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1.
Ultrasonics ; 70: 98-106, 2016 08.
Article in English | MEDLINE | ID: mdl-27153374

ABSTRACT

Ultrasonic phantoms are objects that mimic some features of biological tissues, allowing the study of their interactions with ultrasound (US). In the diagnostic-imaging field, breast phantoms are an important tool for testing performance and optimizing US systems, as well as for training medical professionals. This paper describes the design and manufacture of breast lesions by using polyvinyl chloride plastisol (PVCP) as the base material. Among the materials available for this study, PVCP was shown to be stable, durable, and easy to handle. Furthermore, it is a nontoxic, nonpolluting, and low-cost material. The breast's glandular tissue (image background) was simulated by adding graphite powder with a concentration of 1% to the base material. Mixing PVCP and graphite powder in differing concentrations allows one to simulate lesions with different echogenicity patterns (anechoic, hypoechoic, and hyperechoic). From this mixture, phantom materials were obtained with speed of sound varying from 1379.3 to 1397.9ms(-1) and an attenuation coefficient having values between 0.29 and 0.94dBcm(-1) for a frequency of 1MHz at 24°C. A single layer of carnauba wax was added to the lesion surface in order to evaluate its applicability for imaging. The images of the phantoms were acquired using commercial ultrasound equipment; a specialist rated the images, elaborating diagnoses representative of both benign and malignant lesions. The results indicated that it was possible to easily create a phantom by using low-cost materials, readily available in the market and stable at room temperature, as the basis of ultrasonic phantoms that reproduce the image characteristics of fatty breast tissue and typical lesions of the breast.


Subject(s)
Biomimetic Materials/chemistry , Breast Neoplasms/diagnostic imaging , Mammography/instrumentation , Phantoms, Imaging , Plasticizers/chemistry , Polyvinyl Chloride/chemistry , Equipment Design , Equipment Failure Analysis , Humans , Materials Testing , Reproducibility of Results , Sensitivity and Specificity
2.
FEMS Immunol Med Microbiol ; 46(2): 209-20, 2006 Mar.
Article in English | MEDLINE | ID: mdl-16487302

ABSTRACT

Candida albicans expresses a vast number of hydrolytic enzymes, playing roles in several phases of yeast-host interactions. Here, we identified two novel extracellular peptidase classes in C. albicans. Using gelatin-sodium dodecyl sulfate polyacrylamide gel electrophoresis two gelatinolytic activities were detected at physiological pH: a 60-kDa metallopeptidase, completely blocked by 1,10-phenanthroline, and a 50-kDa serine peptidase inhibited by phenylmethylsulfonyl fluoride. In an effort to establish a probable functional implication for these novel peptidase classes, we demonstrated that the 50-kDa secretory serine peptidase was active over a broad pH range (5.0-7.2) and was capable to hydrolyze some soluble human serum proteins and extracellular matrix components. Conversely, when this isolate was grown in yeast carbon base supplemented with bovine serum albumin, a secretory aspartyl peptidase activity was measured, instead of metallo- and serine peptidases, suggesting that distinct medium composition induces different expression of released peptidases in C. albicans. Additionally, we showed by quantitative proteolytic measurement, flow cytometry and immunoblotting assays that the brain heart infusion medium might repress the Sap1-3 production. Collectively, our results showed for the first time the capability of an extracellular proteolytic enzyme other than aspartic-type peptidases to cleave a broad spectrum of relevant host proteinaceous substrates by the human pathogen C. albicans.


Subject(s)
Blood Proteins/metabolism , Candida albicans/enzymology , Candida albicans/growth & development , Serine Endopeptidases/metabolism , Adult , Candida albicans/pathogenicity , Candidiasis/microbiology , Culture Media , Extracellular Matrix/metabolism , Female , Fungal Proteins/metabolism , Humans , Metalloproteases/metabolism , Urinary Tract Infections/microbiology
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