PubMed · 12862021
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Laura A Alonge. 2003. Could that plastic device harm your patient?. https://doi.org/10.1097/00152193-200307000-00058
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This study aims to investigate the toxicity of di(2-ethylhexyl) phthalate (DEHP) and the potential molecular mechanisms of DEHP-induced bladder cancer (BLCA) using network toxicology and molecular docking strategies. The toxicity of DEHP was assessed using Prox-II software, and potential targets for DEHP-induced BLCA were identified by integrating data from ChEMBL database, Search Tool for Interactions of Chemicals, SwissTargetPrediction, GeneCards, Therapeutic Target Database, Online Mendelian Inheritance in Man, and The Cancer Genome Atlas. STRING database and Cytoscape were employed to construct target networks and determine core targets. The expression levels of core targets were analyzed using R. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes pathway enrichment analyses were performed on potential and core targets. Molecular docking was carried out using CB-Dock 2 to verify the interactions between DEHP and core targets. A total of 105 potential targets related to DEHP-induced BLCA were identified, from which 7 core targets were selected: cyclin-dependent kinase 1, interleukin 6, cyclin-dependent kinase 2, cyclin B1, Erb-B2 receptor tyrosine kinase 2, cyclin B2, and B-cell lymphoma 2. IL-6 and B-cell lymphoma 2 showed downregulated expression in tumor tissues, while cyclin-dependent kinase 1, cyclin-dependent kinase 2, cyclin B1, Erb-B2 receptor tyrosine kinase 2, and cyclin B2 were upregulated. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes enrichment analyses indicated that these targets were enriched in cell signaling and cancer-related pathways. Molecular docking confirmed that DEHP interacts with these core targets. DEHP may promote the development of BLCA by interacting with key proteins and signaling pathways. This study provides a theoretical basis for understanding the molecular mechanisms of DEHP-induced BLCA and offers references for future prevention and treatment strategies.
The present study investigated the levels of phthalate esters in a total of 86 human milk samples collected among 21 breast-feeding mothers over a 6-month postpartum time. Di(2-ethylhexyl) phthalate (DEHP) was the predominant ester with the arithmetic mean value of 222 ng g(-1) (range: 156-398 ng g(-1), 95% confidence limit), followed by dibutyl phthalate (DBP), 0.87 (range: 0.62-1.2) ng g(-1). Diethyl phthalate (DEP), with a mean of 0.31 ng g(-1), was detected in only a small number of samples. Weak correlations between lipid content and levels of phthalate esters were observed. The levels of phthalate esters in human milk fluctuated over the 6-month period; this may indicate a need for multiple sample collection, to calculate average concentrations over the feeding period. Multiple sample collection would provide a better estimate of the exposure of breast-fed infants to phthalate in human milk. For infants relying on breast-feeding, the mean daily intake over the first 6-month period considering a 7 kg infant consuming 750 g of milk was estimated at 167 microg d(-1) for DEHP and less than 1 microg d(-1) for DBP and DEP. While the nutritional and social benefits of breast-feeding are well established, the potential transfer of phthalate esters from mothers to breast-fed infants should also be recognized.
Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The K(m) and V(max) values for mono-2-ethylhexyl phthalate were 26.9 +/- 4.3 microM and 18.1 +/- 0.9 micromol/min . mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% homology with those of meta-cleavage hydrolases which are serine hydrolases but exhibited no significant homology with the sequences of serine esterases. The pentapeptide motif GXSXG, which is conserved in serine hydrolases, was present in the sequence. The enzymatic properties and features of the primary structure suggested that this enzyme is a novel enzyme belonging to an independent group of serine hydrolases.