Purpose: A retrospective clinical-histological study to determine the diagnostic accuracy of mammography using conventional screen-film cassettes (hard copy), high-resolution digital phosphor storage plates (hard copy) and monitor display (soft copy) for microcalcifications and focal lesions (BI-RADS (TM) category 4 or 5).
Materials And Methods: From April to November 2001, 76 patients underwent conventional film-screen mammography and, after diagnosis and preoperative wire localization, digital mammography with the same exposure parameters. Five investigators retrospectively determined the diagnosis after the operation from randomly distributed mediolateral views (hard-copy reading) and from the monitor display (soft-copy reading).
Purpose: To determine the optimum number of specimens of a sonographically guided core biopsy of the breast.
Materials And Methods: From January 2001 to April 2001, sonographically guided core biopsies (coaxial needle: 11 G; core needle: 12 G) were performed on 106 patients with 115 BI-RADS trade mark 4-5 lesions that had corresponding sonographic findings. Five specimens were obtained in anteroposterior direction parallel to the chest wall and each specimen examined histologically.
Purpose: Determination of image quality between conventional film screen system, digital phosphor storage plate mammography (high resolution) and digital mammography.
Materials And Methods: Mammograms of the Wisconsin Mammographic Random Phantom, Model 152 A (Radiation Measurements Inc., Wisconsin) were acquired using a conventional film-screen system, a digital storage phosphor plate system and a digital system.
Recently, a family of G-protein-coupled receptors named endothelial differentiation gene (Edg) receptor family has been identified, which are specifically activated by the two serum lipids, sphingosine-1-phosphate and lysophosphatidic acid. Sphingosine-1-phosphate can also act intracellularly to release Ca2+ from intracellular stores. Since in several cell types, G-protein-coupled lysophosphatidic acid or sphingosine-1-phosphate receptors mobilize Ca2+ in the absence of a measurable phospholipase C stimulation, it was analysed here whether intracellular sphingosine-1-phosphate production was the signalling mechanism used by extracellular sphingosine-1-phosphate for mobilization of stored Ca2+.
View Article and Find Full Text PDFContribution of sphingosine kinase (SPK)-catalyzed production of sphingosine-1-phosphate (SPP), in comparison to phospholipase C (PLC), to Ca(2+) signalling by epidermal growth factor (EGF) was studied in two HEK-293 cell clones (HEK2 and HEK3), expressing functional EGF receptors and exhibiting release of stored Ca(2+) by intracellular SPP. In HEK3 cells, EGF increased [Ca(2+)](i) and stimulated both, SPK and PLC. [Ca(2+)](i) increase, but not PLC stimulation, was strongly reduced by SPK inhibition.
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