors, and extracellular matrix molecules during embryonic tendon development

Kuo

Petersen

Tuan

2008

Developmental Dynamics

109

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Tendon is one of the least understood tissues of the musculoskeletal system in terms of development and morphogenesis. Collagen fibrillogenesis has been the most studied aspect of tendon development, focusing largely on the role of matrix molecules such as collagen type III and decorin. While involvement of matrix molecules in collagen fibrillogenesis during chick tendon development is well understood, the role of growth factors has yet to be elucidated. This work examines the expression patterns of transforming growth factor (TGF) -␤1, -␤2, and -␤3, and their receptors with respect to expression patterns of collagen type III, decorin, and fibronectin. We focus on the intermediate stages of tendon development in the chick embryo, a period during which the tendon micro-and macro-architecture are being established. Our findings demonstrate for the first time that TGF-␤1, -␤2, and -␤3 have distinct spatiotemporal developmental protein localization patterns in the developing tendon and strongly suggest that these isoforms have independent roles in tendon development.

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“…The core protein of decorin interacts with several matrix proteins, such as collagens (51)(52)(53)(54)(55), fibronectin (14,56), and thrombospondin (15). Decorin has been visualized at the ultrastructural level bound at the d band of fibrillar collagen (10) and in association with fibronectin fibrils at the surface of cells (57). Studies of in vitro fibrillogenesis have shown that the interaction of decorin with collagen regulates the rate of collagen fibrillogenesis as well as fibril size and interfibrillar spacing (11,12,58,59).…”

Section: Fig 7 Immunofluorescent Staining For Fibronectin In Vectormentioning

confidence: 99%

Retrovirally Mediated Expression of Decorin by Macrovascular Endothelial Cells

Kinsella¹,

Fischer²,

Mason³

et al. 2000

Journal of Biological Chemistry

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Decorin is a member of the widely expressed family of small leucine-rich proteoglycans. In addition to a primary role as a modulator of extracellular matrix protein fibrillogenesis, decorin can inhibit the cellular response to growth factors. Decorin expression is induced in endothelial cells during angiogenesis, but not when migration and proliferation are stimulated. Thus, decorin may support the formation of the fibrillar pericellular matrix that stabilizes the differentiated endothelial phenotype during the later stages of angiogenesis. Therefore, we tested whether constitutive decorin expression alone could modify endothelial cell migration and proliferation or affect pericellular matrix formation. To this end, replication-defective retroviral vectors were used to stably express bovine decorin, which was detected by Northern and Western blotting. The migration of endothelial cells that express decorin is significantly inhibited in both monolayer outgrowth and microchemotaxis chamber assays. The inhibition of cell migration by decorin was not accompanied by decreased proliferation. In addition, endothelial cells that express decorin assemble an extensive fibrillar fibronectin matrix more rapidly than control cells as assessed by immunocytochemical and fibronectin fibrillogenesis assays. These observations suggest that cell migration may be modulated by the influence of decorin on the assembly of the cell-associated extracellular matrix.Migration and proliferation of endothelial cells and the subsequent establishment of a stable monolayer are critical events in the repair of injured vessels and in angiogenesis and vasculogenesis during development, tumor growth, and tissue repair. Cell migration and proliferation are controlled by growth factors and cell adhesive interactions, which are mediated by cell surface receptors, such as integrins (1) and syndecan-4 (2, 3). Thus, control of cell migration may involve a change in cell-matrix interaction characterized by extracellular matrix remodeling and changes in signaling generated by receptors for both soluble and matrix ligands.Proteoglycans (PGs) 1 are a heterogeneous group of protein families that bear anionic glycosaminoglycan (GAG) chains covalently bound to core proteins. These molecules are prominent constituents of both the extracellular matrix and the cell surface, where they are proposed to play roles in cell adhesion, growth factor interactions, and matrix assembly (4, 5). Decorin is a member of the small leucine-rich PG family (6 -8). The association of decorin with collagen fibrils has long been recognized (9, 10), and experimental studies indicated that decorin regulates collagen fibrillogenesis (11,12). In addition, decorin may affect cell migration and proliferation both by modulation of interactions of cell surface receptors with their matrix ligands, such as fibronectin and thrombospondin (13-15), or by an influence on the availability (16, 17) and function (18, 19) of growth factors that direct these cellular processes.We have previously report...

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Interaction of small dermatan sulfate proteoglycan from fibroblasts with fibronectin.

Cited by 164 publications

References 62 publications

Presence of small proteoglycan fragments in normal and arthritic human cartilage

Presence of small proteoglycan fragments in normal and arthritic human cartilage

Spatiotemporal protein distribution of TGF‐βs, their receptors, and extracellular matrix molecules during embryonic tendon development

Retrovirally Mediated Expression of Decorin by Macrovascular Endothelial Cells

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