Effect of salinity on microplastic accumulation and osmoregulatory toxicity in the fiddler crab Minuca rapax.

The effects of salinity on the accumulation and toxicity of microplastics (MPs) in mangrove invertebrates are still scarcely described. We assessed the accumulation and osmoregulatory toxicity of the estuarine fiddler crab Minuca rapax, exposed to 25 mg L-1 of high-density polyethylene MPs at three combinations of osmotic media (hypo- 6, iso- 25, or hyper-35 psu), in 1, 3 and 5 days of exposure. Gills accumulated more MPs than the digestive tract (DT) and muscle. MP accumulation in the gills and DT was enhanced at 6 psu and reduced at 21 and 35 psu after 1 day of exposure. Muscle MP accumulation was not affected by salinity or exposure time. Osmotic regulation was unaffected by MP exposure in any exposure time. Our findings demonstrate that M. rapax accumulates MPs in gills and DT depending on the salinity and that MPs are not osmoregulatory toxicant for this species.

Defining the TLT-1 interactome from resting and activated human platelets.

The triggering receptor expressed on myeloid cells (TREM) protein family forms a class of type I transmembrane proteins expressed in immune cells that play important roles in innate and adaptive immune responses. The TREM family member TREM-like transcript 1 (TLT-1, also TREML1) is expressed in megakaryocytes and packaged into platelet granules. TLT-1 binds fibrinogen and plays a role in bleeding initiated by inflammatory insults. Here, we describe a proteomics screen that maps the TLT-1 interactome in resting and activated human platelets. Several identified TLT-1 interactors are involved in cell adhesion and migration, as well as platelet activation. Select interactors, including ß3-integrin, RACK1, GRB2, and Rabs 5A, 7, and 11A, were additionally characterized in co-immunoprecipitation/immunoblotting experiments. Finally, several phosphorylation sites were found on immunoprecipitated TLT-1, including Thr280, a novel, regulated site on a conserved residue near the TLT-1 ITIM regulatory sequence. SIGNIFICANCE: Platelet function relies on the secretion of active molecules from intracellular vesicles, or granules, which contain soluble and membrane-bound proteins that are essential for platelet aggregation, coagulation reactions, and pathogen defense mechanisms. TLT-1 is sequestered in α-granules and transported to the plasma membrane, where it plays a unique role in hemostasis after inflammatory insults. Despite the known importance of TLT-1 in platelet biology, our knowledge of TLT-1 mechanistic signaling is limited. This study defines the TLT-1 interactome in resting and active human platelets, identifying several novel TLT-1 interactors, as well as TLT-1 phosphorylation sites, all with likely signaling implications in platelet aggregation dynamics.