No abstract

The signaling pathways that lead to the localization of cellular protein to the area of interaction between T cell and antigenpresenting cell and the mechanism by which these molecules are further sorted to the peripheral supramolecular activation cluster or central supramolecular activation cluster regions of the immunologic synapse are poorly understood. In this study, we investigated the functional involvement of CD28 costimulation in the T cell receptor (TCR)-mediated immunologic synapse formation with respect to protein kinase C (PKC) localization. We showed that CD3 crosslinking alone was sufficient to induce PKC capping in naïve CD4 ؉ T cells. Studies with pharmacologic inhibitors and knockout mice showed that the TCR-derived signaling that drives PKC membrane translocation requires the Src family kinase, Lck, but not Fyn. In addition, a time course study of the persistence of T cell molecules to the immunologic synapse indicated that PKC, unlike TCR, persisted in the synapse for at least 4 h, a time that is sufficient for commitment of a T cell to cell division. Finally, by using TCR-transgenic T cells from either wild-type or CD28-deficient mice, we showed that CD28 expression was required for the formation of the mature immunologic synapse, because antigen stimulation of CD28 ؊ T cells led to a diffuse pattern of localization of PKC and lymphocyte function-associated antigen-1 in the immunologic synapse, in contrast to the central supramolecular activation cluster localization of PKC in CD28 ؉ T cells.

Adhesive hydrogels hold great promise in multiple biomedical applications. However, there still exist practical challenges in underwater specific adhesion of hydrogels to biotic surfaces. Inspired by ctenophores, we develop an...