Traces of tritiated water (HTO) were detected at [the]World Trade Center (WTC) ground zero after the 9/11/01 terrorist attack. A method of ultralow-background liquid scintillation counting was used after distilling HTO from the samples. A water sample from the WTC sewer, collected on 9/13/01, contained 0.174 plus or minus 0.074 (2s) nCi/L of HTO. A split water sample, collected on 9/21/01 from the basement of WTC Building 6, contained 3.53 plus or minus 0.17 and 2.83 plus or minus 0.15 nCi/L, respectively. Several water and vegetation samples were analyzed from areas outside the ground zero, located in Manhattan, Brooklyn, Queens, and Kensico Reservoir. No HTO above the background was found in those samples. All these results are well below the levels of concern to human exposure.

Dantrolene is a drug that suppresses intracellular Ca2+ release from sarcoplasmic reticulum in normal skeletal muscle and is used as a therapeutic agent in individuals susceptible to malignant hyperthermia. Though its precise mechanism of action has not been elucidated, we have identified the N-terminal region (amino acids 1-1400) of the skeletal muscle isoform of the ryanodine receptor (RyR1), the primary Ca2+ release channel in sarcoplasmic reticulum, as a molecular target for dantrolene using the photoaffinity analog [3H]azidodantrolene(1). Here, we demonstrate that heterologously expressed RyR1 retains its capacity to be specifically labeled with [3H]azidodantrolene,indicating that muscle specific factors are not required for this ligand-receptor interaction. Synthetic domain peptides of RyR1, previously shown to affect RyR1 function in vitro and in vivo, were exploited as potential drug binding site mimics and used in photoaffinity labeling experiments. Only DP1 and DP1-2, peptides containing the amino acid sequence corresponding to RyR1 residues 590-609, were specifically labeled by [3H]azidodantrolene. A monoclonal anti-RyR1 antibody which recognizes RyR1 and its 1400 amino acid N-terminal fragment, recognizes DP1 and DP1-2 in both Western blots and immunoprecipitation assays, and specifically inhibits [3H]azidodantrolene photolabeling of RyR1 and its N-terminal fragment in sarcoplasmic reticulum. Our results indicate that synthetic domain peptides can mimic a native, ligand binding conformation in vitro, and that the dantrolene binding site and the epitope for the monoclonal antibody on RyR1 are equivalent and composed of amino-acids 590-609.