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Gene expression induced by LPS, two amyloidogenic peptides, Tau 623-628 and Amylin 28-33, in peritoneal macrophages and B1a cells

ABSTRACT: Amyloidogenic peptides are therapeutic in EAE, reducing systemic levels of IL6, TNF, and INFg. The fibrils are bound and endocytosed in peritoneal MFs and B1a cells. Differential gene expression was used to further understand the process.

ORGANISM(S): Mus musculus

PROVIDER: GSE73026 | GEO | 2015/09/15

SECONDARY ACCESSION(S): PRJNA295984

REPOSITORIES: GEO

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Gene expression induced by LPS, two amyloidogenic peptides, Tau 623-628 and Amylin 28-33, in peritoneal macrophages and B1a cells

Project description:Amyloidogenic peptides are therapeutic in EAE, reducing systemic levels of IL6, TNF, and INFg. The fibrils are bound and endocytosed in peritoneal MFs and B1a cells. Differential gene expression was used to further understand the process. Groups of three female C57BL/6 mice were injected with 10ug of Tau 623-628, Amylin 28-33, LPS, or PBS. 30-40 minutes post injection, the peritoneal cavity was lavaged, CD11b high (MFs) and CD5+CD19+ (B1a lymphocytes) were purified by flow cytometry directly into Trizol. RNA was extracted from the aqueous phase using the Qiagen RNeasy microkits. RNA quality was assessed using the Agilent 2100 bioanalyzer and the RNA 6000 nano reagents kit. One color microarray, Agilent-028005 SurePrint G3 Mouse GE 8x60K Microarray, was performed at the human immune monitoring center. All samples were processed and run at the same time.

2015-09-15 | E-GEOD-73026 | biostudies-arrayexpress

The transcriptional profile analysis of mice peritoneal cavity B1a cells from p40-/-CD25-/- mice

Project description:We have found many differences between B1a cells from p40-/-CD25-/- mice and control mice. To better understand the whole change of transcriptions profile between B1a cells in PC of p40-/-CD25-/- mice and control mice. By using flow cytometry and high-resolution microarrays, we have studied qualitative and quantitative characteristics of B1a cells of p40-/-CD25-/- mice and control mice.

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Expression profiling of mouse B1a cells with high expression of PC1 vs. those with low expression of PC1.

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Effect of hIAPP aggregation on gene expression by mouse bone marrow-derived macrophages after 12 hours

2010-08-11 | GSE23534 | GEO

Bulk RNAseq for B1a B cells of WT and IRF4 T95R mutant mice

Project description:Bulk RNAseq of splenic B1a B cells from wild-type and IRF4 T95R heterozygous mice.

2023-06-01 | E-MTAB-11262 | biostudies-arrayexpress

Expression profiling of mouse B1a cells with high expression of PC1 vs. those with low expression of PC1.

Project description:Mouse peritoneal B1a cells were classified into two groups based upon the expression level of PC1. One is PC1 high group and the other is PC1 low. To evaluate gene expression patterns that distinguished PC1 high expressing B1a cells from PC1 low expressing B1a cells, we used Affymetrix GeneChipM-BM-. Mouse gene 1.0 ST Array. FACS-sorted PC1 high and low cells from individual mouse were used for RNA extraction and Affyarray hybridization. There were six independent biological replications in each group - six cases of PC1 high cells and six cases of PC1 low cells.

2012-07-08 | E-GEOD-39171 | biostudies-arrayexpress

Effect of hIAPP aggregation on gene expression by mouse bone marrow-derived macrophages after 12 hours

Project description:The purpose of this experiment was to determine changes in gene expression by bone marrow-derived macrophages (BMDMs) treated with synthetic human vs. rodent islet amyloid polypeptide (IAPP). Synthetic human IAPP at 15 uM aggregates to form fibrils in vitro, whereas rodent IAPP is non-amyloidogenic. We hypothesized that interaction of macrophages with human IAPP aggregates can activate pro-inflammatory signalling pathways in macrophages, as described for other amyloidogenic peptides. This array includes eight samples from one experiment, with two groups of four replicates each. Each replicate represents BMDMs from one well of a 24-well plate. The control group was treated with 15 uM rat IAPP for 12 hours prior to total RNA extraction; the experimental group was treated with 15 uM human IAPP.

2010-08-11 | E-GEOD-23534 | biostudies-arrayexpress

Modulation of the endocytic, bioenergetic and transcriptomic pathways subserve the neuroprotective, anti-amyloidogenic action of cleavage-specific tau 12A12mAb in Alzheimer’s Disease mouse model

Project description:Beyond deficits in hippocampal-dependent episodic memory, Alzheimer’s Disease (AD) features sensory impairment in visual cognition consistent with extensive neuropathology in the retina. 12A12 is a monoclonal cleavage specific antibody (mAb) which in vivo selectively neutralizes the AD-relevant, harmful N-terminal 20-22kDa tau fragment(s) (i.e NH2htau) without altering the full-length normal protein. When systemically-injected into Tg2576 mouse model overexpressing a mutant form of Amyloid Precursor Protein (APP), APPK670/671L linked to early-onset familial AD, this conformation-specific tau mAb successfully neutralizes the NH2htau accumulating both in their brain and retina and, thus, markedly alleviates the phenotype-associated signs. By means of combined biochemical and metabolic and transcriptomic experimental approach, we report that 12A12mAb downregulates the steady state expression levels of APP and Beta-Secretase 1 (BACE-1) and, thus, limits the Amyloid beta (Aβ) production both in hippocampus and retina from this AD animal model. The endocytic (BIN1, RIN3) and bioenergetic (glycolisis and mitochondria) pathways controlling the cellular fate of APP processing towards the amyloidogenic route subserve the local, antibody-mediated anti-amyloidogenic action in vivo. Our results show for the first time that similar molecular and metabolic retino-cerebral pathways are modulated in coordinated fashion in response to 12A12mAb treatment to tackle the neurosensorial Aβ accumulation in AD neurodegeneration.

2023-06-14 | GSE223593 | GEO

VDJ analysis of IL-10+ and IL-10- splenic B1a, MZ, and FO B cells from sIgM-/- mouse

Project description:We compared the clonotypes of IL-10+ and IL-10- B1a, marginal zone and follicular B cells from the spleen of sIgM-/-IL10GFP mouse using 10X single cell RNAseq to analyze potential differences in clonality between IL-10+ and IL-10- B cells.

2023-11-15 | GSE229063 | GEO

Cross-linked amyloidogenic proteins as potential aggregation inhibitors

Project description:Amyloidogenic proteins, characterized by their ability to form fibrillar aggregates with β sheet structure play an important role in several degenerative diseases, including Parkinson’s disease. Numerous amyloidogenic proteins, such as α synuclein, are intrinsically disordered (or contain ID regions, hence they also present as highly dynamic conformational ensembles in these regions. Aggregation is an inherent property of the polypeptide chains and under non physiological, appropriate conditions most of the proteins can aggregate and form polymers of various structures. Since amyloid fib ril s and oligomers are associated with a great variety of human diseases, inhibition of protein aggregation has great importance and it can be addressed by using small molecules, peptides or proteins. Our research aim was to study the potential application of modified forms of different amyloidogenic proteins as inhibitor molecules by introducing structural constraints in them. Under various conditions, different amyloidogenic proteins’ (α-synuclein and β2-microglobulin) monomer molecules have been cross linked intramolecularly and the heterogeneous mixtures has been fractionated by HPLC. The inhibitory potential of the isolated and effective molecules has been experimentally investigated by various methods ThT assay, TEM, CD spectroscopy). Furthermore, the locations of the crosslinks in the molecules were determined by mass spectrometry, and their structures are modeled in silico. Our results revealed that conformational constrains applied by cross linking on amyloidogenic proteins block their amyloid formation. Moreover, these molecules exhibited inhibitory effect on the aggregation of the unmodified proteins, as well.

2023-10-24 | PXD042501 | Pride

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