Receptor-mediated endocytosis of proteoglycans by human fibroblasts involves recognition of the protein core

Glössl, Josef; Schubert-Prinz, R; Gregory, John D.; Damle, Shridhar P.; Figura, Kurt Von; Kresse, Hans

doi:10.1042/bj2150295

Cited by 61 publications

(28 citation statements)

References 29 publications

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“…A possible feedback mechanism could involve cellular receptors for LRR proteins. Indeed, it has previously been shown that cultured fibroblasts degrade about 30% of newly synthesized decorin (50) via efficient receptor-mediated endocytosis (51). In analogy, it is possible that lumican is also endocytosed and degraded, providing a sensing mechanism.…”

Section: Fibromodulin Knock-out Micementioning

confidence: 99%

Fibromodulin-null Mice Have Abnormal Collagen Fibrils, Tissue Organization, and Altered Lumican Deposition in Tendon

Svensson¹,

Aszódi²,

Reinholt³

et al. 1999

Journal of Biological Chemistry

400

357

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Section: Fibromodulin Knock-out Micementioning

confidence: 99%

Fibromodulin-null Mice Have Abnormal Collagen Fibrils, Tissue Organization, and Altered Lumican Deposition in Tendon

Svensson¹,

Aszódi²,

Reinholt³

et al. 1999

Journal of Biological Chemistry

400

357

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“…As an ubiquitous component of extracellular matrices, decorin is synthesized by the majority of mesenchymal cells (3,5) and is found preferentially in association with collagen fibrils (6,7). However, it also interacts with a variety of other components such as fibronectin (8), thrombospondin (9), transforming growth factor-␤ (TGF-␤) (10), and a receptor required for its endocytosis (11). These binding properties, mainly mediated by the core protein, imply an important role in the structural organization of the extracellular matrix (5,12).…”

mentioning

confidence: 99%

A Composite Element Binding the Vitamin D Receptor and the Retinoic X Receptor α Mediates the Transforming Growth Factor-β Inhibition of Decorin Gene Expression in Articular Chondrocytes

Demoor-Fossard¹,

Galéra²,

Santra³

et al. 2001

Journal of Biological Chemistry

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Decorin, a small leucine-rich proteoglycan may play an important role in the attempt of cartilage repair initiated by chondrocytes in early stages of osteoarthritis, through its ability to bind collagen fibrils and growth factors such as transforming growth factor-␤ (TGF-␤). We previously demonstrated that TGF-␤ decreased decorin mRNA steady state levels in articular chondrocytes (Demoor, M., Ré dini, F., Boittin, M., and Pujol, J.-P. . DNase I footprinting analysis delineated a negative TGF-␤-responsive region between ؊140 and ؊111 bp in the decorin proximal promoter. Gel retardation assays demonstrated that TGF-␤ modulates decorin gene expression through transcription factors, the nature and mode of action of which depend on the differentiation state of the chondrocytes; two DNA-protein complexes were formed in the region ؊144/؊127 bp with nuclear extracts from primary chondrocytes, whereas a higher mobility complex was observed in the ؊127/؊111 bp region for dedifferentiated cells. Antibodies against vitamin D and retinoic acid receptors used in supershift experiments showed that these nuclear receptors are involved in the regulation of decorin gene expression in articular chondrocytes.

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“…Thus decorin has been demonstrated in vitro to bind to several proteins including fibronectin (15), transforming growth factor-␤ (16), and membrane receptors required for its endocytosis (17). In addition, decorin binds to certain types of fibrillar collagens including type I (18), type II (19), and type VI (20) and retards fibrillogenesis (19).…”

mentioning

confidence: 99%

Recombinant Decorin Glycoforms

Ramamurthy

Hocking

McQuillan

1996

Journal of Biological Chemistry

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The vaccinia virus/T7 bacteriophage expression system was used to express human decorin in HT-1080 cells by co-infection with vTF7-3, encoding T7 RNA polymerase, and vDCN1, encoding the decorin core protein fused to a polyhistidine-insulin signal sequence fusion-protein cassette. Overexpression using the vaccinia virus/T7 phage system resulted in secretion of approximately 30 mg of decorin/10 9 cells per 24 h which enabled purification and separation of multiple glycoforms under native conditions. Cells were cultured in the presence of [ 35 S]methionine or a mixture of [ H]glucosamine and [35 S]sulfate, and recombinant glycoprotein purified by metal affinity chromatography which resolved the secreted decorin into two classes, a proteoglycan form and a core protein form. About 25% of the recombinant protein was secreted into the culture medium as core protein devoid of glycosaminoglycan chains. The decorin core protein was resolved into two forms (ϳ49 and ϳ53 kDa) that differed in the extent of N-linked oligosaccharide substitution (2 and 3 N-linked oligosaccharides, respectively). Deglycosylation of the recombinant proteoglycans and core proteins resulted in a single band migrating with an apparent molecular mass ϳ 43 kDa when analyzed by SDS-polyacrylamide gel electrophoresis. Far-UV circular dichroism spectra of native decorin proteoglycan showed a minima at 218 nm, consistent with a secondary structure that is predominantly ␤-sheet. Circular dichroism spectra of bovine decorin extracted from articular cartilage and recombinant decorin similarly treated revealed a minima of 205 nm indicating a loss of secondary structure. The affinity of decorin proteoglycan and core protein for collagenlike molecules was demonstrated, with the complement component C1q exhibiting the most striking affinity for decorin, although adherence to collagen types I and V was also observed. The extensive secondary structure maintained in the purified recombinant protein is likely to be important for the biological function of decorin.

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Receptor-mediated endocytosis of proteoglycans by human fibroblasts involves recognition of the protein core

Cited by 61 publications

References 29 publications

Fibromodulin-null Mice Have Abnormal Collagen Fibrils, Tissue Organization, and Altered Lumican Deposition in Tendon

Fibromodulin-null Mice Have Abnormal Collagen Fibrils, Tissue Organization, and Altered Lumican Deposition in Tendon

A Composite Element Binding the Vitamin D Receptor and the Retinoic X Receptor α Mediates the Transforming Growth Factor-β Inhibition of Decorin Gene Expression in Articular Chondrocytes

Recombinant Decorin Glycoforms

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