Dr. Bruce Pitt is leading a research team in efforts to gain a better understanding of the role of S-nitrosylation of the metal binding intracellular protein, metallothoinein, on zinc homeostasis and endothelial cell function. These studies are aided by a number of microspectrofluorometric approaches, including a green fluorescent protein modified chimera of metallothionein, suitable for fluorescence resonance energy transfer. This chimera contains an enhanced cyan fluorescent protein (ECYP) that serves as a donor for an enhanced yellow flourescence protein (EYFP) that are fused to the N- and C-termini respectively of human metallothionein Iia (hMTIIa). The result of these live cell fluorescence image studies has identified a unique role for metallothionein in NO mediated zinc release. NO mediated changes in labile zinc appear to be inhibitory in proapoptotic conditions in pulmonary endothelial cells, contributing to the notion that S-nitrosylation of zinc sulfur clusters is an important component of NO signaling.
The role of metallothoinein on zinc homeostasis and endothelial cell function