Different regulation of collagen I gene transcription in three‐dimensional lattice cultures

Gillery, Philippe; Leperre, Armelle; Coustry, Françoise; Maquart, François‐Xavier; Borel, J.P.

doi:10.1016/0014-5793(92)80308-4

Cited by 15 publications

(15 citation statements)

References 17 publications

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“…This general mechanism does not rule out the involvement of other mechanisms already demonstrated, and particularly the transcriptional regulation of various genes [7], some of them being down-regulated and other up-regulated. However, this overall regulation of fibroblast metabolism should account for a great part of the modifications noticed in this type of cultures.…”

Section: Discussionmentioning

confidence: 99%

“…This is the case particularly for the type I collagen gene [7], However, the overall decrease of protein synthesis suggests that more general mechanisms are involved.…”

Section: Introductionmentioning

confidence: 91%

“…Cells from subcultures 3 to 10 were used in this study and seeded into monolayers and collagen lattices made of acid soluble calf skin collagen prepared in the laboratory, as previously described [6][7][8]. RNA studies were performed after 1 week of culture.…”

Section: Fibroblast Culturesmentioning

confidence: 99%

“…It was shown that fibroblast activity was strongly modulated by the presence of the extracellular matrix : when cultured in a lattice, cells stopped dividing or divided very slowly [3], their response to growth factors was decreased [4][5][6], and their protein syntheses were strongly inhibited [2,7]. These findings were of particular interest because these features look like those that characterize fibroblasts in vivo, when cells are surrounded by the extracellular matrix, as in the case of skin, and show a low metabolic activity, except in pathological situations such as fibrosis or wound healing.…”

Section: Introductionmentioning

confidence: 99%

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Protein synthesis in collagen lattice‐cultured fibroblasts is controlled at the ribosomal level

et al. 1995

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Fibroblasts cultivated in three-dimensional lattices exhibit a large decrease of protein synthesis, mainly through transcriptional control. However, no previous work was devoted to a potential ribosomal regulation. We evaluated ribosomal ribonucleic acid (RNA) in monolayer-and collagen lattice-cultured fibroblasts. After one week of culture, total RNA was 60% lower in lattice-cultured fihroblasts than in monolayer-cultured cells. The decrease was identical for 18 S and 28 S rRNA subfractions. The half-life of RNA was much shorter in collagen lattice-cultured fihroblasts than in monolayers. These results suggest that protein synthesis in lattice-cultured fibroblasts is partly regulated at the ribosomal level.

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Section: Discussionmentioning

confidence: 99%

“…This is the case particularly for the type I collagen gene [7], However, the overall decrease of protein synthesis suggests that more general mechanisms are involved.…”

Section: Introductionmentioning

confidence: 91%

Section: Fibroblast Culturesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Protein synthesis in collagen lattice‐cultured fibroblasts is controlled at the ribosomal level

et al. 1995

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“…They also demonstrated that this effect is only partly due to the enhancement of collagen density. Gillery et al 39 demonstrated that the retraction and the nature of the fibrillar protein that constitutes the lattices contribute to the lower level of procollagen mRNA in collagen lattice-cultured fibroblasts. Unemori and Werb 40 report that the stimulation of collagenase synthesis in fibroblasts within a collagen gel does not occur if contraction of the gel is inhibited by mechanical means.…”

Section: Discussionmentioning

confidence: 99%

Aortic smooth muscle cells in a three-dimensional collagen lattice culture. Evidence for posttranslational regulation of collagen synthesis.

Redecker-Beuke

Thie

Rauterberg

et al. 1993

Arterioscler Thromb

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Aortic smooth muscle cells were cultivated as monolayers on plastic or within collagen lattices with lowand high-serum supplementation, and the expression of mRNAs specific for pro alpha 1 (I) and pro alpha 1 (HI) collagen were studied by slot blot hybridization. The steady-state levels of pro alpha 1 (I) and pro alpha 1 (HI) collagen mRNA of cells within collagen lattices were found to be higher than those grown on plastic, although the production of collagen was lower. The degradation of pro alpha 1 (I) and pro alpha 1 (HI) collagen mRNAs as revealed in the presence of actinomycin D was not affected by culturing the cells within a collagen lattice. In vitro translation assays of mRNAs of monolayer-and lattice-cultured cells showed no differences in translatability. These data suggest the involvement of posttranslational control of collagen production in collagen lattice-cultured smooth muscle cells. (Arterioscler Thromb. 1993;13:1572-1579 KEY The collagens are known to be synthesized by smooth muscle cells (SMCs) present within the atheromatous plaque. However, the regulatory mechanisms involved in the synthesis of collagens by ill-coordinated cells are unknown. An important question still to be answered in relation to the possible role of collagens in atherogenesis is, therefore, how collagen synthesis of SMCs is regulated under normal and pathophysiological conditions.When healthy arterial SMCs are freed from their physiological matrix and are dispersed into monolayer culture on plastic, they begin to change their ultrastructural character. Cells show a modulation from the contractile state characteristic of the healthy vessel to the synthetic state typical of the atherosclerotic vessel, which is characterized by abundant rough endoplasmic reticulum and a large Golgi complex. When monolayer-cultured SMCs are reintegrated into a tissuelike matrix, ie, a three-dimensional network of type I collagen, SMCs reduce their collagen synthesis and suppress their responsiveness to soluble growth mediators.1112 To elucidate the mechanism responsible for the observed reduction of collagen production, we analyzed the molecular process involved in collagen biosynthesis of matrix-cultured cells. This article presents data concerning the level and the translational capacity of collagen mRNAs in SMCs grown within a type I collagen lattice with low-and high-serum supplementation. Our results showed that the steady-state levels of pro alpha 1 (I) and pro alpha 1 (III) collagen mRNA of SMCs decrease with increases in serum concentration. At each concentration tested, steadystate levels of mRNA in lattice-cultured SMCs were higher than those in monolayer-cultured cells. The elevated collagen mRNAs of lattice-cultured cells, however, were not paralleled by elevated collagen levels. The stabilities of pro alpha 1 (I) and pro alpha 1 (III) collagen mRNAs are not changed by culturing the SMCs within a collagen lattice. As the in vitro translation activity of mRNAs of lattice-cultured SMCs is not affected, it is concluded that control...

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Tissue origin and extracellular matrix control neutral proteinase activity in human fibroblast three-dimensional cultures

et al. 1996

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Remodeling of the extracellular matrix by fibroblasts is an important step in the process of wound healing and tissue repair. We compared the behavior of fibroblasts from two different tissues, dermis and gingiva, in three-dimensional lattices made of two different extracellular matrix macromolecules, collagen and fibrin. Cells were grown in monolayer cultures from normal skin or gingiva and seeded in three-dimensional lattices made of either collagen of fibrin. Photonic and scanning electron microscopy did not reveal any morphological differences between the two types of fibroblasts in both sets of lattices. Both types of fibroblasts retracted collagen lattices similarly and caused only a slight degradation of the collagen substratum. By contrast, when seeded in fibrin lattices, gingival fibroblasts completely digested their substratum in less than 8 days, whereas only a slight fibrin degradation was observed with dermal fibroblasts. The ability of gingival but not dermal fibroblasts to express high levels of tissue plasminogen activators (tPA) when cultured in fibrin lattices was assessed on an immunological basis. Also, deprivation of plasminogen-contaminating fibrinogen preparations or use of tPA inhibitors markedly inhibited both fibrinolysis and retraction rates of fibrin lattices by gingival fibroblasts. Casein-zymography confirmed the intense proteolytic activity induced by fibrin in gingival fibroblasts. It was inhibited by aprotinin and phenyl methylsulfonyl fluoride (PMSF), two non-specific inhibitors of serine proteinases, and by epsilon-amino-caproic acid (epsilon ACA), an inhibitor of plasminogen activators. Monolayer cultures exhibited only trace amounts of caseinolytic activity. Our results demonstrate that the expression of proteinases by fibroblasts is dependent not only on their tissue origin but also on the surrounding extracellular matrix. The intense fibrinolytic activity of gingival fibroblasts in fibrin lattices may explain partially the high rate of healing clinically observed in gingiva.

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Different regulation of collagen I gene transcription in three‐dimensional lattice cultures

Cited by 15 publications

References 17 publications

Protein synthesis in collagen lattice‐cultured fibroblasts is controlled at the ribosomal level

Protein synthesis in collagen lattice‐cultured fibroblasts is controlled at the ribosomal level

Aortic smooth muscle cells in a three-dimensional collagen lattice culture. Evidence for posttranslational regulation of collagen synthesis.

Tissue origin and extracellular matrix control neutral proteinase activity in human fibroblast three-dimensional cultures

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