Transcriptional Activation of the Mouse HSP47 Gene in Mouse Osteoblast MC3T3-E1 Cells by TGF-β1

Yamamura, Isao; Hirata, Hiromi; Hosokawa, Nobuko; Nagata, Kazuhiro

doi:10.1006/bbrc.1998.8216

Cited by 45 publications

(38 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In human vascular smooth muscle cells, human embryonic lung fibroblasts, murine osteoblasts and rat cardiac fibroblasts, HSP47 expression is inducible by TGF-b1. [18][19][20]27 In contrast, we observed no effect of TGF-b1 on HSP47 expression in human HSC, consistent with the results of Kawada et al 11 in murine HSC. Likewise, factors known to stimulate HSP47 expression in other cell types were without effect on human HSC.…”

Section: Discussionsupporting

confidence: 93%

“…[18][19][20][21][22] These included superoxide-generating agents (xanthine-xanthine oxidase, menadione), TGF-b1, hypoxia, and culture on a variety of different matrices. As illustrated in Figure 5, HSP47 expression in activated human HSC was similar in the presence or absence of serum, or following treatment with angiotensin II, TGF-b1, xanthine-xanthine oxidase, menadione, or 1% O 2 for 24 h. Similarly, no effects on HSP47 abundance were observed in HSC treated with the lipid peroxidation-derived aldehyde 4-hydroxynonenal or grown on plates coated with fibronectin, laminin, or collagen types I or IV (data not shown).…”

Section: Modulation Of Hsp47 Expression By Human Hsc In Vitromentioning

confidence: 99%

See 1 more Smart Citation

Expression of HSP47, a collagen-specific chaperone, in normal and diseased human liver

Brown

Broadhurst

Mathahs

et al. 2005

Laboratory Investigation

View full text Add to dashboard Cite

HSP47 is a collagen-specific chaperone that is required for normal collagen synthesis. In animal models of liver injury, hepatic stellate cells (HSC) have been identified as a source of HSP47. Because expression of HSP47 has not been investigated in human liver, the aim of these studies was to characterize expression of HSP47 in human liver and to investigate its regulation in human HSC in vitro. Immunohistochemistry demonstrated staining for HSP47 along the sinusoids of normal and cirrhotic human livers and in fibrous septa. Dual fluorescence confocal microscopy showed colocalization of HSP47 with synaptophysin, a marker for HSC. Levels of immunoreactive HSP47 and its transcript tended to be higher in cirrhotic livers than in normal livers. The abundance of HSP47 protein was unchanged by treatment of cultured human HSC with TGF-b1, angiotensin II, hypoxia and a number of other treatments intended to increase collagen synthesis. A modest reduction in HSP47 was achieved by transfection with antisense oligonucleotides and was associated with a significant decrease in procollagen synthesis. These observations suggest that HSP47 is constitutively expressed in human HSC and that HSP47 may be a target for antifibrotic therapy.

show abstract

Section: Discussionsupporting

confidence: 93%

Section: Modulation Of Hsp47 Expression By Human Hsc In Vitromentioning

confidence: 99%

Expression of HSP47, a collagen-specific chaperone, in normal and diseased human liver

Brown

Broadhurst

Mathahs

et al. 2005

Laboratory Investigation

View full text Add to dashboard Cite

show abstract

“…In particular, the promoter analysis of the collagen genes revealed that TGF-␤1 regulates the transcription of collagen genes via several cis-elements of their promoters (13). TGF-␤ also increases HSP47 gene expression in other cell types (29). We first demonstrated that TGF-␤ stimulates not only collagen but also HSP47 in mesangial cells.…”

Section: Quantitation Of the Expression Ratio Of Hsp47/gapdh Mrna Andmentioning

confidence: 87%

“…Here, we also observed that the expression of HSP47 was regulated by Smad1 under AGE exposure. Yamamura et al (29) has reported that TGF-␤ transcriptionally activates HSP47 gene expression. Thus, Smad1 may partially participate in the TGF-␤-mediated up-regulation of HSP47.…”

Section: Quantitation Of the Expression Ratio Of Hsp47/gapdh Mrna Andmentioning

confidence: 99%

Advanced Glycation End Products Increase Collagen-specific Chaperone Protein in Mouse Diabetic Nephropathy

Ohashi

Abe

Takahashi

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Advanced glycation end products (AGEs) appear to contribute to the diabetic complications. This study reports the inhibitory effect of OPB-9195 (OPB), an inhibitor of AGEs formation, and the role of a collagen-specific molecular chaperone, a 47-kDa heat shock protein (HSP47) in diabetic nephropathy. Transgenic mice carrying nitric-oxide synthase cDNA fused with insulin promoter (iNOSTg) leads to diabetes mellitus. The iNOSTg mice at 6 months of age represented diffuse glomerulosclerosis, and the expression of HSP47 was markedly increased in the mesangial area in parallel with increased expression of types I and IV collagens. OPB treatment ameliorated glomerulosclerosis in the iNOSTg mice associated with the decreased expression of HSP47 and types I and IV collagens. The expression of transforming growth factor-␤ (TGF-␤) was increased in glomeruli of iNOSTg mice and decreased after treatment with OPB. To confirm these mechanisms, cultured mesangial cells were stimulated with AGEs. AGEs significantly increased the expression of HSP47, type IV collagen, and TGF-␤ mRNA. Neutralizing antibody for TGF-␤ inhibited the overexpression of both HSP47 and type IV collagen in vitro. In conclusion, AGEs increase the expression of HSP47 in association with collagens, both in vivo and in vitro. The processes may be mediated by TGF-␤.

show abstract

“…For example, three co-expressed collagen genes are downregulated by CR (Col1a1, Col3a1 and Serpinh1), and in certain cell types, each gene is regulated by transforming growth factor-β (TGF-β) (Yamamura et al, 1998;Verrecchia et al, 2001). In mammals, it has been proposed that CR decreases TGF-β expression, and that this effect is due to lowered oxidative stress, along with reduced 4-hydroxy-2,3-nonenal (HNE) and activator protein 1 activity (AP-1) (Chiarpotto et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Genes regulated by caloric restriction have unique roles within transcriptional networks

Swindell

2008

Mechanisms of Ageing and Development

View full text Add to dashboard Cite

Caloric restriction (CR) has received much interest as an intervention that delays age-related disease and increases lifespan. Whole-genome microarrays have been used to identify specific genes underlying these effects, and in mice, this has led to the identification of genes with expression responses to CR that are shared across multiple tissue types. Such CR-regulated genes represent strong candidates for future investigation, but have been understood only as a list, without regard to their broader role within transcriptional networks. In this study, co-expression and network properties of CR-regulated genes were investigated using data generated by more than 600 Affymetrix microarrays. This analysis identified groups of co-expressed genes and regulatory factors associated with the mammalian CR response, and uncovered surprising network properties of CR-regulated genes. Genes downregulated by CR were highly connected and located in dense network regions. In contrast, CR-upregulated genes were weakly connected and positioned in sparse network regions. Some network properties were mirrored by CR-regulated genes from invertebrate models, suggesting an evolutionary basis for the observed patterns. These findings contribute to a systems-level picture of how CR influences transcription within mammalian cells, and point towards a comprehensive understanding of CR in terms of its influence on biological networks.

show abstract

Transcriptional Activation of the Mouse HSP47 Gene in Mouse Osteoblast MC3T3-E1 Cells by TGF-β1

Cited by 45 publications

References 48 publications

Expression of HSP47, a collagen-specific chaperone, in normal and diseased human liver

Expression of HSP47, a collagen-specific chaperone, in normal and diseased human liver

Advanced Glycation End Products Increase Collagen-specific Chaperone Protein in Mouse Diabetic Nephropathy

Genes regulated by caloric restriction have unique roles within transcriptional networks

Contact Info

Product

Resources

About