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Independent regulation of sterol regulatory element-binding proteins 1 and 2 in hamster liver.

Sheng, Z, Otani, H, Brown, M S, Goldstein, J L·1995·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.92.4.935
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Abstract

Two sterol regulatory element-binding proteins (SREBPs, designated SREBP-1 and SREBP-2), each approximately 1150 amino acids in length, are attached to membranes of the endoplasmic reticulum and nuclear envelope in human and hamster tissue culture cells. In the absence of sterols, soluble fragments of approximately 470 amino acids are released from both proteins by proteolytic cleavage. The soluble fragments enter the nucleus, where they bind to sterol regulatory elements in the promoters of genes encoding the low density lipoprotein receptor and 3-hydroxy-3-methylglutaryl CoA synthase, thereby activating transcription. Proteolytic processing of both SREBPs is blocked coordinately by sterol overloading and enhanced coordinately when sterols are depleted by treatment with an inhibitor of cholesterol synthesis. In contrast to these findings in cultured cells, the current data show that SREBP-1 and -2 are not coordinately regulated in hamster liver. In untreated animals the soluble fragment of SREBP-1, but not of SREBP-2, was detected by immunoblotting of a liver nuclear extract. Depletion of sterols by treatment with a bile acid-binding resin (colestipol) and a cholesterol synthesis inhibitor (mevinolin) led to a marked increase in the nuclear form of SREBP-2 and a reciprocal decline in the nuclear form of SREBP-1. These findings suggest that SREBP-1 is responsible for basal transcription of the low density lipoprotein receptor and 3-hydroxy-3-methylglutaryl CoA synthase genes in hamster liver and that SREBP-2 is responsible for the increased transcription that follows sterol depletion with a bile acid-binding resin and a cholesterol synthesis inhibitor.

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  • In liver cells, when intracellular cholesterol levels rise, LDLR mRNA levels fall substantially along with transcripts of other SREBP target genes.

    “In liver cells, when intracellular cholesterol levels rise, LDLR mRNA levels fall substantially along with transcripts of other SREBP target genes”

    From A novel posttranscriptional mechanism for dietary cholesterol-mediated suppression of liver LDL receptor expression (2014) · cites this paper as [13]

    The abstract (p. 935) links sterol depletion in hamster liver to increased transcription of the LDL receptor and HMG-CoA synthase genes. It also describes sterol overloading as blocking SREBP processing in cultured cells, but does not report that rising cholesterol substantially lowers LDLR mRNA and other SREBP-target transcripts in liver cells. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • Over-accumulation of dietary cholesterol in the liver prevents proteolytic activation of SREBPs and leads to a decline in expression of SREBP target genes, including LDLR and SREBP2 itself.

    “Over-accumulation of dietary cholesterol in the liver prevents the proteolytic activation of SREBPs and leads to a decline in the expression of SREBP target genes, including LDLR and SREBP2 itself.”

    From A novel posttranscriptional mechanism for dietary cholesterol-mediated suppression of liver LDL receptor expression (2014) · cites this paper as [13]

    The Abstract (p. 935) says sterol overloading blocks proteolytic processing of both SREBPs in cultured cells and identifies LDLR as a gene whose transcription SREBPs activate. It contrasts those findings with non-coordinated regulation in hamster liver; it does not show that dietary cholesterol accumulation in liver blocks both SREBPs or lowers expression of LDLR and SREBP2 itself. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

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Citations

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Research works printed but not linked: 18

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Metadata

Authors
Sheng, Z., Otani, H., Brown, M. S., & Goldstein, J. L.
Affiliations
Department of Molecular Genetics, University of Texas Southwestern Medical Center at Dallas 75235.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1995-02-14
Volume
92
Issue
4
Pages
935-938
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.92.4.935
Cited by
265
References
2
Language
en

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