RESUMO
On September 20 of 2017, Hurricane Maria made landfall in Puerto Rico as a strong category 4 hurricane with destructive winds and flooding. Everyone suffered in the aftermath of the hurricane due to overwhelming destruction and lack of available resources. For medical students, these conditions were intensified due to their duty as first responders, academic responsibilities from medical school, personal losses, and financial difficulties. Despite the hardships, these students learned lessons and found solutions to overcome their challenges. The objective of this article is to portray the situations that medical students confronted and offer suggestions on how medical students and academic institutions can prepare for future natural disasters.
Assuntos
Faculdades de Medicina , Estudantes de Medicina , Tempestades Ciclônicas , Humanos , Porto Rico , Faculdades de Medicina/organização & administração , Estudantes de Medicina/psicologiaRESUMO
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.