Non-uniform influence of transforming growth factor-<i>β</i> on the biosynthesis of different forms of small chondroitin sulphate/dermatan sulphate proteoglycan

Breuer, Bettina; Schmidt, Gregory W.; Kresse, Hans

doi:10.1042/bj2690551

Cited by 72 publications

(34 citation statements)

References 29 publications

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“…In MG-63 osteosarcoma cells TGF-fl causes an up-regulation of biglycan, a marked down-regulation of PG-100 and a minor reduction ofdecorin synthesis [9]. Inactivation of TGF-fl by decorin would therefore be expected to interfere with opposite effects on proteoglycan biosynthesis.…”

Section: Resultsmentioning

confidence: 99%

“…Fibroblast-populated collagen lattices were prepared [19] with bovine serum albumin (BSA) in place of serum [9]. Before metabolic labeling, MG-63 cells were preincubated for 20 h with the indicated quantities of TGF-fl and/or decorin in serum-free MEM medium containing 1% BSA.…”

Section: Cell Culture and Metabolic Labelingmentioning

confidence: 99%

“…Human osteosarcoma cells (MG-63), skin fibroblasts [9] and monocyte-like U937 cells [18] were cultured as described. Fibroblast-populated collagen lattices were prepared [19] with bovine serum albumin (BSA) in place of serum [9].…”

Section: Cell Culture and Metabolic Labelingmentioning

confidence: 99%

“…An up-regulation of biglycan has consistently been noted. An increased production of the collagenbinding proteoglycan decorin has been observed in mesangial cells [7] but not in fibroblasts [8,[9][10][11]. Another small proteoglycan, proteoglycan-100 (PG-100), was markedly down-regulated [9].…”

Section: Introductionmentioning

confidence: 99%

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Selective inactivity of TGF‐β/decorin complexes

et al. 1994

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Previous studies had shown that binding of TGF-fl to the small proteoglycan decorin results in its inactivation. Indeed, in osteosarcoma ceils the addition of decorin prevented the TGF-fll-mediated up-regulation of biglycan synthesis. However, the down-regulation of proteoglycan-100 remained unaltered. Even in the presence of a 100,000-fold molar excess of decorin, TGF-fll was fully active in U937 monocytes with respect to the inhibition of cell proliferation. There was no inhibition of the TGF-fl-mediated stimulation of the retraction of fibroblast-populated collagen lattices. Thus, the formation of TGF-fl/decorin complexes leads to the neutralization of distinct effects only.

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Section: Resultsmentioning

confidence: 99%

Section: Cell Culture and Metabolic Labelingmentioning

confidence: 99%

Section: Cell Culture and Metabolic Labelingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Selective inactivity of TGF‐β/decorin complexes

et al. 1994

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“…The physiological regulation of decorin synthesis in different cell types is still a matter of discussion, as the same cytokine can have opposite effects on decorin synthesis; TGF-␤ has been shown to up-regulate decorin in mesangial cells but to downregulate the proteoglycan in most other cell types (8,9). Besides TGF-␤, several other cytokines have been implicated in the regulation of decorin synthesis on a transcriptional as well as on a translational or posttranslational level (IL-1, tumor necrosis factor (TNF)-␣, TGF-␣, epidermal growth factor, etc.…”

mentioning

confidence: 99%

Interleukin (IL)-6 and IL-10 Induce Decorin mRNA in Endothelial Cells, but Interaction with Fibrillar Collagen Is Essential for Its Translation

Strazynski

Eble

Kresse

et al. 2004

Journal of Biological Chemistry

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Decorin, a small multifunctional proteoglycan, is expressed by sprouting endothelial cells (ECs) during inflammation-induced angiogenesis in vivo and by human ECs co-cultured with fibroblasts in a collagen lattice. To investigate how decorin is induced, human EA.hy 926 ECs and/or human umbilical vein ECs were treated with interleukin (IL)-10 and IL-6. Both treatments induced decorin mRNA in human ECs. IL-6 and IL-10 led to a dose-dependent mRNA increase with a maximum at 10 and 50 ng/ml, respectively. The combination of both interleukins together had a stronger effect than one alone. Immunostaining demonstrated that both interleukins caused decorin synthesis in ECs and the formation of capillary-like structures in a collagen lattice. However, immunoprecipitations of interleukin-treated ECs cultured on plastic were negative. Only interleukin-stimulated ECs grown on a collagen type I matrix or growth factor-reduced Matrigel were able to synthesize the proteoglycan. Acid-soluble collagen type I did not support decorin protein synthesis. The addition of antibodies to ␣ 1 or ␣ 2 integrins or the ␣ 2 integrin inhibitor rhodocetin led to an inhibition of synthesis. These data show that IL-10 and IL-6 induce decorin mRNA transcription, but additional signals from the extracellular matrix are necessary for its translation.

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Biglycan and Decorin Gene Expression in Normal and Fibrotic Rat Liver: Cellular Localization and Regulatory Factors

et al. 1992

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The expression of genes encoding the core proteins of the novel small chondroitin/dermatan sulfate proteoglycans decorin and biglycan was studied in the livers of normal rats and in liver tissue during fibrogenesis induced by prolonged bile-duct ligation and thioacetamide poisoning. The cell types responsible for the expression of these transcripts and some key regulatory factors were identified. Both biglycan and decorin messenger RNAs were detected in normal liver tissue. Their relative abundance increased strongly during liver fibrogenesis, reaching highest levels in cirrhotic tissue 8 wk after common bile-duct ligation and after 12 wk of peroral thioacetamide administration, respectively. Specific proteoglycan transcripts were almost absent in hepatocytes from normal and regenerating liver, and only trace amounts were observed in freshly isolated and cultured Kupffer cells. Fat-storing cells clearly expressed both biglycan and decorin transcripts. The steady-state levels of their messenger RNAs increased threefold (biglycan) and fourfold (decorin) during primary culture. Myofibroblastlike cells (transformed fat-storing cells after the second passage) contained dramatically reduced levels of decorin messenger RNA and also lower levels of biglycan messenger RNA compared with primary cultures. These changes of core protein messenger RNA expression were not reflected by the synthesis rates of medium proteoglycans labeled with 35S as Na2SO4, in particular that of medium chondroitin sulfate. Transiently acidified (but not native) conditioned media from Kupffer cells and myofibroblastlike cells and transforming growth factor-beta 1 enhanced the relative abundances of biglycan and decorin messenger RNAs up to five times in primary-cultured fat-storing cells. Biglycan and decorin in myofibroblastlike cells did not respond to these stimuli.(ABSTRACT TRUNCATED AT 250 WORDS)

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Non-uniform influence of transforming growth factor-β on the biosynthesis of different forms of small chondroitin sulphate/dermatan sulphate proteoglycan

Cited by 72 publications

References 29 publications

Selective inactivity of TGF‐β/decorin complexes

Selective inactivity of TGF‐β/decorin complexes

Interleukin (IL)-6 and IL-10 Induce Decorin mRNA in Endothelial Cells, but Interaction with Fibrillar Collagen Is Essential for Its Translation

Biglycan and Decorin Gene Expression in Normal and Fibrotic Rat Liver: Cellular Localization and Regulatory Factors

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