Cortisol decreases the cellular concentration of translatable procollagen mRNA species in cultured human skin fibroblasts

Oikarinen, Jouko; Pihlajaniemi, Taina; Hämäläinen, Leena; Kivirikko, Kari I.

doi:10.1016/0167-4781(83)90148-3

Cited by 20 publications

(7 citation statements)

References 30 publications

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“…demonstrated a down regulation of radiolabeled corticosteroid binding to glucocorticoid receptors in dexamethasone-treated human skin fibroblasts. Glucocortoids have also been shown to decrease collagen synthesis [Russell et al, 1978;Ponec et al, 19791 and type I procollagen mRNAs [Oikarinen et al, 1983;Russell et al, 19891 in human skin fibroblasts. Glucocorticoid treatment has been reported to cause a decrease in glucocorticoid receptor concentration in many tissues and cell lines while adrenalectomy causes an up regulation of glucocorticoid receptor concentration [Okret et al, 1991;Burnstein and Cidlowski, 19921. In our present studies we have identified a non-GRE containing DNA element, the TGF-P element as functional in the dexamethasonemediated down regulation of proal(1) collagen gene expression.…”

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confidence: 99%

Glucocorticoids coordinately regulate type I collagen proα1 promoter activity through both the glucocorticoid and transforming growth factor β response elements: A novel mechanism of glucocorticoid regulation of eukaryotic genes

Meisler

Shull

Xie

et al. 1995

J of Cellular Biochemistry

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Glucocorticoids have previously have shown to decrease Type I collagen synthesis in vivo and in fibroblast cell culture. Several studies have demonstrated that glucocorticoids decrease Type I procollagen gene expression. These latter studies have included uridine incorporation into pro alpha 1 (I) and pro alpha 2 (I) mRNAs and nuclear run-off experiments. Using the ColCat 3.6 plasmid, which contains part of the 5' flanking region of the pro alpha 1 (I) collagen gene and the reporter gene, chloramphenicol acetyltransferase, the present studies demonstrate by stable transfection of fetal rat skin fibroblasts that dexamethasone down regulates the promoter activity of the pro alpha 1 (I) collagen gene. The glucocorticoid-mediated down-regulation of procollagen gene expression was demonstrated using the ColCat 3.6, 2.4, 1.7, or 0.9 plasmid. In addition, competitive oligonucleotide transfection experiments and site specific mutation of the glucocorticoid response element (GRE) in the whole ColCat 3.6 plasmid did not eliminate the effect. The possibility existed that another cis-element in the 5' flanking region of the pro alpha 1 (I) collagen gene was also required for the collagen glucocorticoid-mediated down-regulation of procollagen gene expression, since TGF-beta has been shown to stimulate in a decrease of transforming growth factor-beta (TGF-beta) secretion into the media. Gel mobility studies demonstrated that glucocorticoid treatment of rat skin fibroblasts decreased glucocorticoid receptor binding to the GRE and TGF-beta activator protein to the TGF-beta element which were brought back to control values by coordinate exogenous TGF-beta treatment. Thus the interaction of these TGF-beta molecules with cellular membrane receptors and subsequent transduction is dramatically decreased resulting in less signals to regulate collagen gene expression. These data indicate that glucocorticoids coordinately regulate procollagen gene expression through both the GRE and TGF-beta elements. Depression of procollagen gene expression by glucocorticoids through the TGF-beta element is mediated by decreased TGF-beta secretion, possibly involving a secondary effect on regulatory protein(s) encoded by noncollagenous protein gene(s). The present studies provide the basis for a novel mechanism of glucocorticoid-mediator regulation of eukaryotic genes containing the TGF-beta element.

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Section: %mentioning

confidence: 99%

Glucocorticoids coordinately regulate type I collagen proα1 promoter activity through both the glucocorticoid and transforming growth factor β response elements: A novel mechanism of glucocorticoid regulation of eukaryotic genes

Meisler

Shull

Xie

et al. 1995

J of Cellular Biochemistry

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“…It has been shown that excessive glucocorticoids inhibit the expression of types I and III collagen on mRNA level [3], but increase the concentration of type IV collagen in skeletal muscle [4]. As the function of contractile proteins in single muscle fibers occurs on the level of muscle in cooperation with extracellular matrix (ECM) components, it is important to clarify, how densely these two systems are linked in atrophic muscle.…”

Section: Introductionmentioning

confidence: 99%

Relationship between extracellular matrix, contractile apparatus, muscle mass and strength in case of glucocorticoid myopathy

Riso

Ahtikoski

Alev

et al. 2008

The Journal of Steroid Biochemistry and Molecular Biology

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“…Type IV collagen is a major component in basement membrane [9] and therefore plays a critical role in the cellular arrangement in muscle tissue [13]. Glucocorticoids are known to inhibit the synthesis of collagens by reducing mRNA expression of types I and III collagens [20] and the activity of enzymes participating in the posttranslational modification of collagens [6]. The effects of glucocorticoids on the synthesis of type IV collagen have not been studied widely.…”

Section: Introductionmentioning

confidence: 99%

Regulation of type IV collagen gene expression and degradation in fast and slow muscles during dexamethasone treatment and exercise

Ahtikoski

Riso

Koskinen

et al. 2004

Pfl�gers Archiv European Journal of Physiology

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Glucocorticoids have anti-anabolic effects on many tissues and can cause muscle atrophy. However, their effects on type IV collagen gene expression and degradation in skeletal muscle have not been studied previously. Rats were treated daily with dexamethasone or saline. Half the groups of experimental and control animals were also subjected to daily endurance or uphill running exercise to determine the possible preventive effects of exercise. After an experimental period of 3 or 10 days, the extensor digitorum longus, soleus and tibialis anterior muscles were studied. Dexamethasone treatment for 10 days reduced muscle weight and type IV collagen mRNA abundance in all muscles. Gene expression of matrix metalloproteinase-2 (MMP-2) was decreased in fast muscles. However, the effects of this decrease were possibly attenuated by the simultaneous decrease in the activity of tissue inhibitor of metalloproteinases (TIMP-2). The amount of type IV collagen was not changed during dexamethasone treatment or exercise. The regulation of type IV collagen degradation during dexamethasone treatment varied between slow and fast muscles. Although endurance running prevented muscle atrophy, exercise could not compensate the changes observed in the regulation of type IV collagen gene expression and degradation during dexamethasone treatment.

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Cortisol decreases the cellular concentration of translatable procollagen mRNA species in cultured human skin fibroblasts

Cited by 20 publications

References 30 publications

Glucocorticoids coordinately regulate type I collagen proα1 promoter activity through both the glucocorticoid and transforming growth factor β response elements: A novel mechanism of glucocorticoid regulation of eukaryotic genes

Glucocorticoids coordinately regulate type I collagen proα1 promoter activity through both the glucocorticoid and transforming growth factor β response elements: A novel mechanism of glucocorticoid regulation of eukaryotic genes

Relationship between extracellular matrix, contractile apparatus, muscle mass and strength in case of glucocorticoid myopathy

Regulation of type IV collagen gene expression and degradation in fast and slow muscles during dexamethasone treatment and exercise

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