Nutritional Quality of the Mid-Afternoon Snack of Schooled Children between the Ages of 3 and 12 Years in Three Areas in Spain.

Background: The aim of this study was to analyze the nutritional quality of mid-afternoon snacks for schooled children aged 3 to 12 years in three areas of Catalonia (Spain).

Methods: A descriptive observational study collected information on habits and the mid-afternoon snack of 782 schooled children aged 3 to 12 years in three cities, Barcelona, Girona, and Lleida, located in Catalonia (Spain). The children's families voluntarily agreed to complete an online questionnaire that collected information about demographic data and snacking habits in the afternoon, as well as a record of mid-afternoon snack intake over three school days.

An update of the mechanisms of resistance to EGFR-tyrosine kinase inhibitors in breast cancer: Gefitinib (Iressa) -induced changes in the expression and nucleo-cytoplasmic trafficking of HER-ligands (Review).

Intrinsic resistance to the epidermal growth factor receptor (EGFR; HER1) tyrosine kinase inhibitor (TKI) gefitinib, and more generally to EGFR TKIs, is a common phenomenon in breast cancer. The availability of molecular criteria for predicting sensitivity to EGFR-TKIs is, therefore, the most relevant issue for their correct use and for planning future research. Though it appears that in non-small-cell lung cancer (NSCLC) response to gefitinib is directly related to the occurrence of specific mutations in the EGFR TK domain, breast cancer patients cannot be selected for treatment with gefitinib on the same basis as such EGFR mutations have been reported neither in primary breast carcinomas nor in several breast cancer cell lines.

Mechanism of action of potato carboxypeptidase inhibitor (PCI) as an EGF blocker.

The epidermal growth factor receptor (EGFR) signal transduction pathway plays a prominent role in the development of carcinomas, and is an interesting target for antitumoral therapy. We have previously described how potato carboxypeptidase inhibitor (PCI), a 39-amino acid protease inhibitor with a T-Knot motif, binds to EGFR receptor and inhibits the activation of receptor protein tyrosine kinase. In this paper it is shown that PCI interferes with EGFR activation through inhibition of receptor dimerization and receptor transphosphorylation induced by epidermal growth factor (EGF) and by transforming growth factor alpha (TGF-alpha).