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1.
J Med Ultrasound ; 30(1): 36-40, 2022.
Article in English | MEDLINE | ID: mdl-35465592

ABSTRACT

Background: The rapid growth of using ultrasound-guided interventional procedures, including biopsy and drainage, which considered painful procedures, leads to improving the practice cycle of ultrasound-guided procedures. Fabrication of low-cost tissue-mimicking phantoms that serve as a training tool medium for kidney needle biopsy procedures has dramatically overcome the drawbacks associated with these practices, such as reducing the number of miss lesions, medical errors, and recurrence rate as well as these phantoms are widely available and considered a good substitute for cadavers which were not always available and relativity expensive. However, several drawbacks are associated with current kidney phantom models, mainly the short shelf life and the high fabrication cost. Methods: This study aims to fabricate a realistic three-dimensional static mature human kidney phantom from low cost and available material for training on ultrasound-guided interventional procedures mainly biopsy test; the material used to fabricate our model is the gelatin-agar mixture. Results: This model proved that it is a tissue-mimicking material by measuring their acoustic properties which nearly the same as real human kidney tissue. Conclusion: The results of practicing interventional procedures on our phantom model showed good and easy uses for interventional procedures training as well as make it a preferable and economically affordable model.

2.
Phytochemistry ; 70(5): 579-89, 2009 Mar.
Article in English | MEDLINE | ID: mdl-19359021

ABSTRACT

Papaver somniferum L. was transformed with an RNAi construct designed to reduce transcript levels of the gene encoding the morphine biosynthetic enzyme, salutaridinol 7-O-acetyltransferase (SalAT). RNA interference of salAT led to accumulation of the intermediate compounds, salutaridine and salutaridinol, in a ratio ranging from 2:1 to 56:1. Along the morphine biosynthetic pathway, salutaridine is stereospecifically reduced by salutaridine reductase (SalR) to salutaridinol, which is subsequently acetylated by SalAT. SalAT transcript was shown by quantitative PCR to be diminished, while salR transcript levels remained unaffected. Yeast two-hybrid and co-immunoprecipitation analyses indicated an interaction between SalR and SalAT, which suggested the occurrence of an enzyme complex and provided an explanation for the unexpected accumulation of salutaridine. Decreased concentrations of thebaine and codeine in latex were also observed, while the morphine levels remained constant compared to concentrations found in untransformed control plants.


Subject(s)
Acetyltransferases/genetics , Morphine/biosynthesis , Papaver/genetics , RNA Interference , Base Sequence , Chromatography, High Pressure Liquid , DNA Primers , Papaver/enzymology , Polymerase Chain Reaction , Spectrometry, Mass, Electrospray Ionization , Two-Hybrid System Techniques
3.
J Biol Chem ; 279(23): 24540-51, 2004 Jun 04.
Article in English | MEDLINE | ID: mdl-15037622

ABSTRACT

The plant glutathione S-transferase BI-GST has been identified as a potent inhibitor of Bax lethality in yeast, a phenotype associated with oxidative stress and disruption of mitochondrial functions. Screening of a tomato two-hybrid library for BI-GST interacting proteins identified five homologous Tau class GSTs, which readily form heterodimers between them and BI-GST. All six LeGSTUs were found to be able to protect yeast cells from prooxidant-induced cell death. The efficiency of each LeGSTU was prooxidant-specific, indicating a different role for each LeGSTU in the oxidative stress-response mechanism. The prooxidant protective effect of all six proteins was suppressed in the absence of YAP1, a transcription factor that regulates hydroperoxide homeostasis in Saccharomyces cerevisiae, suggesting a role for the LeGSTUs in the context of the YAP1-dependent stress-responsive machinery. The different LeGSTUs exhibited varied substrate specificity and showed activity against oxidative stress by-products, indicating that their prooxidant protective function is likely related to the minimization of oxidative damage. Taken together, these results indicate that Tau class GSTs participate in a broad network of catalytic and regulatory functions involved in the oxidative stress response.


Subject(s)
Glutathione Transferase/physiology , Oxidative Stress , Proto-Oncogene Proteins c-bcl-2 , Amino Acid Sequence , Catalysis , Dimerization , Dose-Response Relationship, Drug , Glutathione/chemistry , Glutathione/metabolism , Glutathione Disulfide/chemistry , Glutathione Transferase/metabolism , Hydrogen-Ion Concentration , Kinetics , Solanum lycopersicum/metabolism , Models, Molecular , Molecular Sequence Data , Oxidants/chemistry , Oxidants/metabolism , Phenotype , Precipitin Tests , Protein Binding , Protein Structure, Secondary , Proto-Oncogene Proteins/metabolism , Saccharomyces cerevisiae/metabolism , Sequence Homology, Amino Acid , Substrate Specificity , Two-Hybrid System Techniques , bcl-2-Associated X Protein
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