The Kruppel-like Factor Zf9 and Proteins in the Sp1 Family Regulate the Expression of HSP47, a Collagen-specific Molecular Chaperone

Yasuda, Kouji; Hirayoshi, Kazunori; Hirata, Hiromi; Kubota, Hiroshi; Hosokawa, Nobuko; Nagata, Kazuhiro

doi:10.1074/jbc.m208558200

Cited by 33 publications

(19 citation statements)

References 45 publications

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“…By Western analysis, Zf9 in control kidney lysates was just detectable as two immunoreactive peptides of 42 and 46 kD, as shown in Figure 2, similar to its expression in cultured cells [16,23]. Examination of lysates obtained at various periods of reflow following kidney ischemia confirmed the marked induction of Zf9 protein (both the 42 and the 46 kD peptides), as suggested by our previous mRNA expression analysis.…”

Section: Induction Of Mouse Kidney Zf9 and Tgf-b1 Protein After Ischemiasupporting

confidence: 69%

Induction of Zf9 in the kidney following early ischemia/reperfusion

Tarabishi¹,

Zahedi²,

Mishra³

et al. 2005

Kidney International

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Section: Induction Of Mouse Kidney Zf9 and Tgf-b1 Protein After Ischemiasupporting

confidence: 69%

Induction of Zf9 in the kidney following early ischemia/reperfusion

Tarabishi¹,

Zahedi²,

Mishra³

et al. 2005

Kidney International

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“…11 These findings are particularly intriguing in view of that fact that the transcriptional regulation of HSP47 in BALB/c 3T3 cells involves the Kruppel-like factor KLF6 (Zf9). 28 In rat HSC, KLF6 is rapidly induced in response to liver injury and participates in the regulation of genes associated with the fibrogenic phenotype of HSC. 29 Based on these observations, HSP47 expression by HSC might be predicted to be regulated in an activation-dependent manner.…”

Section: Discussionmentioning

confidence: 99%

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

Brown

Broadhurst

Mathahs

et al. 2005

Laboratory Investigation

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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.

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“…COPEB is expressed in pre-adipocytes [26] and is one of the many immediate early genes following adipogenic stimulation. However, it is also expressed in large number of other cell types such as endothelial cells [33], neurophils [36] and fibroblasts [64], allowing for differences in expression due to differences in sample constitution. We conclude that adipose samples within one depot are highly homogenous and that analysis of one biopsy will provide representative data for a single depot.…”

Section: Discussionmentioning

confidence: 99%