INT211557

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Context Info
Confidence 0.75
First Reported 2007
Last Reported 2010
Negated 2
Speculated 2
Reported most in Body
Documents 30
Total Number 32
Disease Relevance 5.03
Pain Relevance 0.94

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

cell adhesion (Scarb1) plasma membrane (Scarb1) cytoplasm (Scarb1)
Anatomy Link Frequency
macrophages 4
anti-SR 2
bile 1
peritoneal macrophages 1
Scarb1 (Mus musculus)
Pain Link Frequency Relevance Heat
agonist 26 99.72 Very High Very High Very High
Inflammation 262 96.36 Very High Very High Very High
Bile 6 94.32 High High
lidocaine 52 91.52 High High
cytokine 108 78.32 Quite High
alcohol 14 67.56 Quite High
Inflammatory response 6 26.88 Quite Low
fibrosis 5 21.96 Low Low
anesthesia 6 5.00 Very Low Very Low Very Low
Kinase C 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Mycobacterial Infection 1326 98.92 Very High Very High Very High
Disorder Of Lipid Metabolism 431 98.64 Very High Very High Very High
Vasculitis 1 96.36 Very High Very High Very High
Obesity 21 92.72 High High
Lipodystrophy 2 90.60 High High
Diabetes Mellitus 5 85.12 High High
Aging 3 84.68 Quite High
Contagious Ecthyma 2 79.36 Quite High
Hepatocellular Cancer 9 75.40 Quite High
Hyperlipidemia 6 74.80 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Stable NIH3T3 or R6F cells expressing SRB1 or SIGNR1 were generated by retroviral transduction as described above and grown in the presence of 0.4mg/ml G418 (InvivoGen).


Gene_expression (expressing) of SRB1
1) Confidence 0.75 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
The PCR product was subcloned into either pcDNA3.1 zip-venus1 or pcDNA3.1 venus2 vectors using NheI-ClaI/BstBI as the restriction sites. ?
Gene_expression (/) of ClaI
2) Confidence 0.65 Published 2010 Journal J Mol Signal Section Body Doc Link PMC2954983 Disease Relevance 0 Pain Relevance 0
The two PCR products of PrP cDNA were cleaved with ClaI and ligated into the pGEM-T easy vector system (TA cloning vector, Promega), generating plasmid pGEM-PrP(Xma-Pml); ClaI.
Gene_expression (cleaved) of ClaI
3) Confidence 0.65 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.27 Pain Relevance 0
Therefore experiments were designed to investigate whether the observed binding of BCG-lux to cells expressing SR-B1 was due to direct interaction of the bacteria with the receptor, or because of an increased accumulation of cholesterol in the membrane.
Gene_expression (expressing) of SR-B1
4) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
SR-B1 is a lipoprotein receptor, and we observed a significant decrease in the binding of BCG-lux to R6F cells expressing SR-B1 when binding was performed in the presence of serum (Fig. 2A, left panel).
Gene_expression (expressing) of SR-B1
5) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
On the other hand, the redundancy may stem from down-regulation of this receptor during mycobacterial infection, as macrophage activation has been shown to suppress SR-B1 expression [30].
Gene_expression (expression) of SR-B1 in macrophage associated with mycobacterial infection
6) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.50 Pain Relevance 0.04
While we clearly show that SR-B1 is involved in recognition of mycobacteria on transfected cells we could not define a role for this receptor in primary cells, although SR-B1 was clearly expressed in wild type macrophages (Fig. 3A) as has been shown earlier for the macrophage cell line RAW264.7 [30].
Gene_expression (expressed) of SR-B1 in macrophage
7) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
We therefore generated R6F cells stably expressing SR-B1 or SIGNR1 (as a positive control) and tested their receptor expression by FACS (Fig. 1D).
Gene_expression (expressing) of SR-B1
8) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
This was further supported by the observation that depletion of the membrane's cholesterol by cyclodextrins did not significantly reduce the amount of BCG-lux binding to R6F cells expressing SR-B1 (Fig. 2F), although SR-B1 transfected R6F cells did show more cholesterol accumulation when stained with filipin compared to control cells (data not shown).
Gene_expression (expressing) of SR-B1
9) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.21 Pain Relevance 0
As SR-B1 is involved in cholesterol transport across the membrane [12]–[14] and as mycobacteria have been shown to display high binding capacity for free cholesterol [26], we wondered if the expression of SR-B1 would lead to an accumulation of cholesterol in the membrane and indirectly lead to increased mycobacterial binding.
Gene_expression (expression) of SR-B1
10) Confidence 0.56 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.14 Pain Relevance 0.03
To decipher the molecular basis of Kit-dependent steatosis, we determined the expression profiles of key genes involved in lipid hepatic metabolism: such as apoliproteins (Apoa1, ApoB), lipoprotein receptors (LdlR, VldlR, Scarb1, Lrp1), lipase (Lipc, LipH, Lpl) and others implicated in hepatic lipidogenesis (Scap, Srebf1, Srebf2), lipid secretion (Pltp, Mttp, Abca1), bile acid synthesis (Cyp8b1, Cyp7a1), lipid transport (Slc10a1, Abcb11, Abcb1a, Abcc2) and a lipodystrophy gene, Lipin 1 (Lpin1), encoding a phosphatidate phosphatase enzyme with transcription activity [26-28].
Spec (determined) Gene_expression (expression) of Scarb1 in bile associated with bile and lipodystrophy
11) Confidence 0.52 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC1940254 Disease Relevance 0.16 Pain Relevance 0.05
This is supported by an earlier study on SR-B1 expression of transfected COS-7 cells, where the presence of SR-B1 had no effect on the level of free cholesterol [29].
Gene_expression (expression) of SR-B1
12) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.11 Pain Relevance 0
As shown in Fig. 2E (left panel) SR-B1 expressing R6F cells pre-incubated with anti-SR-B1 showed a significant reduction in binding of BCG-lux, whereas the antibody had no affect on the binding of the mycobacteria to control SIGNR1 cells.
Gene_expression (expressing) of SR-B1 in anti-SR
13) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.05 Pain Relevance 0
Importantly, pre-incubation of the bacteria in serum did not affect subsequent binding to the SR-B1 expressing cells in the absence of serum.
Gene_expression (expressing) of SR-B1
14) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
Using this approach, we found that R6F cells were negative for SR-B1, while both NIH3T3 cells and RAW264.7 macrophages expressed this receptor (Fig. 1C).
Neg (negative) Gene_expression (negative) of SR-B1 in macrophages
15) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
SR-B1 is a lipoprotein receptor, and we observed a significant decrease in the binding of BCG-lux to R6F cells expressing SR-B1 when binding was performed in the presence of serum (Fig. 2A, left panel).
Gene_expression (expressing) of SR-B1
16) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
Initially, different macrophage populations (alveolar macrophages, bone-marrow derived macrophages (BMDmØ), resident as well as thioglycollate-elicited peritoneal macrophages) were isolated from wild type C57BL/6 mice and tested for the expression of SR-B1 by Western Blotting (Fig. 3A).
Gene_expression (expression) of SR-B1 in peritoneal macrophages
17) Confidence 0.49 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.32 Pain Relevance 0
To test BCG binding in cells which do not express any endogenous SR-B1, we screened several cell lines by Western blotting.
Gene_expression (express) of SR-B1
18) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0
This is supported by an earlier study on SR-B1 expression of transfected COS-7 cells, where the presence of SR-B1 had no effect on the level of free cholesterol [29].
Gene_expression (expression) of SR-B1
19) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0.11 Pain Relevance 0
For the detection of ligand binding to SR-B1, 10µg/ml DiI-labelled LDL (Molecular Probes) was added to SR-B1 expressing R6F cells in serum-free DMEM for 2 hr at 37°C.
Gene_expression (expressing) of SR-B1
20) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794535 Disease Relevance 0 Pain Relevance 0.15

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