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Occupational noise-induced hearing loss is the second most self-reported occupational illness or injury in the United States. Among coal miners, more than 90% of the population reports a hearing deficit by age 55. In this formative evaluation, focus groups were conducted with coal miners in Appalachia to ascertain whether miners perceive hearing loss as a major health risk and if so, what would motivate the consistent wearing of hearing protection devices (HPDs). The theoretical framework of the Extended Parallel Process Model was used to identify the miners' knowledge, attitudes, beliefs, and current behaviors regarding hearing protection. Focus group participants had strong perceived severity and varying levels of perceived susceptibility to hearing loss. Various barriers significantly reduced the self-efficacy and the response efficacy of using hearing protection. (Contains 1 table and 1 figure.)

We used a genetic screening methodology, a human cell line bearing a retinoic-acid-responsive enhanced GFP reporter, and a flow sorter to recover dominant modulators of reporter expression. Four inducers and three suppressors that were fused to the C terminus of a protein scaffold for stability were isolated and their mechanisms of action studied. Mutagenesis experiments indicated that six of these dominant agents exerted their effects at the protein level. The single cDNA coding fragment that was isolated comprised the central 64-amino-acid section of human cyclophilin B, which contained its peptidyl-prolyl isomerase domain; this cyclophilin fragment repressed expression of the retinoic-acid-responsive reporter. The remaining clones encoded peptides shorter than 30 amino acids unrelated to known gene open reading frames. Genetic epistasis studies between the strongest inducer, R3, and a dominant-negative mutant of RAR[alpha] suggest that the two factors function in the same pathway. Transcript microarray analyses suggest that R3 induced a subset of the retinoid-responsive genes in melanoma cells. Finally, yeast two-hybrid assays and co-immunoprecipitation studies of human cell extracts identified PAT1 as a protein that interacts with R3.

INTRODUCTION Although U.S. health care workers face a variety of occupational health and safety hazards, one of the most serious is exposure to blood-borne pathogens through needlesticks. (1-6) The estimate […]

The assembly of the copper sites in cytochrome c oxidase involves a series of accessory proteins, including Cox11, Cox17, and Scol. The two mitochondrial inner membrane proteins Cox11 and Scol are thought to be copper donors to the CuB and CuA sites of cytochrome oxidase, respectively, whereas Cox17 is believed to be the copper donor to Scol within the intermembrane space. In this report we show Cox17 is a specific copper donor to both Scol and Cox11. Using in vitro studies with purified proteins, we demonstrate direct copper transfer from CuCox17 to Scol or Cox11. The transfer is specific because no transfer occurs to heterologous proteins, including bovine serum albumin and carbonic anhydrase. In addition, a C57Y mutant of Cox17 fails to transfer copper to Scol but is competent for copper transfer to Cox11. The in vitro transfer studies were corroborated by a yeast cytoplasm expression system. Soluble domains of Scol and Cox11, lacking the mitochondrial targeting sequence and transmembrane domains, were expressed in the yeast cytoplasm. Metallation of these domains was strictly dependent on the co-expression of Cox17. Thus, Cox17 represents a novel copper chaperone that delivers copper to two proteins. [ABSTRACT FROM AUTHOR]