Dual energy computed tomography of lung nodules: differentiation of iodine and calcium in artificial pulmonary nodules in vitro.

BACKGROUND: Iodine enhancement is a marker for malignancy in pulmonary nodules. The purpose of this in vitro study was to assess whether dual energy computed tomography (DECT) can be used to detect iodine and to distinguish iodine from disperse calcifications in artificial pulmonary nodules. MATERIALS AND METHODS: Small, medium, and large artificial nodules (n=54), with increasing concentrations of iodine or calcium corresponding to an increase in Hounsfield Units (HU) of 15, 30, 45, and 90 at 120 kV, were scanned in a chest phantom with DECT at 80 and 140 kV. Attenuation values of each nodule were measured using semi-automated volumetric analysis. The mean DE ratio with 95% confidence intervals (CI) was calculated for each nodule. RESULTS: The mean maximum diameter of the 18 small nodules was 12 mm (standard deviation: 0.4), 16 mm (0.4) for the 18 medium nodules, and 30 mm (1.1) for the 18 large nodules. There was no overlap of 95% CI of DE ratios of iodine and calcium in nodules≥16 mm. In nodules<16 mm, there was an overlap of DE ratios in low contrast lesions. CONCLUSION: DECT can distinguish iodine from calcium in artificial nodules≥16 mm in vitro. In smaller lesions, a clear differentiation is not possible.

Laminin 5 processing and its integration into the ECM.

Laminins are a family of multi-functional basement membrane proteins. Their C-terminal domain binds to cell surface receptors and is thereby responsible for cell anchorage and the initiation of specific outside-in and inside-out signals. With their N-terminal parts, laminins interact with proteins of the extracellular matrix scaffold to secure the basement membrane to the underlying mesenchymal tissue. Laminins 5A (alpha3Abeta3gamma2), 5B (alpha3Bbeta3gamma2) and 6 (alpha3Abeta1gamma1) are isoforms specific of the basement membrane underneath the epidermis and they undergo a sequential series of extracellular proteolytic changes, which might successively turn on and off one or several of their biological and mechanical functions. Under physiological conditions, such as in adult human skin, epithelial laminins have lost part of the C- and N-terminal domains of the alpha3 and gamma2 chains, respectively. In contrast, in cylindromatosis, a rare inherited disease characterised by major ultrastructural alterations of the basement membrane and altered expression/distribution of integrin receptors, laminin processing has not been completed. Together, these results suggest that laminin processing may regulate signalling pathways and the architecture of the basement membrane by restricting the repertoire of interactions with cell surface receptors and extracellular matrix components.