Srebps
Mostrando 1-12 de 49 artigos, teses e dissertações.
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1. Lipid lowering and polymorphisms effects on the expression of HMGCR, LDLR, SREBF1a, SREBF2, SCAP and NPC1L1 genes in hypercholesterolemic subjects. / Efeitos de hipolipemiantes e polimorfismos sobre a expressão dos genes HMGCR, LDLR, SREBF1a, SREBF2, SCAP e NPC1L1 em indivíduos hipercolesterolêmicos.
A homeostase do colesterol é mediada por proteínas envolvidas na absorção (NPC1L1), regulação (SREBP1, SREBP2, SCAP), síntese (HMGCR) e remoção plasmática (LDLR). Os fármacos inibidores da síntese (vastatinas) e absorção (ezetimiba) do colesterol são potentes agentes hipocolesterolemiantes. Alterações em vários genes têm sido associadas a
Publicado em: 2008
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2. Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi
The proteolytic cleavage of sterol regulatory element-binding proteins (SREBPs) is regulated by SREBP cleavage-activating protein (SCAP), which forms complexes with SREBPs in membranes of the endoplasmic reticulum (ER). In sterol-depleted cells, SCAP facilitates cleavage of SREBPs by Site-1 protease, thereby initiating release of active NH2-terminal fragment
The National Academy of Sciences.
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3. Overexpression of Insig-1 in the livers of transgenic mice inhibits SREBP processing and reduces insulin-stimulated lipogenesis
In the current studies we generated transgenic mice that overexpress human Insig-1 in the liver under a constitutive promoter. In cultured cells Insig-1 and Insig-2 have been shown to block lipid synthesis in a cholesterol-dependent fashion by inhibiting proteolytic processing of sterol regulatory element–binding proteins (SREBPs), membrane-bound transcrip
American Society for Clinical Investigation.
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4. Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
This paper describes insig-2, a second protein of the endoplasmic reticulum that blocks the processing of sterol regulatory element-binding proteins (SREBPs) by binding to SCAP (SREBP cleavage-activating protein) in a sterol-regulated fashion, thus preventing it from escorting SREBPs to the Golgi. By blocking this movement, insig-2, like the previously descr
The National Academy of Sciences.
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5. Specificity in cholesterol regulation of gene expression by coevolution of sterol regulatory DNA element and its binding protein
When demand for cholesterol rises in mammalian cells, the sterol regulatory element (SRE) binding proteins (SREBPs) are released from their membrane anchor through proteolysis. Then, the N-terminal region enters the nucleus and activates genes of cholesterol uptake and biosynthesis. Basic helix–loop–helix (bHLH) proteins such as SREBPs bind to a palindro
The National Academy of Sciences.
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6. Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis.
Cellular cholesterol homeostasis is controlled by sterol-regulated proteolysis of membrane-bound transcription factors called sterol-regulatory element binding proteins (SREBPs). CPP32, a cysteine protease, was shown previously to cleave SREBP-1 and SREBP-2 in vitro at an aspartic acid between the basic helix-loop-helix leucine zipper domain and the first tr
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7. Coactivator-Dependent Acetylation Stabilizes Members of the SREBP Family of Transcription Factors
Members of the SREBP family of transcription factors control cholesterol and lipid homeostasis and play important roles during adipocyte differentiation. The transcriptional activity of SREBPs is dependent on the coactivators p300 and CBP. We now present evidence that SREBPs are acetylated by the intrinsic acetyltransferase activity of p300 and CBP. In SREBP
American Society for Microbiology.
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8. Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes
The synthesis of fatty acids and cholesterol, the building blocks of membranes, is regulated by three membrane-bound transcription factors: sterol regulatory element-binding proteins (SREBP)-1a, -1c, and -2. Their function in liver has been characterized in transgenic mice that overexpress each SREBP isoform and in mice that lack all three nuclear SREBPs as
National Academy of Sciences.
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9. SREBPs, membrane lipid biosynthesis, and fatty acids.
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10. Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins.
We have purified from hamster liver a second cysteine protease that cleaves and activates sterol regulatory element binding proteins (SREBPs). cDNA cloning revealed that this enzyme is the hamster equivalent of Mch3, a human enzyme that is related to the interleukin 1beta converting enzyme. We call this enzyme Mch3/SCA-2. It is 54% identical to hamster CPP32
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11. SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
American Society for Clinical Investigation.
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12. Transcription-dependent degradation controls the stability of the SREBP family of transcription factors
Cholesterol metabolism is tightly controlled by members of the sterol regulatory element-binding protein (SREBP) family of transcription factors. Here we demonstrate that the ubiquitination and degradation of SREBPs depend on their transcriptional activity. Mutations in the transactivation or DNA-binding domains of SREBPs inhibit their transcriptional activi
National Academy of Sciences.