Valorization of Rhopilema hispidum By-Products for Bioactive Peptides with Antibacterial, Enzyme Inhibitory, and Low Cytotoxic Activities
Ontology highlight
ABSTRACT:
ORGANISM(S): Cellular Organisms
SUBMITTER: Benjawan Thumthanaruk
PROVIDER: PXD063639 | JPOST Repository | Tue May 06 00:00:00 BST 2025
REPOSITORIES: jPOST
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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
2013-03-21 | E-GEOD-45357 | biostudies-arrayexpress
Project description:Background: Gastroesophageal reflux disease (GERD) is a chronic condition linked to inflammatory and cancerous alterations in esophageal epithelium. Despite the widespread use of acid suppressing proton pump inhibitors (PPIs), the incidence of esophageal adenocarcinoma (EAC) keeps increasing, underscoring the possible importance of nonacidic reflux components like pepsin in cancer development. Pepsin, a therapeutic target for GERD, has been associated with epithelial damage and metaplasia. Methods: The goal of this study was to investigate the effect of pepsin, at a transcriptional level, and to assess the potential therapeutic value of amprenavir, as a pepsin inhibitor, in vitro. Human esophageal cell lines, immortalized from normal (Het-1A) and Barrett’s esophagus (BAR-T), were exposed to pH 7.0 buffer containing pepsin and/or amprenavir for 1 hour (n=3). RNA-seq was conducted to detect differentially expressed genes (DEGs) with FDR ≤ 0.05 and |log2 fold change| ≥ 0.375, and Ingenuity Pathway Analysis (IPA) was performed to identify the top significantly biological pathways. Results: Pepsin exposure caused notable transcriptomic alterations in both Het-1A and BAR-T cells, specifically impacting mitochondrial function, oxidative phosphorylation, and pathways associated with epithelial integrity, cell signaling, and inflammatory responses. Amprenavir alleviated several of these effects, indicating a protective function in epithelial impairment resulting from peptic injury. Of interest, Het-1A and BAR-T cells demonstrated different reactions to pepsin treatment; BAR-T cells revealed more pronounced changes in pathways associated with wound healing, chronic epithelial formation, and repair, whereas Het-1A cells showed more substantial alterations in systemic damage and mitochondrial pathways. Conclusion: The results of this study underscore the detrimental impact of pepsin on esophageal epithelial cells despite PPI therapy and highlight amprenavir as a promising therapeutic option to mitigate pepsin-induced epithelial injury. Further research to validate these in vitro findings is warranted to assess the efficacy of amprenavir for GERD-related damage and carcinogenesis.
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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:This Agilent QTOF data consists of urine and liver of mice fed AFFF, as well as PFAS chemical standards treated with mouse enzymes for biotransformation. Data acquired by Sheng Liu and David A. Dukes.
It goes alongside the manuscript:
"Expanding PFAS Identification with Transformation Product Libraries: Non-Targeted Analysis Reveals Biotransformation Products in Mice" published in Environmental Science & Technology
An interactive dataset after FluoroMatch annotation for the urine data can be found here:
https://innovativeomics.com/datasets/non-targeted-pfas-dataset-from-urine-of-afff-fed-mice/
Software with the biotransformation libraries can also be found at:
https://innovativeomics.com
Per- and polyfluoroalkyl substances (PFAS) are widely used persistent synthetic chemicals that have been linked to adverse health effects. While the behavior of PFAS has been evaluated in the environment, our understanding of reaction products in mammalian systems is limited. This study identified biological PFAS transformation products and generated mass spectral libraries to facilitate automated search and identification. The biological transformation products of 27 PFAS, spanning 5 chemical subclasses (alcohols, sulfonamides, carboxylic acids, ethers, and esters), were evaluated following enzymatic reaction with mouse liver S9 fractions. Four major pathways were identified by liquid chromatography-high resolution mass spectrometry: glucuronidation; sulfation; dealkylation and oxidation. Class-based fragmentation rules and associated PFAS transformation product libraries were generated and integrated into an automated non-targeted PFAS data analysis software (FluoroMatch). Fragmentation was additionally predicted for the potential transformation products of more than 2,500 PFAS in the EPA CompTox Chemicals Dashboard PFASSTRUCTv4. Generated mass spectral libraries were validated by applying FluoroMatch to a dataset of urine from aqueous film-forming foam (AFFF)-dosed mice. Toxicity predictions showed identified PFAS transformation products as potential developmental and mutagenic toxicants. This research enables more comprehensive PFAS characterization in biological systems which will improve assessment of exposures and evaluation of the associated health impacts.
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