Expression data from Periostin isoform 3 and 6 overexpressing oral cancer cells
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ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE125874 | GEO | 2019/01/31
REPOSITORIES: GEO
Similar Datasets
Project description:Expression data from Periostin isoform 3 and 6 overexpressing oral cancer cells
| PRJNA517802 | ENA
Project description:The aim to the study was to elucidate the character of Clear cell odontogenic carcinoma cell line in comparison with mucoepidermoid carcinoma cell line by carrying out a geome-wide expression analysis.
2016-07-13 | GSE84300 | GEO
Project description:The aim to the study was to elucidate the character of odontogenic epithelial cells from epithelial cell rests of Malassez in comparison with gingival epithelial cells by carrying out a geome-wide expression analysis.
2015-11-18 | GSE75085 | GEO
Project description:Periostin participates in different processes involved in connective tissue homeostasis. It is also involved in repairment of damaged tissues. We used the osteoblast murine cell line MC3T3-E1 cell line to show how overexpresion of periostin is able to increase their adhesion properties while diminishing their migration capacity. By differential gene expression we evaluated putative targets involved in those cellular properties.
2017-02-09 | GSE66416 | GEO
Project description:We compared transcriptional differences between Periostin siRNA treated and GFP-siRNA treated in OP9 cells using Affymetrix mouse 430_2 array.
2012-01-26 | E-MTAB-519 | biostudies-arrayexpress
Project description:Periostin is a matricellular protein encoded by the POSTN gene that is alternatively spliced to produce ten different isoforms of periostin with a molecular weight ranging from 78 to 91 kDa. Periostin is known to promote fibrillogenesis, organize the extracellular matrix, and bind integrin-receptors to induce cell signaling. Periostin is a key component of the wound healing process but is also known to participate in the pathogenesis of different diseases including atopic dermatitis, asthma, and cancer. In both health and disease, the functions of the different periostin isoforms are largely unknown. The ability to precisely determine the isoform profile of a given human sample is fundamental for characterizing their functional significance. Identification of periostin isoforms is most often carried out at the transcriptional level using RT-PCR based approaches. Though, it must be recognized that periostin exerts it functions at the translational level and is an extracellular protein making it impossible to derive transcriptional information for e.g. plasma periostin that is spatially disconnected from the cell it was expressed by. Consequently, monitoring periostin isoforms at the protein level is highly advantageous. In the publication connected to this dataset we present a fully developed top down mass spectrometry assay for identification and quantification of periostin splice isoforms from any human sample at the protein level.
2024-06-11 | PXD045560 | Pride
Project description:Periostin, a matricellular protein, has been reported to be important in supporting tumor cell dissemination. However, the molecular mechanisms underlying periostin function within the tumor microenvironment are poorly understood. In this study, we observe that loss of periostin decreases esophageal squamous cell carcinoma (ESCC) tumor growth in vivo and demonstrate that periostin cooperates with a conformational missense p53 mutation to enhance invasion. Pathway analyses reveal that invasive esophageal cells expressing periostin and p53R175H mutation display activation of signal transducer and activator of transcription 1 (STAT1) target genes, suggesting that the induction of STAT1 and STAT1-related genes could foster a permissive microenvironment that facilitates invasion of esophageal epithelial cells into the extracellular matrix (ECM). Genetic knockdown of STAT1 in transformed esophageal epithelial cells underscores the importance of STAT1 in promoting invasion and potentiate tumor resistance to genotoxic stress. Furthermore, we find that STAT1 is activated in ESCC xenograft tumors but this activation is attenuated with inducible knockdown of periostin in ESCC tumors. Overall, these results highlight the molecular mechanisms supporting the capacity of periostin in mediating tumor invasion during ESCC development. Pre-clinical study hTERT: EPC cells immortalized by expression of hTERT hTERT_p53: EPC cells expressing hTERT and mutant P53 hTERT_p53_POSTN: EPC cells expressing hTERT, mutant P53, and POSTN.
2016-06-01 | E-GEOD-48999 | biostudies-arrayexpress
Project description:Periostin is a matricellular protein known to be alternatively spliced to produce isoforms with a molecular weight of 78-91 kDa. In the extracellular matrix, periostin attach to cell surfaces and induce signaling via integrin-binding and participates in fibrillogenesis to organize collagen in the extracellular space. In the atopic diseases atopic dermatitis and asthma, periostin is known to participate in driving the disease-causing type 2 inflammation. The periostin isoforms expressed in these diseases and the implication of the alternative splicing events are unknown. Here we present two universal assays to map the expression of periostin isoforms on both the transcriptional (RT-qPCR) and translational (PRM-based mass spectrometry) level. We use these assays to study the splice profile of periostin in atopic dermatitis lesions from patients in active treatment vs. normal skin and in in vitro models of atopic dermatitis and asthma. All isoforms expect isoform 3 show decreased expression at the transcriptional level in AD lesions from patients treated with corticosteroids compared to normal skin. The isoforms display an elevated amount at the translational level indicating a delayed response in periostin level during treatment. Expression of the isoforms were upregulated in the in vitro models of atopic dermatitis and asthma at both the transcriptional and translational level with isoform 3 and 5 displaying the highest level of overexpression. Interestingly, the often overlooked isoform 9 and 10 behaved opposite to the other isoforms as they were equally or even less abundant in the disease models compared to the control, and they were identified in the normal skin samples but not in atopic dermatitis lesions. With the assays and findings presented in the publication connected to this dataset we can take further steps in mapping and understanding the role of periostin isoforms.
2024-07-08 | PXD045287 | Pride
Project description:To explore the effects of periostin on tumor-associated macrophagess, we first sorted CD14+ monocytes from peripheral blood mononuclear cells of healthy donors using magnetic-activated cell sorting and then induced their differentiation into macrophages by culture with M-CSF for 5 days. In the absence of IL-4 stimulation, these macrophages expressed CD163 and Arg1 (a marker of M2 macrophage activation) but not CD206, suggesting that they were similar to macrophages in the early stage of mycosis fungoides (low frequency of CD206+ cells and low IL-4 expression). We then stimulated these macrophages with or without 100 ng/ml of periostin for 6 hours and examined gene expression using a cDNA microarray. Periostin stimulated gene expression on monocyte-derived macrophages was measured at 6 hours after exposure to doses of 100 ng/ml periostin.
2015-07-14 | E-GEOD-70821 | biostudies-arrayexpress
Project description:Idiopathic pulmonary fibrosis (IPF) is a devastating disease with only three to five years of the median survival. Fibroblast proliferation is a hallmark of IPF as well as secretion of extracellular matrix proteins from fibroblasts. However, it is still uncertain how IPF fibroblasts acquire the ability to progressively proliferate. Periostin is a matricellular protein that is highly expressed in the lung tissues of IPF patients and plays a critical role in the pathogenesis of pulmonary fibrosis. However, it remains undetermined whether periostin affects proliferation of lung fibroblasts. In this study, we first comprehensively tried to identify periostin-dependently expressed genes in lung fibroblasts finding that many cell-cycle–related genes are involved in the gene profile. We confirmed that periostin silencing downregulates expression of several cell-cycle–related molecules including the cyclin family, the CDK family, the E2F family, and the transcriptional factors such as B-MYB and FOXM1 in lung fibroblasts. Accordingly, periostin silencing slowed proliferation of lung fibroblasts and affects the distribution of cell cycle particularly at the G1/S checkpoint and drives the cells into G1 arrest. Lung fibroblasts derived from IPF patients also required periostin for maximum proliferation. Moreover, CP4715, a potent inhibitor against integrin V3, a periostin receptor, downregulated proliferation along with expression of cell-cycle–related genes in IPF lung fibroblasts as well as normal lung fibroblasts. These results demonstrate that periostin plays a critical role in proliferation of lung fibroblasts and provide us a beneficial basis to apply the inhibitors against the periostin/integrin V3 interaction to IPF patients.
2020-04-14 | GSE132917 | GEO