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1.
Biosens Bioelectron ; 26(6): 2847-51, 2011 Feb 15.
Article in English | MEDLINE | ID: mdl-21163641

ABSTRACT

Organophosphate pesticides present serious risks to human and environmental health. A rapid reliable, economical and portable analytical system will be of great benefit in the detection and prevention of contamination. A biosensor array based on six acetylcholinesterase enzymes for use in a novel automated instrument incorporating a neural network program is described. Electrochemical analysis was carried out using chronoamperometry and the measurement was taken 10s after applying a potential of 0 V vs. Ag/AgCl. The total analysis time for the complete assay was less than 6 min. The array was used to produce calibration data with six organophosphate pesticides (OPs) in the concentration range of 10(-5) M to 10(-9) M to train a neural network. The output of the neural network was subsequently evaluated using different sample matrices. There were no detrimental matrix effects observed from water, phosphate buffer, food or vegetable extracts. Furthermore, the sensor system was not detrimentally affected by the contents of water samples taken from each stage of the water treatment process. The biosensor system successfully identified and quantified all samples where an OP was present in water, food and vegetable extracts containing different OPs. There were no false positives or false negatives observed during the evaluation of the analytical system. The biosensor arrays and automated instrument were evaluated in situ in field experiments where the instrument was successfully applied to the analysis of a range of environmental samples. It is envisaged that the analytical system could provide a rapid detection system for the early warning of contamination in water and food.


Subject(s)
Biosensing Techniques/instrumentation , Organophosphates/analysis , Pesticides/analysis , Acetylcholinesterase , Automation , Biosensing Techniques/methods , Biosensing Techniques/statistics & numerical data , Electrochemical Techniques , Enzymes, Immobilized , Equipment Design , Food Contamination/analysis , Humans , Neural Networks, Computer , Water Pollutants, Chemical/analysis
2.
Dev Biol ; 283(2): 357-72, 2005 Jul 15.
Article in English | MEDLINE | ID: mdl-15936751

ABSTRACT

The Hedgehog signaling pathway is critical for a significant number of developmental patterning events. In this study, we focus on the defects in pharyngeal arch and cardiovascular patterning present in Sonic hedgehog (Shh) null mouse embryos. Our data indicate that, in the absence of Shh, there is general failure of the pharyngeal arch development leading to cardiac and craniofacial defects. The cardiac phenotype results from arch artery and outflow tract patterning defects, as well as abnormal development of migratory neural crest cells (NCCs). The constellation of cardiovascular defects resembles a severe form of the human birth defect syndrome tetralogy of Fallot with complete pulmonary artery atresia. Previous studies have demonstrated a role for Shh in NCC survival and proliferation at later stages of development. Our data suggest that SHH signaling does not act directly on NCCs as a survival factor, but rather acts to restrict the domains that NCCs can populate during early stages (e8.5-10.5) of cardiovascular and craniofacial development.


Subject(s)
Arteries/embryology , Body Patterning , Neural Crest/embryology , Trans-Activators/genetics , Animals , Branchial Region/embryology , Cell Death , Cell Proliferation , Endoderm/physiology , Female , Heart/embryology , Hedgehog Proteins , Intracellular Signaling Peptides and Proteins , Male , Membrane Proteins/biosynthesis , Mice , Mice, Knockout , Neural Crest/cytology , Neural Crest/metabolism , Patched Receptors , Receptors, Cell Surface , Signal Transduction
3.
Mech Dev ; 94(1-2): 117-32, 2000 Jun.
Article in English | MEDLINE | ID: mdl-10842064

ABSTRACT

We previously demonstrated that a member of the Hedgehog gene family, Indian hedgehog (Ihh), is expressed in the visceral endoderm of EC and ES cell embryoid bodies and mouse embryos. Overexpression studies suggested that Ihh was involved in visceral endoderm differentiation. We now provide evidence for a Hh response in the embryoid body core and in the mesothelial layer of the visceral yolk sac. We also demonstrate that treatment of ES embryoid bodies with the Hh antagonists cAMP and forskolin results in downregulation of the Hh response and altered embryoid body differentiation. The outer endoderm layer undergoes a transition to parietal endoderm while formation of an embryonic ectoderm layer surrounding a cavity is inhibited. These treatments also result in a decrease in the expression of markers for the mesoderm derivatives, blood and endothelial cells. We present a model to explain how Ihh and BMP signaling may regulate extraembryonic endoderm and embryonic ectoderm differentiation.


Subject(s)
Cell Differentiation/physiology , Embryo, Mammalian/cytology , Embryo, Mammalian/physiology , Nerve Tissue Proteins , Proteins/metabolism , Repressor Proteins , Signal Transduction , Trans-Activators , Transforming Growth Factor beta , Xenopus Proteins , Animals , Biomarkers , Bone Morphogenetic Protein 2 , Bone Morphogenetic Protein 4 , Bone Morphogenetic Proteins/genetics , Cell Differentiation/drug effects , Colforsin/pharmacology , Cyclic AMP/pharmacology , DNA-Binding Proteins/genetics , DNA-Binding Proteins/metabolism , Ectoderm/cytology , Ectoderm/physiology , Embryo, Mammalian/drug effects , Embryonic Induction/genetics , Endoderm/cytology , Endoderm/physiology , Endothelium/metabolism , Fetal Blood/drug effects , Fetal Blood/metabolism , Gene Expression Regulation, Developmental , Hedgehog Proteins , Intracellular Signaling Peptides and Proteins , Kruppel-Like Transcription Factors , Membrane Proteins , Mice , Oncogene Proteins/genetics , Oncogene Proteins/metabolism , Patched Receptors , Proteins/genetics , Receptors, Cell Surface , Transcription Factors/genetics , Transcription Factors/metabolism , Zinc Finger Protein GLI1 , Zinc Finger Protein Gli2 , Zinc Finger Protein Gli3
4.
J Pediatr Gastroenterol Nutr ; 7(1): 141-4, 1988.
Article in English | MEDLINE | ID: mdl-3335976

ABSTRACT

A newborn infant developed anaphylactic shock three times, once after ingesting his mother's milk and once after ingesting a formula containing casein hydrolysate. Symptoms resolved after cow's milk was withdrawn from the mother's diet and lactation was resumed. The case demonstrates that anaphylactic shock may occur in breast-fed infants and emphasizes the need to consider allergic phenomena even in these infants.


Subject(s)
Anaphylaxis/etiology , Breast Feeding , Hypersensitivity/immunology , Milk Proteins/immunology , Milk/immunology , Animals , Biopsy , Blood , Feces/analysis , Humans , Hypersensitivity/complications , Hypersensitivity/diet therapy , Hypersensitivity/pathology , Infant, Newborn , Rectum/pathology
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