Journal: bioRxiv

Article Title: Granulin loss and TMEM106B risk converge on lysosomal C-terminal fragment pathology in frontotemporal dementia

doi: 10.64898/2026.03.25.713523

Figure Lengend Snippet: A. Western blots show that recombinant progranulin reduces TMEM106B CTF accumulation in GRN KO iNeurons in a dose-dependent manner. Cells were treated with recombinant progranulin for three days before harvest. B. Quantification of TMEM106B dimers, monomers, and CTFs from panel A. Normalized ratios were calculated by dividing the intensity of each TMEM106B species (dimer, monomer, or CTF) by the loading control (GAPDH), then normalizing to the first bar (0 nM progranulin). C. Western blots show that BSA treatment does not reduce TMEM106B CTF accumulation in GRN KO iNeurons in a dose-dependent manner. Cells were treated with BSA for three days before harvest. D. Quantification of TMEM106B dimers, monomers, and CTFs from panel C. Normalized ratios were calculated by dividing the intensity of each TMEM106B species (dimer, monomer, or CTF) by the loading control (GAPDH), then normalizing to the first bar (0 nM BSA). Bar plots represent the mean, and each dot represents a replicate (n = 3 replicates per condition). Statistical significance was determined by a two-sided Welch’s t-test: ns (not significant), p > 0.05; *, p ≤ 0.05; **, p ≤ 0.01; ***, p ≤ 0.001; ****, p ≤ 0.0001.

Article Snippet: Primary antibodies used in this work with dilution information are as follows: TMEM106B (E7H7Z) antibody (1:500; Cell Signaling Technology, 93334), cleaved TMEM106B (Ser120) antibody (1:500; Cell Signaling Technology, 87145), C-terminal TMEM106B antibody (1:1000, created in the Dr. Leonard Petrucelli laboratory), GAPDH (1:2000; Sigma-Aldrich, G8795), Histone H3 antibody (1:5000; Abcam, ab1791), Beta-tubulin antibody (1:40000, Sigma-Aldrich, 66240-1-Ig), Human LAMP1 antibody (1:1000, Cell Signaling Technology, 9091P or 15665S), Mouse LAMP1 antibody (1:1000, DSHB, 1D4B), progranulin antibody (1:1000, R&D Systems, AF2420), CTS B (1:1000, Cell Signaling Technology, 31718T), PDI antibody (1:1000, Enzo Life Sciences, ADI-SPA-891-D), Citrate synthase antibody (1:1000, Cell Signaling Technology, 14309T), Golgin-97 antibody (1:1000, Cell Signaling Technology, 13192T), HA-Tag (C29F4) antibody (1:1000, Cell Signaling Technology, 3724S), Catalase antibody (1:1000, Cell Signaling Technology, D4P7B), GFP antibody (1:2000, Antibodies Incorporated, 75-131), and V5 antibody (1:1000, Thermo Fisher Scientific, R960-25).

Techniques: Western Blot, Recombinant, Control

Journal: bioRxiv

Article Title: Granulin loss and TMEM106B risk converge on lysosomal C-terminal fragment pathology in frontotemporal dementia

doi: 10.64898/2026.03.25.713523

Figure Lengend Snippet: A. Left panel: Schematic of TMEM106B showing the T185S coding variant (rs3173615) located in the C-terminal domain. Right panel: Isogenic iPSC-derived neurons were generated with three genotypes: CC (homozygous threonine, TT), CG (heterozygous threonine/serine, TS), and GG (homozygous serine, SS). B. Western blots show that the copy number of the protective S185 allele anti-correlates with TMEM106B CTF levels in the lysosome. Purified lysosomes were from GRN WT iNeurons with TT, TS, or SS genotypes. Lysosomes were purified by immunoprecipitation using the LysoTag. C. Quantification of TMEM106B dimers, monomers, and CTFs from panel B. Normalized ratios were calculated by dividing the intensity of each TMEM106B species (dimer, monomer, or CTF) by the loading control (LAMP1), then normalizing to the first bar (TT genotype) of each TMEM106B species. D. Western blots show that GRN KO increases TMEM106B CTF levels in iNeurons with SS or TT genotypes. Whole cell lysates were analyzed. E. Quantification of TMEM106B CTFs from panel D. Normalized ratios were calculated by dividing the intensity of TMEM106B CTF by the loading control (beta-tubulin) and then normalizing to the first bar. F. Western blots show that recombinant progranulin treatment reduces TMEM106B CTF accumulation in iNeurons with SS, TS, or TT genotypes in a dose-dependent manner. Cells were treated with recombinant progranulin for three days before harvest. G. Quantification of TMEM106B dimers and CTFs from panel F. Normalized ratios were calculated by dividing the intensity of each TMEM106B species (dimer or CTF) by the loading control (beta-tubulin), then normalizing to the first bar (0 nM progranulin) of each genotype group. Bar plots represent the mean, and each dot represents a replicate (n = 3 replicates per condition). Statistical significance was determined by two-sided Welch’s t-test: ns (not significant), p > 0.05; *, p ≤ 0.05; **, p ≤ 0.01; ***, p ≤ 0.001; ****, p ≤ 0.0001.

Article Snippet: Primary antibodies used in this work with dilution information are as follows: TMEM106B (E7H7Z) antibody (1:500; Cell Signaling Technology, 93334), cleaved TMEM106B (Ser120) antibody (1:500; Cell Signaling Technology, 87145), C-terminal TMEM106B antibody (1:1000, created in the Dr. Leonard Petrucelli laboratory), GAPDH (1:2000; Sigma-Aldrich, G8795), Histone H3 antibody (1:5000; Abcam, ab1791), Beta-tubulin antibody (1:40000, Sigma-Aldrich, 66240-1-Ig), Human LAMP1 antibody (1:1000, Cell Signaling Technology, 9091P or 15665S), Mouse LAMP1 antibody (1:1000, DSHB, 1D4B), progranulin antibody (1:1000, R&D Systems, AF2420), CTS B (1:1000, Cell Signaling Technology, 31718T), PDI antibody (1:1000, Enzo Life Sciences, ADI-SPA-891-D), Citrate synthase antibody (1:1000, Cell Signaling Technology, 14309T), Golgin-97 antibody (1:1000, Cell Signaling Technology, 13192T), HA-Tag (C29F4) antibody (1:1000, Cell Signaling Technology, 3724S), Catalase antibody (1:1000, Cell Signaling Technology, D4P7B), GFP antibody (1:2000, Antibodies Incorporated, 75-131), and V5 antibody (1:1000, Thermo Fisher Scientific, R960-25).

Techniques: Variant Assay, Derivative Assay, Generated, Western Blot, Purification, Immunoprecipitation, Control, Recombinant

Journal: bioRxiv

Article Title: Granulin loss and TMEM106B risk converge on lysosomal C-terminal fragment pathology in frontotemporal dementia

doi: 10.64898/2026.03.25.713523

Figure Lengend Snippet: A. Box plots showing that the common GRN risk variant (rs5848-T) is significantly associated with reduced progranulin protein levels. The association analysis was performed as using limma, adjusting for sex, postmortem interval, and final consensus cognitive diagnosis. B. Box plots showing that the protective TMEM106B rs3173615 allele is significantly associated with reduced levels of peptides mapping to the TMEM106B C-terminal domain (CTD) in the second ROSMAP cohort (ROSMAP-R2). Association analysis was performed using a linear regression model adjusted for sample batch, sex, race, age of death, postmortem interval, and APOE genotype. C. Box plots showing that the protective TMEM106B rs3173615 allele is significantly associated with increased levels of peptides mapping to the TMEM106B N-terminal domain (NTD) in the second ROSMAP cohort (ROSMAP-R2). The association analysis was performed as in panel B. D. Box plots showing that the common GRN risk variant (rs5848-T) is not significantly associated with increased levels of TMEM106B CTD-mapping peptides in the second ROSMAP cohort (ROSMAP-R2). The association analysis was performed as in panel B. E. Box plots showing that the common GRN variant (rs5848-T) is not significantly associated with levels of TMEM106B NTD-mapping peptides in the second ROSMAP cohort (ROSMAP-R2). The association analysis was performed as in panel B. F. Covariate-adjusted box plots illustrating that the protective TMEM106B rs3173615 allele is associated with a stepwise reduction of CTD-mapping peptides across all GRN genotypes in in the first ROSMAP cohort (ROSMAP-R1), displaying the independent, additive effects of both variants. G. Covariate-adjusted box plots showing N-terminal TMEM106B peptides across GRN genotypes in harmonized ROSMAP data. Details of the statistical analysis can be found in the Methods section. Statistical significance was determined by two-sided Welch’s t-test: ns (not significant), p > 0.05; *, p ≤ 0.05; **, p ≤ 0.01; ***, p ≤ 0.001; ****, p ≤ 0.0001.

Article Snippet: Primary antibodies used in this work with dilution information are as follows: TMEM106B (E7H7Z) antibody (1:500; Cell Signaling Technology, 93334), cleaved TMEM106B (Ser120) antibody (1:500; Cell Signaling Technology, 87145), C-terminal TMEM106B antibody (1:1000, created in the Dr. Leonard Petrucelli laboratory), GAPDH (1:2000; Sigma-Aldrich, G8795), Histone H3 antibody (1:5000; Abcam, ab1791), Beta-tubulin antibody (1:40000, Sigma-Aldrich, 66240-1-Ig), Human LAMP1 antibody (1:1000, Cell Signaling Technology, 9091P or 15665S), Mouse LAMP1 antibody (1:1000, DSHB, 1D4B), progranulin antibody (1:1000, R&D Systems, AF2420), CTS B (1:1000, Cell Signaling Technology, 31718T), PDI antibody (1:1000, Enzo Life Sciences, ADI-SPA-891-D), Citrate synthase antibody (1:1000, Cell Signaling Technology, 14309T), Golgin-97 antibody (1:1000, Cell Signaling Technology, 13192T), HA-Tag (C29F4) antibody (1:1000, Cell Signaling Technology, 3724S), Catalase antibody (1:1000, Cell Signaling Technology, D4P7B), GFP antibody (1:2000, Antibodies Incorporated, 75-131), and V5 antibody (1:1000, Thermo Fisher Scientific, R960-25).

Techniques: Variant Assay, Biomarker Discovery

Journal: bioRxiv

Article Title: Enhanced legumain activity links progranulin deficiency to TDP-43 pathology in frontotemporal lobar degeneration

doi: 10.1101/2024.01.16.575687

Figure Lengend Snippet: a , Representative immunoblots of mouse embryonic fibroblasts (MEF), isolated from wild-type (wt) and granulin knockout ( Grn ko) mice, probed for progranulin (PGRN), legumain (LGMN), and calnexin as loading control. MEF are either non-(-), control-( ctrl ) or Lgmn siRNA- transfected. Quantification of LGMN expression normalized to non-transfected wt levels (n=4). b , In vitro LGMN activity of non-(-), mock, ctrl and Lgmn siRNA-transfected Grn ko MEF normalized to non-transfected wt MEF (n=4). c , Representative immunoblot for LGMN in total brain homogenates of 6-month-old wt and Grn ko mice. Proform (LGMN p ), mature form (LGMN m ), and non-specific band (*) are indicated, β-actin verified equal loading. Quantification of the immunoblot signals normalized to wt (n=3 mice per genotype). d , In vitro LGMN activity of brain homogenates from 3-, 6-, 12-13-, and 20-24-month-old wt and Grn ko mice (n=4-6 per genotype and age group). e , Total brain mRNA of 3-, 6-, 12-13-, and 20-24-month-old mice normalized to wt (n=4-5). f , Representative immunoblot for LGMN in MACS-sorted microglia-, astrocyte- and neuron-enriched brain cell fractions of 4-5-month-old wt and Grn ko mice. LGMN p and LGMN m are indicated, calnexin verified equal loading for each fraction. g , Microglia-, astrocyte- and neuron-enriched fractions from 4-5-month-old Grn ko and wt mice analyzed for LGMN activity either normalized to wt microglia or wt of the respective cell type (insert) (n=3 mice per cell type and genotype). h , Lgmn mRNA levels of microglia isolated from 6-month-old wt and Grn ko mice normalized to wt (n=5). i, LGMN in vitro activity in lysates of cultured primary mouse microglia (n=3 mice per genotype). j , k , LGMN expression ( j ) and activity ( k ) analyzed in brain lysates of frontal cortex from FTLD/ GRN patients and pathology-negative control cases (see Extended Data Table 1). LGMN p and LGMN m are quantified in the immunoblot and normalized to the mean signal of control cases ( j ). Data are mean ± s.d. of biologically independent experiments; unpaired two-tailed t-test: ns not significant; * P <0.05, ** P <0.01, *** P <0.001, **** P <0.0001. P values and statistical source data are provided.

Article Snippet: To investigate the inhibitory effect of PGRN on LGMN activity, 200 ng or the indicated amount of human recombinant PGRN (rPGRN, # 10826-H08H, Sino Biological Inc.) was either added to the activation assay or to the activity assay.

Techniques: Western Blot, Isolation, Knock-Out, Transfection, Expressing, In Vitro, Activity Assay, Cell Culture, Negative Control, Two Tailed Test

Journal: bioRxiv

Article Title: Enhanced legumain activity links progranulin deficiency to TDP-43 pathology in frontotemporal lobar degeneration

doi: 10.1101/2024.01.16.575687

Figure Lengend Snippet: a , Representative immunoblots of MEF wt, Grn ko and Grn ko stably transfected with a mouse Grn cDNA probed for PGRN, LGMN, and β-actin to verify equal loading. b , LGMN substrate turnover and quantification of LGMN activity normalized to MEF wt of biologically independent duplicates is shown as mean ± s.d.. c, Schematic of PTV:PGRN single dosing study in Grn ko/h TfR ki. d , LGMN activity of a Grn wt, Grn ko, and Grn ko treated with a single 10 mg/kg i.v. dose of PTV:PGRN for 7 d and 14 d. Data indicate the mean normalized to wt. (n=6 mice per genotype and treatment, 3-4-month-old). e , Representative immunoblot for LGMN in total brain homogenate of wt and Grn ko non-treated and treated mice. Proform (LGMNp), mature form (LGMNm), unspecific band (asterisk) are indicated, β-actin verified equal loading. Quantification of LGMN immunoblot signals normalized to wt (n=6 mice per genotype and treatment). Statistical significance was determined using one-way ANOVA and Tukey’s post hoc test: ns, not significant; * P <0.05, ** P <0.01, **** P <0.0001. P values and statistical source data are provided.

Article Snippet: To investigate the inhibitory effect of PGRN on LGMN activity, 200 ng or the indicated amount of human recombinant PGRN (rPGRN, # 10826-H08H, Sino Biological Inc.) was either added to the activation assay or to the activity assay.

Techniques: Western Blot, Stable Transfection, Transfection, Activity Assay

Journal: bioRxiv

Article Title: Enhanced legumain activity links progranulin deficiency to TDP-43 pathology in frontotemporal lobar degeneration

doi: 10.1101/2024.01.16.575687

Figure Lengend Snippet: Representative immunoblots for PGRN and LGMN in microglia-, astrocyte-and neuron-enriched brain cell fractions isolated from 10-month-old mice. Enrichment of each cell fraction is verified by immunoblotting for IBA1, GFAP and TUJ. Equal amounts of protein were loaded for all cell types, calnexin expression varies between cell types. n=2 mice per cell type and genotype.

Article Snippet: To investigate the inhibitory effect of PGRN on LGMN activity, 200 ng or the indicated amount of human recombinant PGRN (rPGRN, # 10826-H08H, Sino Biological Inc.) was either added to the activation assay or to the activity assay.

Techniques: Western Blot, Isolation, Expressing

Journal: bioRxiv

Article Title: Enhanced legumain activity links progranulin deficiency to TDP-43 pathology in frontotemporal lobar degeneration

doi: 10.1101/2024.01.16.575687

Figure Lengend Snippet: a , Schematic representation of pH-dependent auto- and not auto-catalytic LGMN maturation. N- and C-terminal pro-peptides (p1-p3) and the mature chain (c) with the active site residues (blue stars) are specified. Proform (LGMN p ), intermediate-form (LGMN i ) and mature-form (LGMN m ) are indicated. b , c , Activity analysis of in vitro auto-catalytically matured recombinant (r) LGMN incubated for 4 h at acidic pH. Either rPGRN or elastase-digested PGRN were added after ( b ) or before the 4 h activation step ( c ) (n=3). d , PGRN digest with elastase controlled by immunoblotting. e , f, Activation of rLGMN with/without rPGRN at acidic pH for indicated time points, monitored by immunoblotting. Quantification of the relative LGMN i level (% of total LGMN) ( e ) or activity ( f ) for each timepoint (n=3). g , LGMN activity after 2 h incubation with different concentrations of rPGRN at pH 4. The IC 50 was calculated using a non-linear curve fit, 95% confidence intervals (CI) are indicated (n=3). h , Immunoblot analysis of rPGRN turnover and granulin peptide generation by rLGMN. Stars indicate rLGMN independent bands. Data are mean ± s.d. of independent technical replicates, unpaired two-tailed t-test: ns, Strikingly, rLGMN activity was reduced by more than 50 % when rPGRN was added to pro-rLGMN during the activation step at acidic pH 4 , while elastase-digested rPGRN did not reduce rLGMN activation , suggesting that rPGRN, but not granulins, regulate the maturation of rLGMN. Autocatalytic maturation of pro-rLGMN was then monitored longitudinally at pH 4.0 with and without rPGRN. Proteolytic in vitro maturation and enzymatic activation of rLGMN under acidic conditions was significantly slowed in the presence of rPGRN . Moreover, rPGRN reduced autocatalytic activation of rLGMN in a dose-dependent manner with an IC50 of 39.28 nM . However, after full autocatalytic maturation , the catalytic activity of rLGMN was identical in the presence and absence of rPGRN . Thus, PGRN does not affect the catalytic activity of LGMN per se , but rather slows its autocatalytic maturation. Intriguingly, as suggested before , rLGMN efficiently generates granulin peptides in vitro . After 8 h of co-incubation of rPGRN with rLGMN, full length rPGRN was completely converted into single or multiple granulin peptides. At this time point also full conversion of rLGMN to the intermediate form was observed , further indicating that full length PGRN is needed to slow LGMN activation and that LGMN regulates its own maturation by processing of PGRN in a negative feedback loop. In vivo , the interaction of LGMN with PGRN is supported by reduced generation of granulins in Lgmn ko mice. Granulin peptides are readily detected within purified liver lysosomes of wt mice, but are substantially reduced in Lgmn ko mice . Thus, LGMN regulates its own maturation by processing of PGRN in a negative feedback loop.

Article Snippet: To investigate the inhibitory effect of PGRN on LGMN activity, 200 ng or the indicated amount of human recombinant PGRN (rPGRN, # 10826-H08H, Sino Biological Inc.) was either added to the activation assay or to the activity assay.

Techniques: Activity Assay, In Vitro, Recombinant, Incubation, Activation Assay, Western Blot, Two Tailed Test, In Vivo, Purification

Journal: bioRxiv

Article Title: Enhanced legumain activity links progranulin deficiency to TDP-43 pathology in frontotemporal lobar degeneration

doi: 10.1101/2024.01.16.575687

Figure Lengend Snippet: a , Schematic representation of the media transfer experiment. HeLa cells were transfected with wt mouse LGMN, the proteolytically inactive LGMN C191A variant (mt) or mock (-) and 25% conditioned media supplemented to primary hippocampal mouse neurons for 24 h. ( b,c) , LGMN expression (LGMN p , LGMN i , and LGMN m ) ( b ) and secretion of LGMN p ( c ) by HeLa cells was verified by immunoblotting (n=3 independent experiments). ( c,d ) To monitor autocatalytic processing of LGMN, conditioned media was incubated at pH 7 or pH 4 for 4 h. d , LGMN activity of conditioned media incubated at pH 7 and pH 4 (n=3 independent experiments). ( e- g) , Primary neurons were analyzed after 24 h incubation with conditioned media. Presence of the LGMN proform was confirmed in culture media ( e ). LGMN uptake by neurons ( e ) and TDP-To provide evidence for a pathological link between PGRN reduction, LGMN activation, and enhanced TDP-43 processing in a human disease-relevant system, we generated human iPSC lacking PGRN ( GRN ko iPSC) and differentiated them into human induced pluripotent stem cell-derived microglia (hiMGL) and neurons (hiNE). GRN ko hiMGL showed a 3-4-fold increased expression and activity of LGMN compared to wt hiMGL but only a 1.5-fold increase of LGMN mRNA levels . Thus, the difference in LGMN mRNA levels between wt and GRN ko hiMGL was less pronounced than on LGMN protein or activity levels, further supporting a post-transcriptional regulation of LGMN activity upon PGRN deficiency. In line with our findings in mice , hiNE had almost no LGMN protein expression or activity and showed lower transcript levels than hiMGL . Furthermore, GRN ko hiNE did not show an increase of LGMN activity in contrast to Grn ko mouse neurons . To investigate a potential cross-talk between microglia and neurons upon PGRN deficiency, we co-cultured GRN wt hiNE with either GRN wt or ko hiMGL . In co-cultures of wt hiNE with GRN ko hiMGL, we observed increased mature and active LGMN in lysates . As a consequence, co-culture of GRN ko hiMGL with GRN wt hiNE showed enhanced TDP-43 processing, indicated by reduced TDP- 43 full length and enhanced TDP-43 fragments . To investigate if TDP-43 processing in the co-culture occurs predominantly within neurons, we selectively blocked neuronal LGMN activity by AAV9 (AAV-hSyn-Cst7) mediated neuronal expression of cystatin F (CSTF) prior to co-culturing with hiMGL . CSTF and CSTC are brain expressed , effective inhibitors of LGMN and other cysteine-proteases . Since CTSF showed stronger inhibitory effects in cell culture, we decided to use AAV-hSyn-Cst7. Immunofluorescence confirmed neuronal CTSF expression , which resulted in reduced LGMN maturation and strongly reduced activity . Furthermore, as a consequence of the inhibition of LGMN activity, TDP-43 processing was also reduced to levels seen in wt co-culture .

Article Snippet: To investigate the inhibitory effect of PGRN on LGMN activity, 200 ng or the indicated amount of human recombinant PGRN (rPGRN, # 10826-H08H, Sino Biological Inc.) was either added to the activation assay or to the activity assay.

Techniques: Transfection, Variant Assay, Expressing, Western Blot, Incubation, Activity Assay, Activation Assay, Generated, Derivative Assay, Cell Culture, Co-Culture Assay, Immunofluorescence, Inhibition

Journal: bioRxiv

Article Title: Enhanced legumain activity links progranulin deficiency to TDP-43 pathology in frontotemporal lobar degeneration

doi: 10.1101/2024.01.16.575687

Figure Lengend Snippet: Suggested pathomechanism: In homeostasis, PGRN slows the maturation of LGMN, which is regulated in a negative feed-back loop via processing of PGRN into single granulins by LGMN. Upon PGRN loss-of-function, lysosomal function is impaired and microglia become hyperactivated. In this context, LGMN is not regulated by PGRN anymore and its protein levels and activity increase. The pro-form of LGMN is secreted by activated microglia and taken up by neurons (mechanism unknown), where it hyperprocesses TDP-43 and thereby drives TDP-43 pathology.

Article Snippet: To investigate the inhibitory effect of PGRN on LGMN activity, 200 ng or the indicated amount of human recombinant PGRN (rPGRN, # 10826-H08H, Sino Biological Inc.) was either added to the activation assay or to the activity assay.

Techniques: Activity Assay

Journal: Endocrinology

Article Title: Impact of Low Dose Oral Exposure to Bisphenol A (BPA) on the Neonatal Rat Hypothalamic and Hippocampal Transcriptome: A CLARITY-BPA Consortium Study

doi: 10.1210/en.2016-1339

Figure Lengend Snippet: Candidate and Novel Genes Assessed With qRT-PCR

Article Snippet: Rn00564605_m1 , Ptgds , R. norvegicus prostaglandin D2 synthase (brain) , {"type":"entrez-nucleotide","attrs":{"text":"NM_013015.2","term_id":"31543522","term_text":"NM_013015.2"}} NM_013015.2 , Both , Plays role in neuroprotection; sexually dimorphic expression in neonates; differential expression observed in RNA-seq , 46 , – 48.

Techniques: Control, Membrane, Expressing, Quantitative Proteomics, Variant Assay, In Vitro

Journal: Endocrinology

Article Title: Impact of Low Dose Oral Exposure to Bisphenol A (BPA) on the Neonatal Rat Hypothalamic and Hippocampal Transcriptome: A CLARITY-BPA Consortium Study

doi: 10.1210/en.2016-1339

Figure Lengend Snippet: qRT-PCR Outcomes and Descriptive Statistics for Genes Found to be Significantly Altered by BPA Exposure

Article Snippet: Rn00564605_m1 , Ptgds , R. norvegicus prostaglandin D2 synthase (brain) , {"type":"entrez-nucleotide","attrs":{"text":"NM_013015.2","term_id":"31543522","term_text":"NM_013015.2"}} NM_013015.2 , Both , Plays role in neuroprotection; sexually dimorphic expression in neonates; differential expression observed in RNA-seq , 46 , – 48.

Techniques: Comparison, Control

Journal: Endocrinology

Article Title: Impact of Low Dose Oral Exposure to Bisphenol A (BPA) on the Neonatal Rat Hypothalamic and Hippocampal Transcriptome: A CLARITY-BPA Consortium Study

doi: 10.1210/en.2016-1339

Figure Lengend Snippet: Effects of gestational BPA and EE exposure on neonatal hippocampal expression of selected genes. In females, exposure to 25-μg BPA/kg bw/d significantly increased Oxt expression (A). In males, exposure to 2500- and 25 000-μg BPA/kg bw/d decreased expression of Oxt (B). BPA and EE had no significant effect on Ptgds (C and D), Slc1a2 (E and F), or Slc32a1 (G and H) expression in either females or males. Graphs depict mean ± SEM; *, P ≤ .05.

Article Snippet: Rn00564605_m1 , Ptgds , R. norvegicus prostaglandin D2 synthase (brain) , {"type":"entrez-nucleotide","attrs":{"text":"NM_013015.2","term_id":"31543522","term_text":"NM_013015.2"}} NM_013015.2 , Both , Plays role in neuroprotection; sexually dimorphic expression in neonates; differential expression observed in RNA-seq , 46 , – 48.

Techniques: Expressing

Journal: Endocrinology

Article Title: Impact of Low Dose Oral Exposure to Bisphenol A (BPA) on the Neonatal Rat Hypothalamic and Hippocampal Transcriptome: A CLARITY-BPA Consortium Study

doi: 10.1210/en.2016-1339

Figure Lengend Snippet: Effects of gestational BPA or EE on neonatal hypothalamic expression of selected genes. Exposure to 2.5- and 250-μg BPA/kg bw/d and 0.05-μg EE/kg bw/d increased female expression of Oxt. A, In males, 25-μg BPA/kg bw/d and the highest dose of EE increased Oxt expression (B). Only the highest dose of EE affected Ptgds, increasing expression in both females and males (C and D). Slc1a2 expression levels were not affected by BPA or EE in either sex (E and F). The low dose of EE and 2.5-, 250-, and 25 000-μg BPA/kg bw/d masculinized (increased) female expression of Slc32a1 (G). The high dose of EE increased male expression of Slc32a1 (H). BPA or EE did not affect Lepr expression in either females (I) or males (J). Graphs depict mean ± SEM; *, P ≤ .05 and **, P ≤ .01.

Article Snippet: Rn00564605_m1 , Ptgds , R. norvegicus prostaglandin D2 synthase (brain) , {"type":"entrez-nucleotide","attrs":{"text":"NM_013015.2","term_id":"31543522","term_text":"NM_013015.2"}} NM_013015.2 , Both , Plays role in neuroprotection; sexually dimorphic expression in neonates; differential expression observed in RNA-seq , 46 , – 48.

Techniques: Expressing