The role of PKC-beta in B cell activation
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ABSTRACT:
PROVIDER: PRJNA437924 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR6825860_1.fastq.gz | Fastqsanger.gz | |||
| SRR6825860_2.fastq.gz | Fastqsanger.gz | |||
| SRR6825861_1.fastq.gz | Fastqsanger.gz | |||
| SRR6825861_2.fastq.gz | Fastqsanger.gz | |||
| SRR6825862_1.fastq.gz | Fastqsanger.gz |
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Project description:Bariatric surgery has demonstrated a significant therapeutic impact in reducing obesity and achieving euglycemia in diabetic patientspatients with diabetes. We previously demonstrated that iIntestinal glucotonic transformation, defined as increased intestinal serum glucose uptake and secretion into the lumen, has anplays a vital important role in bypass surgeryies. Altered transcriptomes were evaluated in variable intestinal glucotonic models and big-data artificial intelligence AI-based drug discovery systems. We found noted that protein kinase C (PKC) activation mimics the intestinal transcriptome changes alterations observed in during intestinal glucotonic transformation. Among PKC subfamilies, atypical PKC promotes GLUT1- mediated intestinal glucotonic transformation without inducing oncogenic proliferation. Intestinal aPKC activation through via the transposon expression vector induces serum glucose uptake into intestinal tissue and excretion into the lumeinal space. . Prostratin, a non-tumorigenic phorbol ester, was found observed to activate aPKC and induce a similar glucotonic effect. Taken together, our study results highlightCollectively, we identified a a new chemical compound and target molecular pathways that may provide a distinct and effective approach to to treating diabetes .
2025-08-13 | GSE240754 | GEO
Project description:Bariatric surgery has demonstrated a significant therapeutic impact in reducing obesity and achieving euglycemia in diabetic patientspatients with diabetes. We previously demonstrated that iIntestinal glucotonic transformation, defined as increased intestinal serum glucose uptake and secretion into the lumen, has anplays a vital important role in bypass surgeryies. Altered transcriptomes were evaluated in variable intestinal glucotonic models and big-data artificial intelligence AI-based drug discovery systems. We found noted that protein kinase C (PKC) activation mimics the intestinal transcriptome changes alterations observed in during intestinal glucotonic transformation. Among PKC subfamilies, atypical PKC promotes GLUT1- mediated intestinal glucotonic transformation without inducing oncogenic proliferation. Intestinal aPKC activation through via the transposon expression vector induces serum glucose uptake into intestinal tissue and excretion into the lumeinal space. . Prostratin, a non-tumorigenic phorbol ester, was found observed to activate aPKC and induce a similar glucotonic effect. Taken together, our study results highlightCollectively, we identified a a new chemical compound and target molecular pathways that may provide a distinct and effective approach to to treating diabetes .
2025-07-23 | GSE239399 | GEO
Project description:Mimicking gastric bypass glucotonic effect: the role of atypical PKC activation and GLUT1
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Project description:Mimicking gastric bypass glucotonic effect: the role of atypical PKC activation and GLUT1
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Project description:A variety of airborne pathogens can induce inflammatory responses in airway epithelial cells, which is a crucial component of host defence. However, excessive inflammatory responses and chronic inflammation also contribute to different diseases in the respiratory system. We hypothesized that the activation of protein kinase C (PKC) is one of the essential mechanisms of inflammatory responses in airway epithelial cells. In the present study, we stimulated human bronchial lung epithelial (BEAS-2B) cells with phorbol ester Phorbol 12, 13-dibutyrate (PDBu), and examined gene expression profile with microarray analysis. Bioinformatics suggested that PKC activation induced dramatic changes in gene expression related to multiple cellular functions. The top two functional networks of genes were centered on NFM-NM-:B and TNF-M-NM-1, which are two commonly known pathways for cell death and inflammation. Subsequent tests confirmed the decrease in cell viability and increase in the production of various cytokines. Interestingly, each of the increased cytokines was differentially regulated at mRNA and/or protein levels by different sub-class of PKC isozymes. We conclude that many pathogen-induced cell death and cytokine production in airway epithelial cells may be mediated through PKC related signaling pathways. These findings suggest that PKCs can be new targets for treatments of lung diseases. Three groups of BEAS-2B cells were prepared: control, 0.5 hour of PDBu stimulation, and 4 hours of PDBu stimulation. Each group consisted of three biological replicates.
2013-05-27 | E-GEOD-44747 | biostudies-arrayexpress
Project description:A variety of airborne pathogens can induce inflammatory responses in airway epithelial cells, which is a crucial component of host defence. However, excessive inflammatory responses and chronic inflammation also contribute to different diseases in the respiratory system. We hypothesized that the activation of protein kinase C (PKC) is one of the essential mechanisms of inflammatory responses in airway epithelial cells. In the present study, we stimulated human bronchial lung epithelial (BEAS-2B) cells with phorbol ester Phorbol 12, 13-dibutyrate (PDBu), and examined gene expression profile with microarray analysis. Bioinformatics suggested that PKC activation induced dramatic changes in gene expression related to multiple cellular functions. The top two functional networks of genes were centered on NFκB and TNF-α, which are two commonly known pathways for cell death and inflammation. Subsequent tests confirmed the decrease in cell viability and increase in the production of various cytokines. Interestingly, each of the increased cytokines was differentially regulated at mRNA and/or protein levels by different sub-class of PKC isozymes. We conclude that many pathogen-induced cell death and cytokine production in airway epithelial cells may be mediated through PKC related signaling pathways. These findings suggest that PKCs can be new targets for treatments of lung diseases.
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Project description:Pharmacological inhibition of protein kinase C beta (PKC-beta) # by the compound LY317615 has been tested on primary cultured mouse brain microvascular endothelial cells, stimulated in-vitro for 8h at a concentration of 5 µM. The aim of the study was the question if inhibition of PKC-beta leads to inhibition of genes responsible for T-cell migration in order to investigate LY-317615 as a possible experimental therapy for multiple sclerosis.
2013-07-08 | GSE48572 | GEO
Project description:Targeting protein kinase C (PKC) isoforms by the small molecule inhibitor enzastaurin has shown promising pre-clinical activity in a wide range of tumor cells. In this study, we further delineated its mechanism of action in multiple myeloma (MM) cells and found a novel role of b-catenin in regulating growth and survival of tumor cells. Specifically, inhibition of PKC leads to rapid accumulation of b-catenin by preventing the phosphorylation required for its proteasomal degradation. Microarray analysis and siRNA-mediated gene silencing in MM cells revealed that accumulated b-catenin activates early ER stress signaling via eIF2a, CHOP and p21, leading to immediate growth inhibition. Furthermore, accumulated b-catenin contributes to enzastaurin-induced cell death. Both sequential knock-down of b-catenin, c-Jun, and p73, as well as overexpression of b-catenin or p73 confirmed that accumulated b-catenin triggers c-Jun-dependent induction of p73, thereby conferring MM cell apoptosis. In summary, our data reveal a novel role of b-catenin in ER stress-mediated growth inhibition, and a new pro-apoptotic mechanism triggered by b-catenin upon inhibition of PKC isoforms. Moreover, we identify p73 as a potential novel therapeutic target in MM. Based on these and previous data, enzastaurin is currently under clinical investigation in a variety of hematologic malignancies including MM. Keywords: time course
2008-11-11 | GSE13514 | GEO
Project description:Pharmacological inhibition of protein kinase C beta (PKC-beta) # by the compound LY317615 has been tested on primary cultured mouse brain microvascular endothelial cells, stimulated in-vitro for 8h at a concentration of 5 µM. The aim of the study was the question if inhibition of PKC-beta leads to inhibition of genes responsible for T-cell migration in order to investigate LY-317615 as a possible experimental therapy for multiple sclerosis. primary cultured mouse brain microvascular endothelial cells (MBMEC) have been prepared from new-born mice and cultured for one week. Then stimulated for 8h with 5 µM LY317615. Two samples had been treated for the last 24h with 500 µM TNF-alpha and 500 µM IFN-gamma (inflamed) whereas two samples had been left untreated (naive). RNA was prepared using TRIZOL according to standard protocols.
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Project description:PKCb-null (Prkcb-/-) mice are severely immunodeficient. Here we show that mice whose B cells lack PKCb fail to develop germinal centers and plasma cells, which in concert undermine affinity maturation and antibody production in response to immunization. Moreover, Prkcb-/- B cells fail to differentiate into plasma cells in response to viral infection. At a cellular level, we show that activated Prkcb-/- B cells exhibit defective antigen polarization and mTORC1 signaling. While the loss of antigen polarization impairs antigen presentation and restricts the potential of Prkcb-/- B cells to develop into GC B cells, altered mTORC1 signaling affects gene expression, metabolic reprogramming and mitochondrial remodeling which together overwhelmingly oppose commitment to plasma cell differentiation. Mechanistically, we show that PKCb-mediated metabolic reprogramming is required for sustained heme biosynthesis that is essential for effector fate decision in B cells. Taken together, our study reveals mechanistic insights into the function of PKCb as a key regulator of B-cell polarity and metabolic reprogramming that instructs B-cell fate.
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