Report

Annual

BuDocks technical digest, construction, maintenance & operation of the Navy's shore establishments

Mode of access: Internet.

Women's retreat at Kate Millett's farm in Poughkeepsie, NY

General note: Title and date provided by Bettye Lane.

Migration and Residence Patterns of Salmonids in Puget Sound, Washington

Thesis (Ph.D.)--University of Washington, 2016-08

Bay Side Scene at Cedar Point

This image shows the peaceful scene of the bay side of Cedar Point around 1885. In the distance can be seen the city of Sandusky, Ohio. A steamer docks nearby/

Dredging the Cedar Point Lagoons

This picture shows the men of the Detroit Dredging Company hand digging lagoons for owner George A. Boeckling at Cedar Point. The lagoon network would be used for transportation so that visitors could reach the boat docks at the Hotel Breakers. They also made it possible to carry coal to the new electric power station. Visitors could also enjoy traveling the lagoons by themselves.

Involvement of cell surface TG2 in the aggregation of K562 cells triggered by gluten

Gluten-induced aggregation of K562 cells represents an in vitro model reproducing the early steps occurring in the small bowel of celiac patients exposed to gliadin. Despite the clear involvement of TG2 in the activation of the antigen-presenting cells, it is not yet clear in which compartment it occurs. Herein we study the calcium-dependent aggregation of these cells, using either cell-permeable or cell-impermeable TG2 inhibitors. Gluten induces efficient aggregation when calcium is absent in the extracellular environment, while TG2 inhibitors do not restore the full aggregating potential of gluten in the presence of calcium. These findings suggest that TG2 activity is not essential in the cellular aggregation mechanism. We demonstrate that gluten contacts the cells and provokes their aggregation through a mechanism involving the A-gliadin peptide 31-43. This peptide also activates the cell surface associated extracellular TG2 in the absence of calcium. Using a bioinformatics approach, we identify the possible docking sites of this peptide on the open and closed TG2 structures. Peptide docks with the closed TG2 structure near to the GTP/GDP site, by establishing molecular interactions with the same amino acids involved in stabilization of GTP binding. We suggest that it may occur through the displacement of GTP, switching the TG2 structure from the closed to the active open conformation. Furthermore, docking analysis shows peptide binding with the β-sandwich domain of the closed TG2 structure, suggesting that this region could be responsible for the different aggregating effects of gluten shown in the presence or absence of calcium. We deduce from these data a possible mechanism of action by which gluten makes contact with the cell surface, which could have possible implications in the celiac disease onset.