Journal: Biology of reproduction

Article Title: Stearoyl-CoA desaturase activity in bovine cumulus cells protects the oocyte against saturated fatty acid stress.

doi: 10.1095/biolreprod.116.146159

Figure Lengend Snippet: Figure 2. SCD1 gene and protein expression in cumulus cells and oocytes. (A) The increase of SCD1 mRNA expression in cumulus cells of COCs at 23 h of maturation in comparison to 0 h of maturation, maturation in control medium (green bar), and after exposure to stearic and palmitic acid (100 and 150 μM; purple bar), and stearic, palmitic, and oleic acid (100, 150 and 200 μM; blue bar). Results are presented as mean ± SD; data with different letters differ significantly (P ≤0.01). (B) Representative immunoblot showing expression of SCD1 and actin in oocyte and cumulus cells. SCD1 protein expression in oocytes and cumulus cells is shown at 0 h and after 23 h of maturation in control medium and in the presence of 250 μM stearic acid.

Article Snippet: The membranes were rinsed in TBS-Tween [(TBS with 0.05% Tween-20 (ICN, Aurora OH, USA)] and blocked with 5% nonfat dry milk in TBS-Tween (blocking buffer) for 1 h and probed with primary SCD1 antibody (custom rabbit anti-bovine SCD1, Pacific Immunology, Ramona CA, USA; a kind gift of Dr. Benjamin Corl, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA) or with a polyclonal antibody against ß-actin (sc-1616, Santa Cruz Biotechnology, Dallas, TX, USA) diluted 1:1000 in blocking buffer at 4◦C overnight.

Techniques: Expressing, Comparison, Control, Western Blot

Journal: Biology of reproduction

Article Title: Stearoyl-CoA desaturase activity in bovine cumulus cells protects the oocyte against saturated fatty acid stress.

doi: 10.1095/biolreprod.116.146159

Figure Lengend Snippet: Figure 3. SCD activity in cumulus cells prevents negative impact of saturated free fatty acid on oocyte developmental competence. Percentages of cleavage (A, C, E) and blastocyst formation (B, D, F) of oocytes from COCs matured in control medium (green bars) and in the presence of (A, B) saturated stearic acid (250 μM; orange bar), (C, D) palmitic acid (250 μM; red bar), or (E and F) saturated stearic and palmitic acid (100 and 150 μM; purple bar) and with SCD inhibition (white bars with outline in color of experimental condition). The SCD1 inhibitors were from Biovision (BIO) or Cayman (CAY). Results are presented as mean ± SD; data with different letters differ significantly (P < 0.05).

Article Snippet: The membranes were rinsed in TBS-Tween [(TBS with 0.05% Tween-20 (ICN, Aurora OH, USA)] and blocked with 5% nonfat dry milk in TBS-Tween (blocking buffer) for 1 h and probed with primary SCD1 antibody (custom rabbit anti-bovine SCD1, Pacific Immunology, Ramona CA, USA; a kind gift of Dr. Benjamin Corl, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA) or with a polyclonal antibody against ß-actin (sc-1616, Santa Cruz Biotechnology, Dallas, TX, USA) diluted 1:1000 in blocking buffer at 4◦C overnight.

Techniques: Activity Assay, Control, Inhibition

Journal: Biology of reproduction

Article Title: Stearoyl-CoA desaturase activity in bovine cumulus cells protects the oocyte against saturated fatty acid stress.

doi: 10.1095/biolreprod.116.146159

Figure Lengend Snippet: Figure 4. Apoptosis and necrosis rates in COCs after exposure to stearic acid with and without SCD1 activity. SCD1 activity was inhibited (white bars with outline in the color of experimental condition) in the control group (green bars) and in the presence of saturated stearic acid (250 μM; orange bar). In panel A, the apoptosis levels in cumulus cells from the different conditions are presented; panel B presents the necrosis levels. Results are presented as mean ± SD. Data with different letters differ significantly (P < 0.05). BIO = SCD1 inhibitor from Biovision.

Article Snippet: The membranes were rinsed in TBS-Tween [(TBS with 0.05% Tween-20 (ICN, Aurora OH, USA)] and blocked with 5% nonfat dry milk in TBS-Tween (blocking buffer) for 1 h and probed with primary SCD1 antibody (custom rabbit anti-bovine SCD1, Pacific Immunology, Ramona CA, USA; a kind gift of Dr. Benjamin Corl, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA) or with a polyclonal antibody against ß-actin (sc-1616, Santa Cruz Biotechnology, Dallas, TX, USA) diluted 1:1000 in blocking buffer at 4◦C overnight.

Techniques: Activity Assay, Control

Journal: Biology of reproduction

Article Title: Stearoyl-CoA desaturase activity in bovine cumulus cells protects the oocyte against saturated fatty acid stress.

doi: 10.1095/biolreprod.116.146159

Figure Lengend Snippet: Figure 5. The molar ratio of C18:1/C18:0 based on the levels in matured cumulus cells. SCD1 activity was inhibited (white bars with outline in the color of experimental condition) in the control group (green bars) and in the presence of saturated stearic acid (250 μM; orange bars) during maturation. Panel A presents the C18:1/C18:0 ratio based on the levels of C18:0 presented in panel B and C18:1 in panel C in the lipid of cumulus cells from matured COCs. Results are presented as mean ± SD. Data with different letters differ significantly (P < 0.05). BIO = SCD1 inhibitor from Biovision. CPS = ion counts per second.

Article Snippet: The membranes were rinsed in TBS-Tween [(TBS with 0.05% Tween-20 (ICN, Aurora OH, USA)] and blocked with 5% nonfat dry milk in TBS-Tween (blocking buffer) for 1 h and probed with primary SCD1 antibody (custom rabbit anti-bovine SCD1, Pacific Immunology, Ramona CA, USA; a kind gift of Dr. Benjamin Corl, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA) or with a polyclonal antibody against ß-actin (sc-1616, Santa Cruz Biotechnology, Dallas, TX, USA) diluted 1:1000 in blocking buffer at 4◦C overnight.

Techniques: Activity Assay, Control

Journal: Biology of reproduction

Article Title: Stearoyl-CoA desaturase activity in bovine cumulus cells protects the oocyte against saturated fatty acid stress.

doi: 10.1095/biolreprod.116.146159

Figure Lengend Snippet: Figure 6. Lipid droplet formation in cumulus cells after exposure to stearic and oleic acid without and with SCD1 inhibition. Panel A shows the confocal images of lipid droplets (green) and cumulus cell nuclei (red) for the different maturation groups; control, stearic, and oleic acid without and with a SCD1 inhibitor; (B) Graph representing the number of lipid droplets in cumulus cells after maturation in control medium (green bar), and in the presence of stearic acid (orange bar) or oleic acid (blue bar) during 23 h of maturation without and with inhibition of SCD1 activity (white bars with outline in the color of experimental condition); (C) Graph representing the mean size of lipid droplets, data are normalized on the basis of the control group without SCD1 inhibition. The average diameter of lipid droplets in the control group was 0.99 ± 0.14 μm. Results are presented as mean ± SD. Data with different letters differ significantly (P < 0.05). BIO = SCD1 inhibitor from Biovision. Scale bar represents 20 μm.

Article Snippet: The membranes were rinsed in TBS-Tween [(TBS with 0.05% Tween-20 (ICN, Aurora OH, USA)] and blocked with 5% nonfat dry milk in TBS-Tween (blocking buffer) for 1 h and probed with primary SCD1 antibody (custom rabbit anti-bovine SCD1, Pacific Immunology, Ramona CA, USA; a kind gift of Dr. Benjamin Corl, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA) or with a polyclonal antibody against ß-actin (sc-1616, Santa Cruz Biotechnology, Dallas, TX, USA) diluted 1:1000 in blocking buffer at 4◦C overnight.

Techniques: Inhibition, Control, Activity Assay

Journal: Life Metabolism

Article Title: Regulation of hepatic lipid metabolism by intestine epithelium-derived exosomes

doi: 10.1093/lifemeta/load044

Figure Lengend Snippet: miR-21a-5p and miR-145a-5p regulate liver lipid metabolism through direct suppression of Ccl1 and Btg1 , respectively. (a–e) CCL1-dependent mechanism by which miR-21a-5p regulates liver lipid metabolism. (a) Dual-luciferase assay was performed to validate the direct interaction between miR-21a-5p and 3ʹ-UTR of Ccl1 gene. (b) Raw264.7 cells were transfected with miR-21a-5p mimics or scramble sequences, and the mRNA levels of inflammation marker genes were analyzed by RT-qPCR. (c and d) Representative F4/80 staining of liver section and numbers of F4/80 + cells in HFD-induced obese mice injected with AAV9-miR-21a-5p or AAV-9 scramble. (e) Cellular TG and cholesterol in AML12 cells co-cultured with miR-21a-5p-treated Raw264.7 cells. Results were expressed as mean ± SEM and analyzed by one-way or two-way ANOVA, or Student’s t -test, n = 5 − 7, * denotes P < 0.05. (f–k) MiR-145a-5p regulates liver lipid metabolism through direct suppression of Btg1 . (f) Dual-luciferase assay was performed to validate the direct interaction between miR-145a-5p and 3ʹ-UTR of Btg1 gene. (g) TG concentration of AML12 cells transfected with miR-145a-5p mimics and a plasmid expressing Btg1 -encoding sequences without 3ʹ-UTR. Protein expression of SCD1 in livers of mice treated with AAV9-miR-145a-5p-sponge (h and i) or intExo/miR-145a-5p (j and k). Results were expressed as mean ± SEM and analyzed by one-way ANOVA or Student’s t -test, n = 4 − 8, * denotes P < 0.05.

Article Snippet: SCD1 Rabbit pAb , ABclonal , A16429.

Techniques: Luciferase, Transfection, Marker, Quantitative RT-PCR, Staining, Injection, Cell Culture, Concentration Assay, Plasmid Preparation, Expressing

Journal: Life Metabolism

Article Title: Regulation of hepatic lipid metabolism by intestine epithelium-derived exosomes

doi: 10.1093/lifemeta/load044

Figure Lengend Snippet: qPCR primers.

Article Snippet: SCD1 Rabbit pAb , ABclonal , A16429.

Techniques:

Journal: Life Metabolism

Article Title: Regulation of hepatic lipid metabolism by intestine epithelium-derived exosomes

doi: 10.1093/lifemeta/load044

Figure Lengend Snippet:

Article Snippet: SCD1 Rabbit pAb , ABclonal , A16429.

Techniques:

Journal: bioRxiv

Article Title: A stress-induced Tyrosine tRNA depletion response mediates codon-based translational repression and growth suppression

doi: 10.1101/416727

Figure Lengend Snippet: (A) Cells depleted of tRNA Tyr GUA or YARS were processed for label free quantitation by mass spectrometry to identify proteins that were reduced by a log 2 -fold change of 0.5 or more. This set was overlapped with proteins containing a higher than median abundance of Tyr codon content to identify candidate mediators of the pleiotropic effects of tRNA Tyr GUA depletion. (B) GO functional analysis of the 109 candidate gene-set from (A). (C) Quantitative western blot validation depicting abundances of protein targets (EPCAM, SCD, and USP3) identified from (A). HSC70 was used as a loading control and is not modulated upon molecular perturbation of tRNA Tyr GUA . (D) Quantification of western blot analysis in (C) (n=4). A one-tailed Mann-Whitney test was used to test for statistical significance between knockdown and control conditions. (E) Growth curves for MCF10A cells were transfected with either control siRNA or two independent siRNA targeting EPCAM, SCD, or USP3. Note that the control cell growth curve is the same in all graphs and were plotted separately for clarity and does not represent independent experiments. Two-way ANOVA was used to test for significance. Data represent mean ± s.e.m. *p < 0.05, **p < 0.01, and ***p < 0.001

Article Snippet: Antibodies used were YARS (Abcam, ab150429, RRID: AB_2744675, 1:1000), EPCAM (Proteintech, 21050-1-AP, RRID: AB_10693684, 1:1000), SCD (Proteintech, 23393-1-AP, RRID: AB_2744674, 1:1000) USP3 (Proteintech, 12490-1-AP, RRID: AB_10639042, 1:1000), SSB (MBL, RN074PW, RRID: AB_11124309, 1:1000), hnRNPA1 (Santa Cruz, sc-32301, RRID: AB_627729, 1:1000), hnRNPA0 (Bethyl Laboratories, A303-941A, RRID: AB_2620290, 1:1000), DIS3L2 (Novus biologicals, NBP2-38264), Myc (Cell Signaling, 2276S, RRID: AB_331783), and Luciferase (Proteintech, 27986-1-AP, RRID:AB_2750646).

Techniques: Quantitation Assay, Mass Spectrometry, Functional Assay, Western Blot, One-tailed Test, MANN-WHITNEY, Transfection

Journal: bioRxiv

Article Title: A stress-induced Tyrosine tRNA depletion response mediates codon-based translational repression and growth suppression

doi: 10.1101/416727

Figure Lengend Snippet: (A) Quantitative western blot EPCAM, SCD, and USP3 in MCF10A cells 24 hours after treatment with H 2 O 2 (200μM). HSC70 was used as a loading control. (B) Quantification of western results in (A) (n=9). A one-tailed Mann-Whitney test was used to establish statistical significance between treated and control conditions. (C) A schematic of the codon-based USP3 reporter. A Myc-tagged WT or mutant reporter with 5 Tyr codons mutated to Ala codons were cloned upstream of a Luciferase used for transfection normalization. (D) Quantitative western blot for the Myc-tag and Luciferase (top) with normalized fluorescent intensities (bottom) are shown (n=3). (E) Ribosome occupancy of 20-22nt RPFs in tRNA Tyr GUA -depleted cells compared to control cells reveal greater occupancy at both tyrosine codons in tRNA Tyr GUA -depleted cells. (F) Genes were sorted based on their changes in GC-corrected translation efficiency (TE) values, with reduced TE in tRNA Tyr GUA -depleted cells shown in left and enhanced TE shown on right. The red bars over each column depict the range of values in that bin. We then assessed the distribution of genes with high tyrosine codon content across these three bins using mutual information calculation and testing (see methods for details). For visualization, we used the hypergeometric distribution to assign p-values to the overlap between tyrosine-rich genes and each of the three bins. We then defined an enrichment score as –log of p-value, if there was a significant enrichment. If the overlap is significantly fewer than expected by chance, log of p-value is used instead (depletion). The resulting enrichment score is then shown as a heatmap with gold depicting positive enrichment. Data represent mean ± s.e.m. *p < 0.05, **p < 0.01, and ***p < 0.001

Article Snippet: Antibodies used were YARS (Abcam, ab150429, RRID: AB_2744675, 1:1000), EPCAM (Proteintech, 21050-1-AP, RRID: AB_10693684, 1:1000), SCD (Proteintech, 23393-1-AP, RRID: AB_2744674, 1:1000) USP3 (Proteintech, 12490-1-AP, RRID: AB_10639042, 1:1000), SSB (MBL, RN074PW, RRID: AB_11124309, 1:1000), hnRNPA1 (Santa Cruz, sc-32301, RRID: AB_627729, 1:1000), hnRNPA0 (Bethyl Laboratories, A303-941A, RRID: AB_2620290, 1:1000), DIS3L2 (Novus biologicals, NBP2-38264), Myc (Cell Signaling, 2276S, RRID: AB_331783), and Luciferase (Proteintech, 27986-1-AP, RRID:AB_2750646).

Techniques: Western Blot, One-tailed Test, MANN-WHITNEY, Mutagenesis, Clone Assay, Luciferase, Transfection

Journal: American journal of physiology. Renal physiology

Article Title: Liver X receptor agonist TO-901317 upregulates SCD1 expression in renal proximal straight tubule.

doi: 10.1152/ajprenal.00131.2005

Figure Lengend Snippet: Fig. 4. Autoradiograph of in situ hybridization analysis demonstrating SCD1 mRNA expression in mouse kidneys. Radiolabed mouse SCD1 antisense ribo- probe (352 bp) was used. Black grains indicate hybridization signals of SCD1 mRNA. Much more intensive SCD1 mRNA signals were observed in TO-901317- treated mouse kidneys (right) than that in vehicle-treated mouse kidneys (left). Note: SCD1 mRNA was also highly expressed in perirenal adipose tissues. No specific signals were detected using sense SCD1 riboprobe (data not shown).

Article Snippet: Goat anti-mouse SCD1 antibody, rabbit antihuman SREBP1c antibody, and goat anti-human Tamm-Horsfall protein antibody were purchased from Santa Cruz (Santa Cruz, CA) and Organon-Technika.

Techniques: Autoradiography, In Situ Hybridization, Expressing, Hybridization

Journal: American journal of physiology. Renal physiology

Article Title: Liver X receptor agonist TO-901317 upregulates SCD1 expression in renal proximal straight tubule.

doi: 10.1152/ajprenal.00131.2005

Figure Lengend Snippet: Fig. 5. Immunohistochemical studies showing intrarenal SCD1 protein expression in vehicle (middle)- and TO-901317-treated (right) mice. Mice were administrated with vehicle or LXR agonist TO-901317 (3 mgkg1day1) for 3 days. Note: immunoreactivity of SCD1 protein (brown color) was observed in the outer stripe of the outer medulla in both vehicle- and TO-901317-treated mice (B and C, magnification 50). The higher magnification demonstrates SCD1 immunoreactivity was only localized in a subset of tubular structures (E and F, magnification 400). In the kidneys of mice receiving TO-901317 treatment (C and F), SCD1 immunoreactivity was much higher than that in vehicle-treated control animals (B and E). Note: no positive SCD1 immunostaining was observed in absence of SCD1 antibody in control normal mouse kidney (A and D).

Article Snippet: Goat anti-mouse SCD1 antibody, rabbit antihuman SREBP1c antibody, and goat anti-human Tamm-Horsfall protein antibody were purchased from Santa Cruz (Santa Cruz, CA) and Organon-Technika.

Techniques: Immunohistochemical staining, Expressing, Control, Immunostaining

Journal: American journal of physiology. Renal physiology

Article Title: Liver X receptor agonist TO-901317 upregulates SCD1 expression in renal proximal straight tubule.

doi: 10.1152/ajprenal.00131.2005

Figure Lengend Snippet: Fig. 6. Double-labeling studies demonstrat- ing SCD1 mRNA was expressed in aqua- porin-2 (AQP2)-negative renal tubules in mouse kidneys. Kidney sections from TO- 901317-treated animals were subjected to in situ hybridization of SCD1 mRNA and im- munohistochemical examination of AQP2 protein. Black dots and brown color repre- sent SCD1 mRNA hybridization signals and AQP2 immunoreactivity, respectively. Note that SCD1 mRNA expression (pink arrows) did not overlap with AQP2 immunoreactiv- ity in collecting duct (red arrows). Glom, glomerulus. Magnification 400.

Article Snippet: Goat anti-mouse SCD1 antibody, rabbit antihuman SREBP1c antibody, and goat anti-human Tamm-Horsfall protein antibody were purchased from Santa Cruz (Santa Cruz, CA) and Organon-Technika.

Techniques: Labeling, In Situ Hybridization, Hybridization, Expressing

Journal: American journal of physiology. Renal physiology

Article Title: Liver X receptor agonist TO-901317 upregulates SCD1 expression in renal proximal straight tubule.

doi: 10.1152/ajprenal.00131.2005

Figure Lengend Snippet: Fig. 7. In situ hybridization and immunohis- tochemistry studies showing SCD1 mRNA expression in Tamm-Horsfall (T-H)-negative renal tubules. In situ hybridization analysis of SCD1 mRNA and immunohistochemical study of Tamm-Horsfall protein were per- formed in the kidneys of TO-901317-treated mice as described under MATERIALS AND METHODS. Black grains and brown color rep- resent SCD1 mRNA signals and Tamm- Horsfall immunoreactivity, respectively. Note SCD1 mRNA expression did not over- lap with Tamm-Horsfall immunostaining in medullary thick ascending limb (mTAL). Magnification 400.

Article Snippet: Goat anti-mouse SCD1 antibody, rabbit antihuman SREBP1c antibody, and goat anti-human Tamm-Horsfall protein antibody were purchased from Santa Cruz (Santa Cruz, CA) and Organon-Technika.

Techniques: In Situ Hybridization, Expressing, Immunohistochemical staining, Immunostaining

Journal: American journal of physiology. Renal physiology

Article Title: Liver X receptor agonist TO-901317 upregulates SCD1 expression in renal proximal straight tubule.

doi: 10.1152/ajprenal.00131.2005

Figure Lengend Snippet: Fig. 10. A: schematic illustration of intrarenal lo- calization of SCD1 in the proximal straight tubules (PST, black arrow) of mouse kidney. SCD1 was expressed in the outer stripe (OS) of the outer medulla and was not colocalized with AQP2-posi- tive (magenta arrow) and Tamm-Horsfall-positive (yellow arrow) renal tubules. The cubic shape of cells expressing SCD1 excluded the endothelial cells of vasa recta (red arrow) and epithelial cells of thin limbs of Henle’s loop. IS, inner stripe. B: mechanisms involved in LXR activation-induced SCD1 gene expression in renal proximal tubules. MCD, medullary collecting duct.

Article Snippet: Goat anti-mouse SCD1 antibody, rabbit antihuman SREBP1c antibody, and goat anti-human Tamm-Horsfall protein antibody were purchased from Santa Cruz (Santa Cruz, CA) and Organon-Technika.

Techniques: Expressing, Activation Assay, Gene Expression

Journal: PLoS ONE

Article Title: Fatty Liver Is Associated with Transcriptional Downregulation of Stearoyl-CoA Desaturase and Impaired Protein Dimerization

doi: 10.1371/journal.pone.0076912

Figure Lengend Snippet: Left panel: Each bar represents the mean ± SE values of Sprague Dawley (SD) rats randomly divided into two experimental groups (standard chow diet CD: n=10; high fat diet HFD: n=15). Right panel: Each bar represents the mean ± SE values of SHR (n=13) and WKY (n=14) divided into two experimental groups (CD:SHR, n= 6 and WKY, n=7; HFD: SHR, n=7 and WKY, n=7). The statistical significance of SHR vs. WKY indicates the comparison between strains independent of diet by two-way ANOVA. In each sample, the Scd1 expression was normalized by the expression of Tbp (TATA box binding protein).

Article Snippet: After blocking with 5% nonfat dry milk in TBST buffer [20 mmol/L of Tris–HCl (pH 7.6), 137 mmol/L of NaCl, and 0.25% of Tween-20], the membranes were probed with rabbit polyclonal anti-Scd1 (Abnova, Taipei, Taiwan), followed by incubation with HRP-conjugated anti-rabbit polyclonal immunoglobulin G secondary antibody (GeneTex, Inc., GTX26795, Irvine, CA, USA).

Techniques: Comparison, Expressing, Binding Assay

Journal: PLoS ONE

Article Title: Fatty Liver Is Associated with Transcriptional Downregulation of Stearoyl-CoA Desaturase and Impaired Protein Dimerization

doi: 10.1371/journal.pone.0076912

Figure Lengend Snippet: Upper left panel: Representative analysis of liver Scd1 protein levels in each experimental model (SHR or WKY) with beta-actin as loading control. Upper right panel: Densitometric quantification of liver SCD1 monomer/dimer ratio protein levels. Values are means ± SE for 13 animals in the SHR group and 14 in the WKY group according to diet, as explained in the legends for and . Lower left and right panels: Densitometric quantification of the liver Scd1 monomeric and dimeric band, respectively, in each experimental group according to diet. Liver scd1 protein expression measured by ELISA. Upper right panel: HFD-induced NAFLD: Each bar represents the mean ± SE values of SD rats randomly divided into two experimental groups (CD: n=10; HFD: n=15). Lower right panel: Each bar represents the mean ± SE values of SHR and WKY divided into two experimental groups (CD:SHR, n= 6 and WKY, n=7; HFD: SHR, n=7 and WKY, n=7). Results are expressed pg/µl proteins.

Article Snippet: After blocking with 5% nonfat dry milk in TBST buffer [20 mmol/L of Tris–HCl (pH 7.6), 137 mmol/L of NaCl, and 0.25% of Tween-20], the membranes were probed with rabbit polyclonal anti-Scd1 (Abnova, Taipei, Taiwan), followed by incubation with HRP-conjugated anti-rabbit polyclonal immunoglobulin G secondary antibody (GeneTex, Inc., GTX26795, Irvine, CA, USA).

Techniques: Control, Expressing, Enzyme-linked Immunosorbent Assay

Journal: PLoS ONE

Article Title: Fatty Liver Is Associated with Transcriptional Downregulation of Stearoyl-CoA Desaturase and Impaired Protein Dimerization

doi: 10.1371/journal.pone.0076912

Figure Lengend Snippet: SCD (SCD1): stearoyl-CoA desaturase (delta-9-desaturase); CYB5A: cytochrome b5 type A (microsomal); CYP51A1: cytochrome P450, family 51, subfamily A, polypeptide 1, HMGCS1 3-hydroxy-3-methylglutaryl-CoA synthase 1 (soluble); ELOVL5: ELOVL fatty acid elongase 5; SCD5: stearoyl-CoA desaturase 5; FADS6: fatty acid desaturase domain family, member 6; ELOVL2: ELOVL fatty acid elongase 2; FADS1: fatty acid desaturase 1; ELOVL6: ELOVL fatty acid elongase 6; DHCR7: 7-dehydrocholesterol reductase; SQLE: squalene epoxidase; PPARG: peroxisome proliferator-activated receptor gamma; DEGS2: degenerative spermatocyte homolog 2, lipid desaturase; RXRB: retinoid X receptor, beta; RARA: retinoic acid receptor, alpha; TF: transferring; PPARA: peroxisome proliferator-activated receptor alpha; DEGS1: degenerative spermatocyte homolog 1, lipid desaturase; CYB561: cytochrome b-561; PHF20: PHD finger protein 20.

Article Snippet: After blocking with 5% nonfat dry milk in TBST buffer [20 mmol/L of Tris–HCl (pH 7.6), 137 mmol/L of NaCl, and 0.25% of Tween-20], the membranes were probed with rabbit polyclonal anti-Scd1 (Abnova, Taipei, Taiwan), followed by incubation with HRP-conjugated anti-rabbit polyclonal immunoglobulin G secondary antibody (GeneTex, Inc., GTX26795, Irvine, CA, USA).

Techniques: Transferring

Journal: PLoS ONE

Article Title: Fatty Liver Is Associated with Transcriptional Downregulation of Stearoyl-CoA Desaturase and Impaired Protein Dimerization

doi: 10.1371/journal.pone.0076912

Figure Lengend Snippet: Direct SCD1-related nodes are shown in red. A few nodes are labeled for the sake of simplicity. The gene labels are official names.

Article Snippet: After blocking with 5% nonfat dry milk in TBST buffer [20 mmol/L of Tris–HCl (pH 7.6), 137 mmol/L of NaCl, and 0.25% of Tween-20], the membranes were probed with rabbit polyclonal anti-Scd1 (Abnova, Taipei, Taiwan), followed by incubation with HRP-conjugated anti-rabbit polyclonal immunoglobulin G secondary antibody (GeneTex, Inc., GTX26795, Irvine, CA, USA).

Techniques: Labeling