Regulation of type I collagen genes expression

Rossert, Jérôme; Terraz, Catherine; Dupont, Stéphanie

doi:10.1093/ndt/15.suppl_6.66

Cited by 73 publications

(55 citation statements)

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“…Within bone, Col3.6 is expressed in precursor cells in the suture mesenchyme, as well as in preosteoblasts and the fibrous layers of the inner and outer periosteum and their downstream progeny (24). In contrast, Col2.3 and Col3.2 are identified specifically in osteoblasts and osteocytes (26)(27)(28)(29). We surmise that the reported osteoporotic phenotype of Col3.6-Cre:Rosa-Nicd Tg/Tg may be caused by early and constant Nicd activation that likely interrupts physiological lineage transition from the preosteoblast into mature osteoblasts and osteocytes (15).…”

Section: Discussionmentioning

confidence: 99%

“…S3). To circumvent osteosclerosis resulting from the noninducible, persistent expression of Nicd by Dmp1-Cre, we selected Col3.2-CreERT2 to achieve a spatiotemporal control of Nicd activity in mature osteoblasts and osteocytes in bone, as previously reported (26)(27)(28)(29). Of note is that the expression of the 3.2-kb Col1a1 promoter is restricted to mature osteoblasts and osteocytes similarly to the 2.3-kb Col1a1 promoter, but is distinct from that of the Col3.6 promoter.…”

Section: Controlled Notch Overexpression In Osteoblast Lineage Cellsmentioning

confidence: 99%

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Anabolic actions of Notch on mature bone

Liu

Ping

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Notch controls skeletogenesis, but its role in the remodeling of adult bone remains conflicting. In mature mice, the skeleton can become osteopenic or osteosclerotic depending on the time point at which Notch is activated or inactivated. Using adult EGFP reporter mice, we find that Notch expression is localized to osteocytes embedded within bone matrix. Conditional activation of Notch signaling in osteocytes triggers profound bone formation, mainly due to increased mineralization, which rescues both age-associated and ovariectomy-induced bone loss and promotes bone healing following osteotomy. In parallel, mice rendered haploinsufficient in γ-secretase presenilin-1 (Psen1), which inhibits downstream Notch activation, display almost-absent terminal osteoblast differentiation. Consistent with this finding, pharmacologic or genetic disruption of Notch or its ligand Jagged1 inhibits mineralization. We suggest that stimulation of Notch signaling in osteocytes initiates a profound, therapeutically relevant, anabolic response.

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Section: Discussionmentioning

confidence: 99%

Section: Controlled Notch Overexpression In Osteoblast Lineage Cellsmentioning

confidence: 99%

Anabolic actions of Notch on mature bone

Liu

Ping

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Whereas c-Fos expression in young and aged skin is unaltered, c-Jun expression is higher in aged skin than in young skin (8). Some recent reports have suggested that the major regulatory mechanism of procollagen expression involves transcriptional control (28)(29)(30)(31). Decreased procollagen expression is partly mediated by c-Jun, which is induced by UV light and interferes with procollagen transcription (9).…”

Section: Discussionmentioning

confidence: 99%

Photoprotective and anti-skin-aging effects of eicosapentaenoic acid in human skin in vivo

Kim

Cho

Lee

et al. 2006

Journal of Lipid Research

108

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Skin aging can be attributed to photoaging (extrinsic) and chronological (intrinsic) aging. Photoaging and intrinsic aging are induced by damage to human skin attributable to repeated exposure to ultraviolet (UV) irradiation and to the passage of time, respectively. In our previous report, eicosapentaenoic acid (EPA) was found to inhibit UV-induced matrix metalloproteinase-1 (MMP-1) expression in human dermal fibroblasts. Therefore, we investigated the effects of EPA on UV-induced skin damage and intrinsic aging by applying EPA topically to young and aged human skin, respectively. By immunohistochemical analysis and Western blotting, we found that topical application of EPA reduced UV-induced epidermal thickening and inhibited collagen decrease induced by UV light. It was also found that EPA attenuated UV-induced MMP-1 and MMP-9 expression by inhibiting UV-induced c-Jun phosphorylation, which is closely related to UV-induced activator protein-1 activation, and by inhibiting JNK and p38 activation. EPA also inhibited UV-induced cyclooxygenase-2 (COX-2) expression without altering COX-1 expression. Moreover, it was found that EPA increased collagen and elastic fibers (tropoelastin and fibrillin-1) expression by increasing transformin growth factor-b expression in aged human skin.Together, these results demonstrate that topical EPA has potential as an anti-skin-aging agent. Skin aging can be attributed to extrinsic aging and intrinsic (chronological) aging and is commonly related to increased wrinkling, sagging, and laxity (1). Extrinsic aging is generally referred to as photoaging and is caused by repeated exposure to ultraviolet (UV) light. Whereas naturally aged skin is smooth, pale, and finely wrinkled, photoaged skin is coarsely wrinkled and associated with dyspigmentation and telangiectasia (2). Alterations in collagen, the major structural component of the skin, have been considered to be a cause of skin aging and are observed in naturally aged and photoaged skin (3, 4). However, the mechanisms of collagen destruction in aged skin have not been fully clarified.Collagen destruction is, in part, related to the induction of matrix metalloproteinase (MMP) secreted by epidermal keratinocytes and dermal fibroblasts. MMP levels are increased by various stimuli, such as UV light, oxidative stress, and cytokines. UV light rapidly activates activator protein-1 (AP-1) DNA binding and induces MMPs, including MMP-1 (collagenase), stromelysin (MMP-3), and gelatinase (MMP-9) (5). UV-induced MMP-1 expression induces the cleavage of fibrillar collagen (types I and III) at a single site. Once collagen is cleaved by MMP-1, it is further degraded by MMP-3 and MMP-9, which are also increased by UV light exposure (6). In human skin, UV-induced AP-1 transcriptional activity that is closely related to MMP expression is limited by c-Jun expression, because c-Fos is constitutively expressed (7). Moreover, whereas c-Fos expression levels in young (18-28 years old) and aged (.80 years old) skin are not different, c-Jun express...

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“…Type I collagen consists of three polypeptide chains in a triple helix and the helix consists of two ␣-1 and a single ␣-2 chain, each ϳ1050 aa in length (41,42). Type I collagen is widely distributed and is a major component of the anterior uveal tract (43,44).…”

Section: Discussionmentioning

confidence: 99%

Type I Collagen Is the Autoantigen in Experimental Autoimmune Anterior Uveitis

Bora

Sohn

Kang

et al. 2004

The Journal of Immunology

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This study was undertaken to identify and characterize the Ag responsible for the induction of experimental autoimmune anterior uveitis (EAAU). Melanin-associated Ag isolated from bovine iris and ciliary body was digested with the proteolytic enzyme V8 protease to solubilize the proteins and the pathogenic protein was purified to homogeneity. Lewis rats were sensitized to various fractions and investigated for the development of anterior uveitis and an immune response to the purified Ag. The uveitogenic Ag had a mass of 22 kDa (SDS-PAGE) and an isoelectric point of 6.75. The N-terminal amino acid sequence of this protein demonstrated 100% homology with the bovine type I collagen α-2 chain starting from amino acid 385 and will be referred to as CI-α2 (22 kDa). Animals immunized with bovine CI-α2 (22 kDa) developed both cellular and humoral immunity to the Ag. They developed anterior uveitis only if the CI-α2 chain underwent proteolysis and if the bound carbohydrates were intact. EAAU induced by CI-α2 (22 kDa) can be adoptively transferred to naive syngenic rats by primed CD4+ T cells. EAAU could not be induced by the adoptive transfer of sera obtained from animals immunized with CI-α2 (22 kDa). The α-1 and α-2 chains (intact or proteolytically cleaved) of type I collagen from calfskin were not pathogenic. Although human anterior uveitis has been historically characterized as a collagen disease, this is first time collagen has been directly identified as the target autoantigen in uveitis.

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Regulation of type I collagen genes expression

Cited by 73 publications

References 0 publications

Anabolic actions of Notch on mature bone

Anabolic actions of Notch on mature bone

Photoprotective and anti-skin-aging effects of eicosapentaenoic acid in human skin in vivo

Type I Collagen Is the Autoantigen in Experimental Autoimmune Anterior Uveitis

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