The biology of cross-talk between activated growth factor receptors and cell-surface integrins is an area which has attracted much interest in recent years (Schwartz and Ginsberg, 2002). This review discusses the relationship between the insulin-like growth factor (IGF) axis and cell-surface integrin receptors in the regulation of various aspects of cell physiology. Key to these interactions are signals transmitted between integrins and the IGF-I receptor (IGF-IR) when either or both are bound to their cognate ligands and we will review the current state of knowledge in this area. The IGF axis comprises many molecular components and we will also discuss the potential role of these species in cross-talk with the integrin receptor. With respect to integrin ligands, we will mainly focus on the well-characterized interactions of the two extracellular matrix (ECM) glycoproteins fibronectin (FN) and vitronectin (VN) with cell-surface ligands, and, how this affects activity through the IGF axis. However, we will also highlight the importance of other integrin activation mechanisms and their impact on IGF activity.

Beta-adrenocepetor antagonists (beta-blockers) alter the nanostructure of lysozyme amyloids, resulting in different drug release profiles.

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This paper summarizes key information on topics of contemporary interest in human and ecological per‐ and polyfluoroalkyl substance (PFAS) risk assessment, which were discussed at the PFAS Experts Symposium 2. For human health, the discussion focused on the toxicologic and epidemiologic endpoints and exposure assumptions that contribute to differences in PFAS regulatory criteria. For ecological risk, the discussion assessed the current state of the science available to support ecological screening levels and identified key data gaps and uncertainties in our understanding of ecological exposure and toxicity. Finally, the paper summarizes a panel discussion that addressed the challenges and uncertainties of regulating PFAS as a class.

The fibronectin fragment, 9th-10th-type III domains (FIII9-10), mediates cell attachment and spreading and is commonly investigated as a bioadhesive interface for implant materials such as titania (TiO 2 ). How the extent of the cell attachment-spreading response is related to the nature of the adsorbed protein layer is largely unknown. Here, the layer thickness and surface fraction of two FIII9-10 mutants (both protonated and deuterated) adsorbed to TiO 2 were determined over concentrations used in cell adhesion assays. Unexpectedly, the isotopic forms had different adsorption behaviours. At solution concentrations of 10 mg l 21 , the surface fraction of the less conformationally stable mutant (FIII9 0 10) was 42% for the deuterated form and 19% for the protonated form (fitted to the same monolayer thickness). Similarly, the surface fraction of the more stable mutant (FIII9 0 10-H2P) was 34% and 18% for the deuterated and protonated forms, respectively. All proteins showed a transition from monolayer to bilayer between 30 and 100 mg l 21, with the protein longitudinal orientation moving away from the plane of the TiO 2 surface at high concentrations. Baby hamster kidney cells adherent to TiO 2 surfaces coated with the proteins (100 mg l 21) showed a strong spreading response, irrespective of protein conformational stability. After surface washing, FIII9 0 10 and FIII9 0 10-H2P bilayer surface fractions were 30/25% and 42/ 39% for the lower/upper layers, respectively, implying that the cell spreading response requires only a partial protein surface fraction. Thus, we can use neutron reflectivity to inform the coating process for generating bioadhesive TiO 2 surfaces.

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