Novel flame retardants detected in marine plastic litter in coastal areas in Central Chile.

Flame retardants (FRs) are released throughout the plastic life cycle, potentially impacting the environment, biodiversity, and human health. This study analyzed novel flame retardants (NFR) in marine plastic litter (MPL) from six coastal areas in central Chile in November 2017. Target chemicals (n = 19) were analyzed using ultrasonic extraction with hexane, gas chromatography, and mass spectrometry (GC-MS). From all nineteen NFRs analyzed, only ten (53 %) were routinely detected. BTBPE (1,2-bis(2,4,6-tribromophenoxy) ethane) showed the highest concentrations at the Bellavista site (618 to 424,000 pg g-1), and HBB (Hexabromobiphenyl), banned since 1970, was detected in Coliumo (2630 to 13,700 pg g-1). These results show emerging transport patterns and underscore the critical need for enhanced waste management practices for MPL in coastal regions to prevent adverse impacts on marine biodiversity.

TRPM4 Is a Novel Component of the Adhesome Required for Focal Adhesion Disassembly, Migration and Contractility.

Cellular migration and contractility are fundamental processes that are regulated by a variety of concerted mechanisms such as cytoskeleton rearrangements, focal adhesion turnover, and Ca2+ oscillations. TRPM4 is a Ca2+-activated non-selective cationic channel (Ca2+-NSCC) that conducts monovalent but not divalent cations. Here, we used a mass spectrometry-based proteomics approach to identify putative TRPM4-associated proteins. Interestingly, the largest group of these proteins has actin cytoskeleton-related functions, and among these nine are specifically annotated as focal adhesion-related proteins. Consistent with these results, we found that TRPM4 localizes to focal adhesions in cells from different cellular lineages. We show that suppression of TRPM4 in MEFs impacts turnover of focal adhesions, serum-induced Ca2+ influx, focal adhesion kinase (FAK) and Rac activities, and results in reduced cellular spreading, migration and contractile behavior. Finally, we demonstrate that the inhibition of TRPM4 activity alters cellular contractility in vivo, affecting cutaneous wound healing. Together, these findings provide the first evidence, to our knowledge, for a TRP channel specifically localized to focal adhesions, where it performs a central role in modulating cellular migration and contractility.