Objectives: The aims of the study are to evaluate the feasibility of using pH-sensitive magnetic resonance imaging, chemical exchange saturation transfer (CEST) in pancreatic imaging and to differentiate pancreatic ductal adenocarcinoma (PDAC) with the nontumor pancreas (upstream and downstream) and normal control pancreas.
Methods: Sixteen CEST images with PDAC and 12 CEST images with normal volunteers were acquired and magnetization transfer ratio with asymmetric analysis were measured in areas of PDAC, upstream, downstream, and normal control pancreas. One-way analysis of variance and receiver operating characteristic curve were used to differentiate tumor from nontumor pancreas.
Results: Areas with PDAC showed higher signal intensity than upstream and downstream on CEST images. The mean (standard deviation) values of magnetization transfer ratio with asymmetric analysis were 0.015 (0.034), -0.044 (0.030), -0.019 (0.027), and -0.037 (0.031), respectively, in PDAC area, upstream, downstream, and nontumor area in patient group and -0.008 (0.024) in normal pancreas. Significant differences were found between PDAC and upstream ( P < 0.001), between upstream and normal pancreas ( P = 0.04). Area under curve is 0.857 in differentiating PDAC with nontumor pancreas.
Conclusions: pH-sensitive CEST MRI is feasible in pancreatic imaging and can be used to differentiate PDAC from nontumor pancreas. This provides a novel metabolic imaging method in PDAC.
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http://dx.doi.org/10.1097/MPA.0000000000002059 | DOI Listing |
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State Key Laboratory of Water Environment Simulation, School of Environment, Beijing Normal University, Beijing 100875, China. Electronic address:
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Escherichia coli (E. coli) O157:H7 is a highly pathogenic zoonotic bacterium, with water serving as a key medium for its environmental transmission. However, the survival characteristics of E.
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Division of Endocrinology and Metabolism, Department of Medicine, University of California, San Diego, La Jolla, CA, USA.
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View Article and Find Full Text PDFPrep Biochem Biotechnol
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Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran.
L-asparaginase (asparagine amidohydrolase) contributes to 40% of the total enzyme demands worldwide and is one-third of the global requirement as an anti-cancerous drug in treating acute lymphocytic leukemia (ALL), a type of leukemia. This protein breaks down L-asparagine into aspartic acid and ammonia those involved in ALL, rely on for growth and survival. Both non-recombinant and recombinant L-asparaginase can be produced by bacteria when a suitable substrate and method (solid-state fermentation (SSF) or submerged fermentation (SmF) which are techniques to grow microorganisms under controlled conditions), is provided.
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