Trypsin
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA844483 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR19514351_1.fastq.gz | Fastqsanger.gz | |||
| SRR19514351_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 2 of 2 |
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Project description:We have comprehensively profiled the time-series changes in gene expression dependent on enzymatic treatment using trypsin, and attempted to elucidate the global changes suppressed by treatment with cold active protease in a low-temperature environment.
2022-06-20 | GSE168452 | GEO
Project description:The level of trypsin-2 has been shown to correlate with the malignancy and metastatic potential of many cancer. We used microarrays to detail how tryspin-2 overexpression changes the gene profile of human tongue squamous cell carcinoma cell line (HSC-3). We compared trypsin-2 overexpressing HSC-3 line to HSC-3 which was transfected with control vector and because of that did not expressed trypsin-2 at all.
2012-10-02 | E-GEOD-32056 | biostudies-arrayexpress
Project description:The level of trypsin-2 has been shown to correlate with the malignancy and metastatic potential of many cancer. We used microarrays to detail how tryspin-2 overexpression changes the gene profile of human tongue squamous cell carcinoma cell line (HSC-3).
2012-10-02 | GSE32056 | GEO
Project description:Human embryonic kidney cell (HEK293) were treated with PAR2 peptide agonist 2f-LIGRLO-NH2 (1.5h, 3h, 6h and 12h) or trypsin (6h). Comparison of genes similarly regulated by both treatments allowed better characterization of PAR2 induced response as both agonists had been reported as non-specific for PAR2.
2010-11-19 | GSE24332 | GEO
Project description:Gliadin triggers T-cell mediated immunity in celiac disease, and has cytotoxic effects on enterocytes mediated through obscure mechanisms. In addition, gliadin transport mechanisms, potential cell surface receptors and gliadin-activated downstream signaling pathways are not completely understood. In order to screen for novel downstream gliadin target genes we performed a systematic whole genome expression study on intestinal epithelial cells. Undifferentiated Caco-2 cells were exposed to pepsin- and trypsin- digested gliadin (PT-G), a blank pepsin-trypsin control (PT) and to a synthetic peptide corresponding to gliadin p31-43 peptide for six hours. RNA from four different experiments was used for hybridization on Agilent one color human whole genome DNA microarray chips. The microarray data were analyzed using the Bioconductor package LIMMA. Genes with nominal p < 0.01 were considered statistically significant. Compared to the untreated cells 1705, 1755 and 211 probes were affected by PT-G, PT and p31-43 respectively. 46 probes were significantly different between PT and PT-G treated cells. Among the p31-43 peptide affected probes, 10 and 21 probes were affected by PT-G and PT respectively. Only PT-G affected genes could be validated by quantitative real-time polymerase chain reaction. All the genes were, nonetheless, also affected to a comparable level by PT treated negative controls. In conclusion, we could not replicate previously reported direct effects of gliadin peptides on enterocytes. The PT-G affected genes in the microarray analysis were validated by qRT-PCR, however these genes were also affected by PT treated negative controls suggesting that certain epitopes derived from pepsin and trypsin may also affect epithelial cell gene transcription. Our study demonstrates novel non-enzymatic effects of pepsin and trypsin on cells and calls for proper controls in pepsin and trypsin digested gliadin experiments. It is conceivable that gliadin effects on enterocytes are secondary mediated through oxidative stress, NFkB activation and IL-15 up-regulation.
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Project description:Enzymatic treatment using trypsin and cold-active protease for C2C12 myoblasts
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Project description:Being a sessile organism, plants are constantly confronted by various biotic (pest and pathogen) and abiotic (drought, salinity, flood, extreme temperatures, etc.) stresses. In response to these environmental stresses, plants have developed numerous defense mechanisms. One of the basal defense responses in plants are mediated by trypsin inhibitors (TIs). Putranjiva roxburghii trypsin inhibitor (PRTI), a potent trypsin inhibitor from P. roxburghii showing sequence similarity with a group of genes known to have defense and storage function such as wound inducible (WIN) proteins, vegetative storage proteins (VSPs), and Bark storage protein (BSPs) was overexpressed in Citrus aurantifolia. PRTI overexpressing lines were tolerant to various abiotic stresses (salinity, drought, and alkalinity) and two pests namely, Scirtothrips citri and Papilio demoleus. The molecular insights underlying the heterologous overexpression of PRTI at the transcriptomic level reveals the upregulation of stress responsive genes and involvement of hormonal signal transduction and transporters. Further, genes related to DNA repair, amino acid synthesis, and development were also found to be upregulated. Our study also reveals the nuclear-cytoplasmic localization and alteration phytohormone profile by PRTI overexpression in transgenic lines as compared to wild-type which clearly indicates the role of abscisic acid ABA in stress tolerance.
2022-12-31 | GSE208104 | GEO
Project description:Human embryonic kidney cell (HEK293) were treated with PAR2 peptide agonist 2f-LIGRLO-NH2 (1.5h, 3h, 6h and 12h) or trypsin (6h). Comparison of genes similarly regulated by both treatments allowed better characterization of PAR2 induced response as both agonists had been reported as non-specific for PAR2. Six conditioned experiments with 3 replicates each. Individual grown and harvested.
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Project description:Precision de novo peptide sequencing using mirror proteases of Ac-LysargiNase and trypsin for large-scale proteomicsPrecision de novo peptide sequencing using mirror proteases of Ac-LysargiNase and trypsin for large-scale proteomics
2019-01-11 | PXD008688 | Pride
Project description:Gliadin triggers T-cell mediated immunity in celiac disease, and has cytotoxic effects on enterocytes mediated through obscure mechanisms. In addition, gliadin transport mechanisms, potential cell surface receptors and gliadin-activated downstream signaling pathways are not completely understood. In order to screen for novel downstream gliadin target genes we performed a systematic whole genome expression study on intestinal epithelial cells. Undifferentiated Caco-2 cells were exposed to pepsin- and trypsin- digested gliadin (PT-G), a blank pepsin-trypsin control (PT) and to a synthetic peptide corresponding to gliadin p31-43 peptide for six hours. RNA from four different experiments was used for hybridization on Agilent one color human whole genome DNA microarray chips. The microarray data were analyzed using the Bioconductor package LIMMA. Genes with nominal p < 0.01 were considered statistically significant. Compared to the untreated cells 1705, 1755 and 211 probes were affected by PT-G, PT and p31-43 respectively. 46 probes were significantly different between PT and PT-G treated cells. Among the p31-43 peptide affected probes, 10 and 21 probes were affected by PT-G and PT respectively. Only PT-G affected genes could be validated by quantitative real-time polymerase chain reaction. All the genes were, nonetheless, also affected to a comparable level by PT treated negative controls. In conclusion, we could not replicate previously reported direct effects of gliadin peptides on enterocytes. The PT-G affected genes in the microarray analysis were validated by qRT-PCR, however these genes were also affected by PT treated negative controls suggesting that certain epitopes derived from pepsin and trypsin may also affect epithelial cell gene transcription. Our study demonstrates novel non-enzymatic effects of pepsin and trypsin on cells and calls for proper controls in pepsin and trypsin digested gliadin experiments. It is conceivable that gliadin effects on enterocytes are secondary mediated through oxidative stress, NFkB activation and IL-15 up-regulation. In total, 16 samples were analyzed of which 4 were control (MED) samples, 4 samples of p31-43 treatment, 4 samples of PT treatmetn and 4 samples of PT-G treatment
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