Publication for Hmgcr and Srebf2

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
mmu Hmgcr 3-hydroxy-3-methylglutaryl-Coenzyme A reductase 15357 [link]
mmu Srebf2 sterol regulatory element binding factor 2 20788

Pubmed ID Priority Text
27329838 0.99 SREBP2 increase transcription of HMGCR, which upregulates the Mevalonate pathway.
0.98 SREBP-2 and nuclear factor Y (NF-Y); both SREBP-2 and NF-Y can potently induce HMGCR expression, which catalyzes activation of the mevalonate pathway.
0.98 SREBP-2 (and possibly others) to transcriptionally activate HMGCR, resulting in upregulation of the mevalonate pathway, enhanced GTPase activity, and stimulation of survival pathways, such as the HIPPO pathway (Figure 13).
0.98 SREBP2 which bind to the sterol regulatory element (SRE) in the HMGCR promoter.
0.66 HMGCR transcription factor SREBP2 was seen in p53MUT compared to p53WT cells (SREBP2 red, nuclei blue).
21767660 0.99 SREBP-2 target genes, including HMG-CoA reductase, during he initial period of the differentiation process to macrophages.
28395113 0.98 HMGCR in mouse livers was alleviated upon SREBP-2 knockdown.
0.98 SREBP-2 and CREB are important for the role of CRTC2 in regulating HMGCR transcription.
0.98 SREBP-2 target genes (HMGCR, HMGCS, and LDLR) but also ameliorated SREBP-2 gene expression at low cholesterol levels (Fig. 8B).
0.98 SREBP-2 up-regulates the transcription of HMGCR by recognizing the SRE sequence in the HMGCR promoter.
0.98 SREBP-2 transcription and, consequently, up-regulation of hepatic HMGCR and cholesterol synthesis (Fig. 8D).
0.97 sterol regulatory element binding protein 2 (SREBP-2) and its target gene 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), which is the rate-limiting enzyme in cholesterol synthesis.
0.97 SREBP-2 by interfering with the recognition of insulin response element 1 in the SREBP-2 promoter by forkhead box O1, thus inducing SREBP-2/HMGCR signaling and subsequently facilitating hepatic cholesterol synthesis.
0.97 SREBP-2/HMGCR signaling, resulting in hepatic cholesterol synthesis.
0.96 HMGCR gene promoter contains CRE and SRE binding sites, which are the targets of the CREB and SREBP-2 proteins, respectively.27 CRTC2, a coactivator of CREB, increases CREB activity following its association with residues in the carboxy-terminal basic Leu zipper domain of CREB.38 However, mutation of CRE attenuated the activity of HMGCR-Luc, though not completely.
0.96 HMGCR by SREBP-2 over CREB.
0.95 SREBP-2 target genes HMGCR and LDLR.
0.93 SREBP-2 and HMGCR) was consistent with hepatic CRTC2 levels.
0.91 HMGCR through SREBP-2.
0.89 SREBP-2 is a master regulator that controls the transcription of critical genes involved in cholesterol synthesis and uptake.29 Thus, we examined the effect of CRTC2 on HMGCR through SREBP-2.
0.75 HMGCR expression with HMGCR-Luc (mutation of SRE) and with lentivirus-mediated knockdown of SREBP-2.
0.70 SREBP-2 silencing (Lv-SiSREBP-2) to further determine the role of SREBP-2 in the CRTC2-induced regulation of HMGCR (Fig. 6F, left).
27502578 0.98 Srebf2, Fasn and Hmgcr were hypomethylated in the BPA-exposed mice, which is very likely to contribute to the promoted transcription of Srebf1 and Srebf2 and their targets.
0.97 Srebf2, Fasn and Hmgcr (Fig. 5A-D).
0.97 Srebf2 and Hmgcr (Fig. 7A-D).
0.97 Srebf2 decreased Hmgcr expression (Fig. 7E-H).
0.97 Srebf2 lead to decreased expression of Fasn and Hmgcr, respectively.
0.97 Srebf2 with Hmgcr.
0.97 Hmgcr expression by Srebf2 knockdown were compromised by BPA treatment.
0.96 Srebf2, CpG sites11, 13, 14, 15 of Fasn, CpG sites 2, 5 of CGI-A of Hmgcr and CpG sites 1, 2, 7 of CGI-B of Hmgcr (Fig. 5A-D).
0.96 Srebf2, Fasn and Hmgcr induced by BPA treatment also progressed with treatment duration.
0.92 Srebf2, Fasn and Hmgcr decreased with aging in our BPA and control mice.
0.90 Srebf2, CpG sites 1, 2, 8, 13, 14, 15 of Fasn, CpG sites 1, 2, 5 of CGI-A of Hmgcr and CpG sites 1, 7, 11 of CGI-B of Hmgcr.
0.89 Srebf2, the average DNA methylation levels of Fasn and Hmgcr also decreased with aging in both groups.
0.88 Srebf2, CpG sites 1, 2, 11, 12, 13, 14, 15 of Fasn, CpG sites 1of CGI-A of Hmgcr and CpG sites 1, 7 of CGI-B of Hmgcr.
0.85 Srebf2, Fasn and Hmgcr in the BPA-exposed mice were significantly lower than the control mice.
0.84 Hmgcr expression by Srebf2 knockdown were compromised by BPA treatment compared with the control (treated with DMSO).
26634251 0.98 SREBP-2 binding coincident with SHP binding was detected at genes related with sterol biosynthesis, including the rate-limiting enzyme HMGCR, a master transcription activator, SREBP-2, and its partner proteins, INSIG and SCAP (Fig. 4c, Additional file 1: Figure S3).
0.98 SREBP-2 antibody, Hmgcr sequence enriched by re-precipitation with SHP antibody was increased by FGF19 (Fig. 6e).
0.98 SREBP-2 at Hmgcr was not increased by FGF19 (Fig. 5b), these results suggest that SREBP-2 binds constitutively to Hmgcr and recruits SHP to the gene upon FGF19 treatment.
0.98 Hmgcr, Insig-1, and Srebp-2 by FGF19 treatment was nearly abolished when SREBP-2 was downregulated in hepatocytes (Fig. 6f), indicating that SHP occupancy is dependent on SREBP-2.
0.98 SREBP-2 target genes related with sterol biosynthesis, including Hmgcr.
0.97 SREBP-2 target sterol biosynthesis-related genes (Fig. 7e) and significantly decreased HMGCR protein levels in WT mice (Fig. 7f).
0.96 SREBP-2 binding, published previously, at many sterol biosynthetic genes, including the HMG CoA Reductase (Hmgcr) gene.
0.96 SREBP-2 at Hmgcr, resulting in epigenomic repression
0.86 SREBP-2 transactivation by FGF19, we examined the effects of mutation of Thr-55 on expression of Hmgcr, Insig, and Srebp-2 genes using luciferase reporter plasmids containing the promoter regions of these genes that bound both SHP with SREBP-2.
29968750 0.98 SREBP2 and an increase in phospho ACC/ACC and phospho HMGCR/HMGCR ratio involved in the de novo lipogenesis and cholesterol deposition in PA-treated cells.
0.98 SREBP2/HMGCR and PPARalpha/CPT1A/UCP2 signaling pathways plays an important role in mediating the prophylactic role of HIET against PA-induced intracellular lipid accumulation.
0.97 SREBP2 controls the cholesterol homeostasis via activating the gene, HMGCR, required for cholesterol synthesis.
0.97 SREBP2, and HMGCR and up-regulated the protein expressions of phospho ACC, phospho HMGCR, PPARalpha, CPT1A, and UCP2 in PA-treated cells.
0.96 SREBF2, and HMGCR and up-regulated the mRNA expressions of PPARA, CPT1A, and UCP2 in PA-treated cells.
0.96 SREBP2/HMGCR and PPARalpha/CPT1A/UCP2 signaling pathways in PA-treated hepatocytes.
0.96 SREBF2, and HMGCR and an increase in PPARA, CPT1A, and UCP2 in PA-treated cells.
0.93 SREBP2, and HMGCR and the downregulation of phospho ACC, phospho HMGCR, PPARalpha, CPT1A, and UCP2.
0.91 SREBP2, and HMGCR and up-regulate the phospho ACC, phospho HMGCR, PPARalpha, CPT1A, and UCP2 protein expression in PA-treated cells.
25489402 0.98 HMG-CoA reductase is associated with SREBP-2, AMPK, and ACAT-2 in hepatic cholesterol synthesis.
0.96 sterol regulatory element binding protein-2 (SREBP-2), and 3-hydroxyl-3-methylglutaryl coenzyme A (HMG-CoA) reductase was decreased, while expression of phosphorylated adenosine monophosphate activated protein kinase (p-AMPK)/AMPK ratio, cholesterol 7-alpha-hydroxylase (CYP7a1), and sterol 12-alpha-hydroxylase (CYP8b1) was increased in mice fed red rice.
0.96 HMG-CoA reductase, ACAT-2 and SREBP-2 expression, and the increased degradation of cholesterol by the increased expression of CYP7a1 and CYP8b1.
0.96 SREBP-2, HMG-CoA reductase, and p-AMPK/AMPK ratio.
0.95 HMG-CoA reductase, ACAT-2, p-AMPK/AMPK, and SREBP-2, and by enhancing hepatic cholesterol degradation through CYP7a1 and CYP8b1 in mice fed a hypercholesterolemic diet.
0.93 HMG-CoA reductase, and SREBP-2, and by enhancing hepatic cholesterol degradation through CYP7a1 and CYP8b1 in mice fed a hypercholesterolemic diet.
0.91 HMG-CoA reductase and SREBP-2 in mice fed a high fat diet, and by inhibition of HMG-CoA reductase and p-AMPK in hepatoma cells.
29237705 0.98 HMGCR promoter synchronized by beta-catenin and SREBP2N.
0.97 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) is tightly regulated by sterol regulatory element-binding transcription factor 2 (SREBP2).
0.97 SREBP2 (SREBP2N) to regulate the expression of HMGCR.
0.96 HMGCR promoter impaired the increased HMGCR mRNA level synchronized by LiCl and SREBP2N.
0.96 HMGCR promoter induced by SREBP2N (Fig. 5 G).
0.94 SREBP2N and HMGCR promoter (Fig. 5 I), but also blunted the induction of HMGCR by exogenous SREBP2N (Fig. 5 J).
0.89 HMGCR promoter (dCas9 2 and dCas9 5) impaired the interaction between SREBP2 and TBE2 in the HMGCR promoter.
30679938 0.98 SREBP-2 and its target genes HMG-CoAR and 3-hydroxy-3-methylglutaryl-Coenzyme A synthase (HMG-CoAS), which are key enzymes in cholesterol biosynthesis.
0.97 SREBP-2 is responsible for cholesterol-related genes, e.g., HMG-CoAR (a key enzyme in cholesterol biosynthesis).
0.97 SREBP-2 expression, resulting in low HMG-CoAR expression, which led to marked decreases in both serum and hepatic levels of TC and TG in SCLE treated mice.
0.97 SREBP-2 and the target gene HMG-CoAR; II: the AMPK phosphorylation also stimulated the ATGL, HSL expression and the phosphorylation of HSL to modulate hydrolysis of triglyceride; III: enhanced the activity and expression of CAT and ACO to promote fatty acid beta-oxidation.
0.97 SREBP-2 and the target gene HMG-CoAR.
0.93 SREBP-2 and HMG-CoAR expression levels.
0.74 SREBP-2 and HMG-CoAR mRNA levels.
30785396 0.98 SREBP-2 were reduced in Ubiad1Ki/Ki MEFs (Figure 4A, compare lanes 3 and 4), which is consistent with reduced levels of Hmgcr mRNA and increased levels of intracellular cholesterol (Figure 4B).
0.98 SREBP-2 and its target genes (including HMGCR) were elevated in livers of lovastatin-treated animals; mRNA for SREBP-1c was reduced by the inhibitor (Figure 6:figure supplement 1).
0.98 HMGCR protein in Ubiad1Ki/Ki corneas was accompanied by reduced levels of mRNAs encoding SREBP-2, HMGCR, and other cholesterol biosynthetic enzymes (Figure 7C).
0.98 HMGCR protein occurred despite reduced levels of its mRNA (Figures 1 and 2), which was attributable to reduced proteolytic activation of SREBP-2 (Figures 1B and 2A) resulting from accumulation of hepatic cholesterol (Figure 1:figure supplement 1B and Table 1).
0.97 HMGCR protein persisted in livers of Ubiad1Ki/Ki mice fed cholesterol, even though the feeding regimen continued to block proteolytic activation of SREBP-2 (Figure 5A and C) and reduce levels of mRNAs for HMGCR and other SREBP-2 targets (Figure 5:figure supplement 1).
0.94 HMGCR and UBIAD1 proteins (lanes 1-3), whereas levels of nuclear SREBP-1 and SREBP-2 were either unchanged (nuclear SREBP-1, lanes 4-6) or reduced (nuclear SREBP-2, lanes 7-9).
0.93 HMGCR protein primarily by inhibiting activation of SREBP-2 (35); similar results were obtained in the current study (Figure 5C).
26180602 0.98 SREBP-2 enters the nucleus to induce transcription of its target genes such as HMGCR which mediates the rate-limiting step in cholesterol synthesis.
0.96 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) and sterol regulatory element binding protein 2 (SREBP-2) were found to be statistically decreased in FO+ALA-PS-treated but not FO-treated animals, as compared to those in HFD-fed animals.
0.96 SREBP-2 and HMGCR play a pivotal role in cholesterol homoeostasis.
0.96 SREBP-2 and HMGCR in hamster given high cholesterol diet.
0.94 SREBP-2 pathway to downregulate HMGCR expression, which in turn reduce the cholesterol synthesis.
0.51 HMGCR and SREBP-2 were observed in FO+ALA-PS group but not in FO group.
27211556 0.98 SREBP2 (Srebf2), 3-hydroxy-3-methylglutaryl-CoA reductase (Hmgcr), 3-hydroxy-3-methylglutaryl-Coenzyme A synthase (Hmgcs) and the liver X receptor alpha (LXRalpha, Nr1h3)), which are all important in cholesterol synthesis, were significantly decreased by irisin treatment.
0.98 Srebf2, Hmgcr, Hmgcs and Ldlr were decreased by irisin treatment in the presence or absence of OA in cultured hepatocytes (Fig. 4b).
0.98 Srebf2, Hmgcr, Hmgcs and LXRalpha were decreased by treatment of hepatocytes with irisin in the presence or absence of OA (Fig. 4f).
0.97 SREBF2, HMGCR and HMGCS was significantly blocked by inhibition of AMPK by AMPKalpha1 knockdown (Fig. 7c).
0.94 Srebf2, Hmgcr and Hmgcs (Supplemental Fig. 3).
0.91 SREBP2 and its target genes HMGCS2 and HMGCR, a key transcriptional factor and the rate-limiting enzymes for cholesterol synthesis respectively; 4) The effects of irisin on genes related to triglyceride synthesis and beta-oxidation were negligible in hepatocytes.
28808191 0.98 SREBP2 to the SRE of the LDLR gene and HMGCR gene promotes transcription of the mRNAs, ultimately resulting in increased LDLR protein on the cell surface and increased HMGCR protein in the ER membrane.
0.98 HMGCR and INSIG1 (lowering endogenous synthetic levels of cholesterol), stimulate the expression of IDOL to degrade LDLR, and stimulate the expression of ABCA1/ABCG1 to promote cholesterol removal from the cell, thereby acting as an effective foil to the SREBP2 pathway.
0.98 HMGCR is activated by SREBP2.
0.98 SREBP2, which can lead to a confounding effect of low cellular cholesterol levels leading to upregulation of HMGCR, LDLR (increasing cellular cholesterol levels through endogenous and exogenous pathways) and upregulation of PCSK9 (decreasing cell surface levels of LDLR).
0.98 SREBP2 trafficking and processing, leading to a downregulation of HMGCR expression, especially under chronic high LDL-C conditions.
0.98 SREBP2, thereby preventing upregulation of transcription of LDLR and HMGCR (among others).
28970592 0.98 sterol-regulatory element-binding protein-2 (SREBP-2), hepatocyte nuclear factor 1alpha (HNF-1alpha), and 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase in LDLR+/- mice.
0.97 sterol-regulatory element-binding protein-2 (SREBP-2), hepatocyte nuclear factor 1alpha (HNF-1alpha), and 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase in LDLR+/- mice.
0.97 SREBP-2, HNF-1alpha and HMG-CoA reductase.
0.97 SREBP-2, HNF-1alpha and HMG-CoA reductase, which indicated that PCSK9Qbeta-003 vaccine also regulated lipid homeostasis.
0.94 HMG-CoA reductase and increases circulating levels of PCSK9 by as much as 30%, compared with placebo, making them somewhat self-limiting to further reduce LDL-C. This likely occurs because the transcription factor SREBP-2, that is indirectly up-regulated by statin, activates the Ldlr and Pcsk9 genes.
0.82 SREBP-2, which activates the Ldlr and Pcsk9 genes, and thus makes statin somewhat self-limiting to further reduce LDL-C. To assess the effect of PCSK9Qbeta-003 vaccine on lipid homeostasis in LDLR+/- mice, we evaluated the mRNA expression of SREBP-2, HNF-1alpha and HMG-CoA reductase in liver.
31239739 0.98 HMGCR and LDLr is mediated via a negative feedback mechanism that is tightly controlled by the other two proteins, SREBP-2 and SREBP SCAP, which are important for keeping a balance of cholesterol at cell and systemic level.
0.98 SREBP2-LDLr negative feedback system is disrupted by damage factors, the increasing HMGCR-mediated cholesterol synthesis and LDLr-mediated cholesterol uptake may exacerbate cholesterol accumulation in kidneys, subsequently causing renal injuries mediated by lipids.
0.97 HMGCR is the key enzyme for cholesterol synthesis and low density lipoprotein receptor (LDLr) is the mediator of cholesterol uptake, the two key proteins which are predominantly regulated by SREBP-2.
0.97 SREBP2, and SCAP expression, the renal expression of HMGCR protein was down-regulated with an increasing dose of quercetin in db/db mice as compared with diabetic controls after treatment for 10 weeks, and the differences were statistically significant (P<0.05, Figure 8B).
0.96 HMGCR, SREBP-2, and SCAP subsequently attenuated the renal lipid profile change and lipid droplet accumulation, resulting in the alleviation of renal injury of db/db mice.
0.93 SREBP2-LDLr signaling pathway and the expression of HMGCR in the kidneys, could be therapeutic mechanisms for ameliorating early stage DN.
27200103 0.98 SREBP-2 is a leucine zipper transcription factor that controls a rate-limiting enzyme in cholesterol synthesis, HMG-CoA reductase (HMGCR), when the factor binds sterol response element.
0.98 SREBP-2 and the knockdown of SREBP-2 induced downregulation of AACS and HMGCR gene expression.
0.97 SREBP-2, AACS, and HMGCR mRNA levels were dramatically suppressed in the mice that were fed FAVA (Figures 5(b) and 5(c)).
0.97 SREBP2, AACS, and HMGCR mRNA levels.
0.92 SREBP-2, AACS, and HMGCR RNA in the mouse liver were induced by FAVA.
27385127 0.98 SREBP-2, however, primarily targets genes of the cholesterol biosynthetic pathway, including its rate-limiting enzyme hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR).
0.98 SREBP-2 mRNA expression remained unchanged during normal differentiation, HMGCR gene expression, one of the cholesterol synthetic pathway genes preferentially regulated by SREBP-2, was also increased when cells were undergoing differentiation under normal conditions (Fig. 6C).
0.97 SREBP-2 target gene HMGCR was significantly decreased following S1P inhibition at 1, 2 and 3 days after inhibitor treatment, compared with controls.
0.95 HMGCR mRNA expression without a reduction in SREBP-2 protein levels in Schwann cells.
0.91 SREBP-2 mature form, diminished HMGCR mRNA expression was observed which was associated with a more modest reduction at the protein level than what was detected for FASN and ACC.
27929393 0.98 SREBP-2, and HMGCR.
0.98 SREBP-2 enhances the production of enzymes involved in cholesterol synthesis such as hydroxyl-methylglutryl -coenzyme A (HMG) synthase and HMGCR.
0.97 SREBP-2 mRNA expression via LXRalpha, an oxysterol receptor that induces ABCG1/5/8, and thus reduces HMGCR to produce less free cholesterol.
0.95 sterol regulatory element-binding protein-2 (SREBP-2), acetyl-CoA carboxylase (ACC), HMG-CoA reductase (HMGCR), ATP-binding cassette transporter G5/G8 (ABCG5/8), cholesterol 7 alpha-hydroxylase (CYP7A1), and sterol 12-alpha-hydroxylase (CYP8B1), as well as oxidative stress markers, including superoxide dismutase 1 (SOD1), superoxide dismutase 2 (SOD2), glutathione peroxidase (GPX), and catalase, were also regulated by XB supplementation.
0.73 SREBP-2 and HMGCR.
28262793 0.98 SREBP-2 also induces expression of the key enzyme of cholesterol biosynthesis, HMG-CoA reductase.
0.98 SREBP-2 activation was enhanced and SREBP-2 target genes were upregulated in S1P lyase-deficient MEFs, leading to enhanced cholesterol uptake which compensated for decreased HMG-CoA reductase protein expression and cholesterol biosynthesis.
0.96 SREBP-2 activation and induced HMG-CoA reductase downregulation in wild-type MEFs, but the effects were not significant (Fig. 7).
0.83 SREBP-2 and protein expression of HMG-CoA reductase and APP.
0.80 SREBP-2 and expression of HMG-CoA reductase.
28275691 0.98 SREBP-2, which induces the expression of 3-hydroxy-3-methylglutaryl-coenzyme A-CoA reductase (HMGCR) and low-density lipoprotein receptor (LDLR) to increase intracellular cholesterol levels.
0.98 SREBP-2 cleavage and higher HMGCR and LDLR mRNA levels (Figure 4C and D).
0.98 SREBP-2, HMGCR, and LDLR mRNA levels were repressed in DIO mice as a result of cholesterol accumulation, and were induced in ChTM-fed mice as a result of CYP7A1 induction (Figure 9C).
0.98 SREBP-2 activity and the expression of SREBP-2 target genes LDLR and HMGCR, leading to reduced cholesterol uptake and de novo cholesterol synthesis.
0.98 SREBP-2 activation, leading to induction of LDLR and HMGCR expression to replenish cellular cholesterol.
28427397 0.98 SREBP-2 promotes the expression of target genes involved in cholesterol biosynthesis such as 3-hydroxy-3-methylglutaryl-CoA synthase (HMGCS), HMGCR and LDLR.
0.95 SREBP-2, HMGCR, LPL, and apo B significantly decreased in a dose dependent manner in the HVC1-treated groups compared to that in the HCD group.
0.95 SREBP-2, HMGCR, LPL, and apoB and increased that of LXR in the liver tissue of HCD-fed LDLR-/- mice.
0.95 SREBP-2 and HMGCR.
0.94 SREBP-2 and HMGCR in the HCD group compared to that in the ND group.
30954949 0.98 Srebp2 led to the augmented expression of cholesterol biosynthesis genes, including Hmgcr, Sqle and Mvd (figure 2D), resulting in highest CE levels in Fasn(-) HCC (figures 2D and 4D).
0.98 HMGCR in a SREBP2-dependent manner, as silencing of SREBP2 blocked siFASN-induced HMGCR upregulation (figures 6B and online supplementary figure S21).
0.98 sterol regulatory element binding protein 2 (Srebp2), which upregulates the key enzyme Hmgcr of cholesterol biosynthesis, resulting in cholesterol accumulation and, eventually, HCC formation.
0.97 SREBP2 (figure 6C, D), as well as increased HMGCR mRNA expression (figure 6E).
0.89 SREBP2/HMGCR and the related cholesterol biosynthesis contribute to hepatocarcinogenesis.
18852694 0.98 SREBP2 controls expression of LDLR and 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme for cholesterol synthesis (Brown and Goldstein, 1997; Shimano, 2001).
0.97 HMG-CoA reductase, another target gene of SREBP2.
0.93 SREBP2 by fenofibrate, we evaluated the expression of HMG-CoA reductase mRNA, another target gene regulated by SREBP2 activity.
0.90 sterol regulatory element-binding protein 2 (SREBP2) and expression of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, but has no effect on the expression of SREBP cleavage-activating protein (SCAP).
21109190 0.98 HMGCR, farnesyl diphosphate synthase (FDPS) and squalene epoxidase (SQLE), as well as those of the cytoplasmic precursor form of SREBP-2 were decreased as assessed by Western blotting (Figure 1D).
0.98 Srebf2 mRNA and a 38% decrease in Hmgcr mRNA (Figure 2D).
0.97 Srebf2 mRNA and those for two of its downstream targets - Hmgcr and Fdps (Figure S3A).
0.95 Srebf2 and Hmgcr genes in primary cultured mouse hippocampal neurons (Figure 6C).
23080229 0.98 SREBP-2, HMG-CoAR, FAS and CYP7A1.
0.97 SREBP-2, FAS, HMG-CoAR and C/EBP-beta was blunted in CHOP-/- mouse primary hepatocytes.
0.97 SREBP-2, FAS, HMG-CoAR and C/EBP-beta was inhibited in CHOP-/- mice.
0.97 SREBP-2, HMG-CoAR, FAS, and C/EBPbeta, and reduced CYP7A1 expression.
24768901 0.98 SREBP2 show that the levels of Plin5 mRNA and protein were significantly decreased following SREBP2 overexpression, while known SREBP2 targets (Ldlr and Hmgcr) were induced, and the expression of Plin2 and Plin3 did not change under the same conditions (Fig. 2B, D).
0.96 Srebp-2 and SREBP-2 targets (Hmgcr, Pcsk9) (Fig. S1A).
0.96 Srebp2 prevented the induction of both Ldlr and Hmgcr by simvastatin.
0.96 SREBP2 would control cholesterogenesis by both upregulating the expression of enzymes (i.e. HMGCR) and promoting substrate availability.
25237360 0.98 HMG-CoA reductase) and sterol regulatory element binding factor-2 (SREBF-2).
0.98 sterol regulatory element binding factor-2 that activates transcription of genes for HMG-CoA reductase and other enzymes of the pathway for cholesterol synthesis.
0.98 HMG-CoA reductase as well as SREBF-2 expression by AR and ARD extract may be a major mechanism leading to the attenuated biosynthesis of lipids in liver.
0.94 HMG-CoA reductase, SREBF-2 and cholesterol-7alpha-hydroxylase (CYP7A1) in order to find the potential molecular mechanism by which ARD modulated lipid profiles.
29073233 0.98 SREBF2, SREBF1c, and HMGCR by a protein kinase AMPK inhibits transcriptional activity of SREBFs and enzyme activity of HMGCR.
0.98 SREBF2 target Hmgcr, a key enzyme in cholesterol biosynthesis, were decreased only by 18% in female mice and by 13% in male mice (Fig 4A).
0.96 SREBF2 and HMGCR, the two key players in cholesterol biosynthesis, was unchanged (Fig 5A and 5B), suggesting that transcriptional regulation of cholesterol biosynthesis was not significantly activated in the Cyp46a1-/- brain.
0.74 Srebf2 and Hmgcr in the Cyp46a1-/- brain (Fig 4A) did not appear to translate into the decreases at the protein level.
29183708 0.98 SREBP-2 translocates to the nucleus, where it binds to sterol response elements (SREs) present in the promoters of sterol-responsive genes, including HMGCR and the low-density lipoprotein receptor (LDLR), thus promoting cholesterol biosynthesis and uptake.
0.98 HMGCR and by targeting the transcription factors (SREBP-1 and SREBP-2) that control the expression of these enzymes (Figure 1).
0.97 HMGCR expression, a number of miRNAs have also been reported to control cholesterol synthesis indirectly by targeting SREBP-2 and INSIG.
0.96 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), or indirectly targeting the important regulators in biosynthesis pathway including sterol regulatory element-binding protein-2 (SREBP-2) and insulin induced gene (INSIG).
29738536 0.98 SREBP2 cleavage and CBP gene expression as a response to reduced cholesterol biosynthesis triggered by HMG-CoA reductase inhibition in several cell types.
0.98 SREBP2 cleavage and CBP gene expression due in part to reduced cholesterol biosynthesis downstream of HMG-CoA reductase inhibition.
0.97 HMG-CoA reductase, reduces SREBP2 activation and pravastatin-induced PARP cleavage.
0.82 SREBP2 cleavage and CBP gene expression act by the same mechanism in NSPCs, we treated NSPCs with 10 muM pravastatin and either 1 muM or 10 muM of farnesyl pyrophosphate (FPP), a CBP intermediate downstream of HMG-CoA reductase and precursor to both cholesterol and isoprenoids.
30821074 0.98 SREBP-2) on the promoters of the fatty acid synthase (FAS) and 30-hydroxylmethyl glutaryl coenzyme A reductase (HMGCR), thereby stimulating their transcription and promoting hepatocyte lipogenesis and cholesterol synthesis.
0.98 SREBP-2, the mRNA levels of two critical enzymes of cholesterol biosynthesis, namely, 30-hydroxylmethyl glutaryl coenzyme A synthase (HMGCS) and 30-hydroxylmethyl glutaryl coenzyme A reductase (HMGCR), were decreased in diabetic mice with sh-YAP (Figure 4H).
0.92 SREBP-2 binding to the FAS and HMGCR promoters.
0.68 SREBP-2 depletion could also abolish the enhancement of YAP on HMGCR-luc activity (Figure 6E).
22441164 0.98 SREBP-2 and its target genes HMGCR, IDI1, FPPS, SQLE, and LSS was significantly decreased in WY-14,643-treated vs. control mouse liver (Fig. 4D).
0.98 SREBP-2 target genes (e.g., HMGCR, IDI1, FPPS, SQLE, LSS, SREBP-2) and ER stress markers (e.g., Grp78, TRIB3, ATF4, CHOP, p8) is already increased in livers from embryonic day 18.5 SW/129 Pex2-/- mice compared to controls (W.J. Kovacs and P.L. Faust, unpublished results).
0.97 SREBP-2 and its target genes HMG-CoA synthase 1 (HMGCS1), HMGCR, FPPS, IDI1, SQS, squalene epoxidase (SQLE), lanosterol synthase (LSS), 7-dehydrocholesterol reductase (DHCR7), LDL receptor (LDLR) and Insig-1 were all significantly increased 1.6- to 4.7-fold in P0 129 Pex2-/- versus control mouse liver.
23563690 0.98 SREBP2 was readily detectable at the promoters of Hmgcr and Hmgcs (Fig. 1e).
0.98 SREBP2 at the promoters of Hmgcr and Hmgcs (Fig. 1e).
0.98 Hmgcr and Hmgcs, canonical SREBP2 target genes.
25378657 0.98 SREBP-2 target genes, including Hmgcr, Hmgcs, Fpps, Ss, Ldlr, and Pcsk9.
0.87 SREBP-2 mRNA were not increased in these animals, and were not accompanied by increased expression of key SREBP-2 target genes such as Hmgcr and Hmgcs.
0.86 SREBP-2 target genes encoding enzymes in the cholesterol biosynthetic pathway, namely HMGCR, 3-hydroxy-3-methylglutaryl-CoA synthase (HMGCS), and DHCR24, were not significantly different in the three genetically modified lines of mice from those of WT mice.
25933205 0.98 SREBP-2 transgenic mice exhibit a significant increase in the rate of cholesterol synthesis and elevated expression of HMGCS (13-fold), HMGCR (75-fold) and LDLR (5.8-fold).
0.98 HMGCR, HMGCS, and the SREBP-2 precursor and nuclear active forms in the liver compared with Tshr +/+ mice.
0.97 SREBP-2 and HMGCR expression in the liver of a new transgenic mouse model with liver-specific expression of constitutively active (CA)-AMPK-alpha1, but in adipose tissue, SREBP-2 and HMGCR mRNA expression was down-regulated.
26567374 0.98 SREBP-2 (encoded by Srebf2) and many of its target genes including Hmgcr, Ldlr, and Pcsk9 in Mmp2 -/- mice (Figure 3C).
0.98 SREBP-2 pathway to decrease hepatic synthesis and uptake of cholesterol; at the same time, oxysterols activate LXR-alpha signaling to increase the clearance of hepatic cholesterol.28, 29 Consistently, WT mice fed chow supplemented with 0.15% cholesterol exhibited decreased hepatic expression of Srebf2 and Hmgcr along with a powerful induction of Cyp7a1 and Cyp27a, 2 rate-limiting enzymes in the bile acid synthesis pathways.
0.98 Srebf2, Hmgcr, Cyp7a1, and Cyp27a) showed blunted transcriptional responses reminiscent of a hepatic insensitivity to dietary cholesterol, whereas other genes such as Srebf1 and Fasn, were clearly uncoupled in their responses (Figure 4).
27284309 0.98 SREBP-2 involved in cholesterol metabolism, including 3-hydroxy-3-methylglutaryl coenzyme A synthase (Hmgcs), HMG CoA reductase (Hmgcr) and low density lipoprotein receptor (Ldlr) were also upregulated in the insulin-resistant and diabetic groups.
0.98 SREBP-2 contributes to enhanced skeletal muscle cholesterol uptake and biosynthesis by driving the expression of genes including Ldlr, Hmgcs and Hmgcr.
0.96 SREBP-2), Fasn, Acc, Scd1, Cd36/FAT, Ldlr, Hmgcs and Hmgcr significantly increased in insulin-resistant and diabetic hamsters.
30310412 0.98 HMGCR acted as the rate-limiting enzyme to catalyze endogenous cholesterol synthesis, and SREBP-2 may activate HMGCR mRNA to perform the synthesis and uptake of cholesterol.
0.96 SREBP2, CYP7A1, and CYP7B1 were downregulated, while CYP7A1, CYP7B1, LXR, and HMGCR mRNA were increased 3-fold under the administration of YCHD.
0.95 HMGCR mRNA may be closely activated by higher SREBP-2.
30609251 0.98 SREBP2, HMGCR, and HMGCS, which are related to cholesterol synthesis, was increased with aging.
0.97 SREBP2, HMGCR, and HMGCS, genes for cholesterol synthesis, was gradually increased in liver tissues during aging.
0.94 sterol regulatory element-binding protein 2 (SREBP2; Figure 3e, p = 0.006) and 3-hydroxy-3-methylglutaryl-CoA synthase 1 (HMGCS; Figure 3g, p = 0.002) were increased in 20-month-old mice, compared to the case for 2-month-old mice, and that of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) was increased in 20-month-old mice, compared to the case for 8-month-old mice (Figure 3f, p = 0.016).
19721697 0.98 SREBP-2 controls genes involved in cholesterol synthesis, such as Hmg-CoA reductase (Hmgcr), SREBP-1c mainly regulates genes implicated in lipogenesis, such as the gene encoding fatty acid synthase (FAS).
0.97 Hmgcr, Low density lipoprotein receptor (Ldlr), and Acetoacetyl-CoA synthetase (Aacs) in Rev-KO and TgRev animals suggested that the activity of SREBP2 was affected in these animals as well (Figure 1D), in spite of the apparently normal Srebp2 mRNA accumulation (Figure S4A).
21459323 0.98 SREBP-2, the elevation in mRNAs encoding two key enzymes of cholesterol biosynthesis, HMGCR and HMGCS, was prevented by S17834 in insulin resistant mice (Fig. 2E).
0.98 SREBP-2 processing and HMGCS and HMGCR expression.
22245387 0.98 Hmgcr mRNA levels and reduced expression of Srebf2 and other cholesterol biosynthesis genes are unclear, similarly uneven effects on expression of cholesterol biosynthesis genes/enzymes have been previously reported in the nervous system.
0.97 HMG-CoA reductase (HMGCR) is the rate-limiting enzyme of cholesterol biosynthesis and its expression is regulated by SREBF2.
23838163 0.98 SREBP2 along with its intronic microRNA-33 (miR-33), which replenishes cellular cholesterol by inducing genes that encode proteins such as 3-hydroxy-3-methyl-glutaryl (HMG)-CoA reductase and LDL receptor (LDLR) and suppressing the ATP-binding cassette transporter 1 (ABCA1).
0.97 SREBP2-targeted genes, ie, HMG-CoA reductase, HMG-CoA synthase, squalene synthase, and LDLR was higher with OS than PS (Figure 1C).
24025456 0.98 HMGCR and desmosterol interfered with SREBP-2 processing and reduced the expression of Hmgcr.
0.96 3-hydroxy-3-methylglutaryl-Coenzyme A reductase (HMGCR), the LDL receptor (LDLR), or sterol regulatory element binding protein, type 2 (SREBP-2) as the major cholesterol-related transcriptional regulator, did identify sex differences in disruption of cholesterol homeostasis and disease outcome (e.g., in NAFLD).
25804527 0.98 sterol regulatory element binding protein 2 (SREBP-2), the key transcription factor that induces the expression of both Ldlr and Hmgcr, was found markedly increased at 4 h TPA exposure in the skin of Tm7sf2+/+ mice (Fig. 1F).
0.97 Hmgcr) and cholesterol uptake (Ldlr), as well as increased expression of the transcription factor (Srebp-2) responsible for driving expression of these genes detected in wild type animals, were all lost in Tm7sf2-/- mice.
27694328 0.98 Srebf2, Hmgcr, Ldlr, and Pcsk9.
0.97 Srebf2 and Hmgcr when fed chow, and their response to dietary cholesterol supplementation was different from those of Mmp2 -/-, Mmp7 -/-, Mmp9 -/-, and WT mice (Figure S6).
27892461 0.98 SREBP2-dependent transcriptional regulation, including Srebf2, Ldlr, Pcsk9 and Hmgr, while a slight increase in Srebf1c expression was observed (Supplementary Fig. 6I).
0.97 SREBF2, HMGR, PCSK9 and LDLR mRNA, with maximum effects reaching 1.4, 1.3, 1.5 and 2.3-fold, respectively (Fig. 5f).
29853881 0.98 HMGCR and SREBP2/HNF4alpha/CYP7A1 pathways.
0.94 HMGCR and SREBP2/HNF4alpha/CYP7A1 pathways; therefore, we next investigated whether ARRBs participated in this process, and if so, how.
30619997 0.98 Hmgcr, including farnesyl diphosphate synthase (Fdps), squalene epoxidase (Sqle), and 7-dehydrocholesterol reductase (Dhcr7), were markedly elevated by approximately 2-fold to 3-fold in HMGCR KI livers compared to WT littermates (Fig. 3C) despite the absence of changes in the mRNA expression of the upstream activator sterol regulatory element binding transcription factor 2 (Srebf2) (Supporting Fig. S4C).
0.98 HMGCR KI livers, leading to inappropriately activated sterol regulatory element binding protein 2 (SREBP2) transcriptional activity.
31327168 0.98 Srebp2 and target genes involved in cholesterol synthesis, including Hmgcr, Acss2, Pmvk, Mvd, Fdft1, Ldlr, and Sqle (Figure 2A).
0.98 SREBP2, as well as the protein levels of SREBP targets HMGCR and ACSS2 (Figure 3C).
31573042 0.98 SREBP-2, HMGcoAR serve important roles in lipid synthesis, and the results of the present study demonstrated that DADS downregulated the expression of these genes.
0.97 SREBP-2, HMGCoAR, PPARgamma and SCD1, which are associated with lipid synthesis.
32111832 0.98 SREBP2 is primarily implicated in the regulation of genes linked to cholesterol synthesis and uptake, including those encoding for the rate-limiting enzymes in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) and squalene epoxidase (SQLE), and the low-density lipoprotein receptor (LDLR).
0.98 Srebf2 and a panel of its downstream transcriptional targets Hmgcs, Hmgcr, Sqs, Dhcr24, Pcsk9, and Ldlr (Fig. 4c).
24465397 0.98 SREBP2 expression (as assessed by both the N-terminal, representing the transgene, and the C-terminal specific primers) and a subsequent decline in the expression of its target genes HMG-CoA reductase ( Figure 7B ).
24978143 0.98 SREBP2 regulated genes including LDLR, HMGCR and PCSK9 compared with mice injected with a control lentivirus.
25739789 0.98 Hmgcr, Sqle, Dhcr24, Tm7sf2), together with Srebf2 (Fig. 3a).
25794851 0.98 Srebp-2 expression reversed hypercholesterolemia in DKO mice caused by FGF21 deficiency and concurrently reduced the expression of several cholesterologenic genes, including 3-hydroxy-3-methylglutaryl-CoA reductase, farnesyl diphosphate synthetase, squalene synthase, and 3-hydroxy-3-methylglutaryl-CoA synthetase, which are all well-known downstream targets of Srebp-2 (Figure 8C).
27707816 0.98 SREBP-2 target gene, HMG-CoA reductase (Hmgcr), as well as the SREBP-1c target gene, Fasn, indicating SCAP loss of function (supplemental Fig. S1C, D).
28150810 0.98 Hmgcr, Idi1, Sqle, Cyp51, Msmo1, Hsd17b7, and Dhcr24) were among the genes down-regulated in XX/Sry Sertoli cells, suggesting that the down-regulation of the cholesterogenic genes was primarily the result of the decreased expression of Srebf2.
28244871 0.98 SREBP-2-regulated genes involved in cholesterol biosynthesis and uptake (HMG-CoA synthase, HMG-CoA reductase, farnesyl diphosphate synthase, squalene synthase, and PCSK9) were reduced by 60-80% in hepatocyte-Srebf-2-/- livers compared to controls.
29307784 0.98 SREBP2 (Fig. 6D) despite WT females expressing higher levels of SREBP2 target proteins in de novo cholesterol synthesis, i.e. HMGCS1 (Fig. 6E) and HMGCR (Fig. 6F).
19260826 0.97 Hmgcr and Ldlr, two preferential SREBP-2 target genes, was suppressed by desmosterol.
0.95 SREBP-2 processing (Figure 4A) and decreased Hmgcr, Ldlr and Insig1 mRNA levels (Figure 4B), although less potently than 25HC.
0.94 SREBP-2 processing as well as Hmgcr, Ldlr and Insig1 expression (Supplementary Figure S2).
22394543 0.97 Hmgcr as well as Srebp-2, Cyp51 and Dhcr7 were significantly upregulated in mice on the Western diet when compared to the control group.
0.96 Srebp-2, Hmgcr, Cyp51 and Dhcr7 in liver samples of the mice fed the Western diet, suggesting that hepatic cholesterol synthesis is increased as well.
25352833 0.97 SREBP-2, HMGCR, peroxisome proliferator-activated receptor alpha (PPAR-alpha), fatty acid binding protein (L-FABP), and carnitine palmitoyltransferase 1A (CPT1A) was decreased.
0.94 SREBP-2 and HMGCR and decreased expression of liver X receptor (LXR)-alpha, LXR-beta, and ABCA1 in kidneys of these mice.
26311497 0.97 HMGCR, HMGCS, LDLR, FDPS, SS, ACC, FAS, SCD-1 and GPAT, but also ameliorated gene expression in SREBP pathway, including SREBP-1a, SREBP-1c, SREBP-2 and Insig-1,without change in Scap expression (Fig. 6b).
0.91 HMGCR, HMGCS, LDLR, FDPS (farnesyl diphosphate synthase), SS, FAS (FA synthase), SCD-1 (stearoyl CoA desaturase-1), ACC (acetyl CoA carboxylase), ACLY (ATP citrate lyase), GPAT (glycerol-3-phosphate acyltransferase), SREBP-1c, SREBP-2, and Insig-1 were all lower in PAQR3-shRNA group than in the control mice.
30054450 0.97 SREBP2 targets hydroxymethylglutaryl (HMG)-CoA synthase (Hmgcs1) and HMG-CoA reductase (Hmgcr) in LPS-primed cells, and the transcript levels were significantly down-regulated in Npc1-/- cells (Fig. S2, D-F).
0.97 Srebp2 and the target genes Hmgcs1 and Hmgcr (Fig. S2, G-I).
23554170 0.97 HMGCR activity and Abeta to impair SREBP2 processing (Grimm et al,; Mohamed et al,).
26226008 0.97 SREBP2 upregulates cholesterol synthesis and uptake by increasing HMGCoA-R, HMGCoA-S1, methylsterol monoxygenase (SC4MOL), LDLR, and SRB1, and decreases cholesterol efflux and catabolism by suppressing ABCA1, ABCG1, ABCG5/G8, and CYP7A1.
29404461 0.97 SREBP-2 proteins and decreased the expression of multiple SREBP target genes, including HMGCR and PCSK9.
27852305 0.96 SREBP-2 and HMGCR, which are key regulatory factors for cholesterol synthesis in the liver, were significantly increased in the NAFLD mice.
0.96 SREBP-2/HMGCR signaling pathways in the liver.
0.95 SREBP-2/HMGCR signaling pathways in the liver.
0.92 SREBP-2 and HMGCR in NAFLD mice.
0.86 SREBP-2 and HMGCR was significantly decreased in the NAFLD + SCP group.
0.51 SREBP-2 and HMGCR) in the liver was suppressed by SCP-100 mg/kg/day.
25849138 0.96 SREBP-2 was sufficient to induce Ldlr, Hmgcr and miR-182 (Fig. 2m,n).
0.95 Srebp-2 and its targets, Hmgcr, Ldlr and miR-182 (Supplementary Fig. 2k).
0.53 SREBP-2 targets, 3-hydroxy-3-methylglutaryl-CoA reductase (Hmgcr), farnesyl diphosphate synthase (Fdps), squalene synthase (Fdft1), Cyp51 and the LDL receptor (Ldlr) were also normalized in LIRKO mice by treatment with FMO3 ASO (Fig. 2j).
19500568 0.96 SREBP-2 bound directly to the Srd5a2 promoter as well as to promoters for known SREBP-2 target gene including HMG CoA reductase.
0.94 SREBP-2 and HMGCR in L/E treated mouse liver.
28386276 0.96 SREBP-2 is an important transcriptional regulator of HMGCR expression, and our previous study found that TSH can increase SREBP-2 expression in vitro; we found that the expression of mature SREBP-2 increased in SCH mice compared to the control mice; however, the expression of precursor SREBP-2 had no significant change (Figure 3(e)).
23139832 0.95 sterol regulatory element-binding protein 2 (SREBP2) and up-regulation of 3-hydroxy-3-methylglutaryl-coenzyme reductase (HMGCR), a SREBP2 target gene and the rate-limiting enzyme for cholesterol biosynthesis, were reported in rodents fed a soy protein diet.
0.91 Hmgcr, Idi1, Fdps, Sqle, Dhcr7 and Pmvk), including Hmgcr - that is the gene encoding the rate limiting enzyme for cholesterol biosynthesis - were up-regulated at 4-wk..Upstream regulator analysis indicated that SREBF2, SREBF1, SIRT2, FOXO1, EGR2, PPARGC1B were predicted "active", whereas PPARA, CEBPE, HMGA1and WT1 were predicted "inhibit" (Table S5).
28874658 0.95 Srebp2, Hmgcr, Sqs and Hmgcs1 transcripts in prostate of wild type (WT) and Pten pc -/- mice.
29122977 0.95 SREBP-2 and SREBP-2 regulates enzymes both upstream and downstream HMGCR, including FPP and GGPP synthases; thus, it is likely that the effect of Abeta on protein prenylation would be more severe than the effects of HMGCR inhibitors.
19691840 0.93 Hmgcr, Insig1 and Sqle while expression of Cyp51a1 and Srebp2 remained unchanged.
0.76 SREBP-2 dependent genes by CAR, analysis of Hmgcr, Sqle and Insig1 promoters was performed to search for potential CAR binding sites.
18771980 0.89 SREBP-2, HMGCR and LDLR, and to study the correlations between the expression of these mediators.
25593129 0.74 Srebp-2 mRNA, the expression of SREBP-2 target genes, that included cytochrome P450 51 (Cyp51), farnesyl diphosphate synthase (Fdps), HMG-CoA reductase (Hmgcr) and squalene synthase (Sqle), were unchanged (Fig. 3A).
21459322 0.57 SREBP-2 targets from the ChIP-seq analysis (Figure S4B) and expression of all three were induced by the sterol depletion similar to Hmgcr analyzed as a control.



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