Background Low temperature plasmas have been proposed in medicine as agents for tissue disinfection and have received increasing attention due to the frequency of bacterial resistance to antibiotics. This study explored whether atmospheric-pressure cold plasma (APCP) generated by a new portable device that ionizes a flow of helium gas can inactivate ocular pathogens without causing significant tissue damage. Methodology/Principal Findings We tested the APCP effects on cultured Pseudomonas aeruginosa , Escherichia coli , Staphylococcus aureus , Candida albicans , Aspergillus fumigatus and Herpes simplex virus-1, ocular cells (conjunctival fibroblasts and keratocytes) and ex-vivo corneas. Exposure to APCP for 0.5 to 5 minutes significantly reduced microbial viability (colony-forming units) but not human cell viability (MTT assay, FACS and Tunel analysis) or the number of HSV-1 plaque-forming units. Increased levels of intracellular reactive oxygen species (ROS) in exposed microorganisms and cells were found using a FACS-activated 2′,7′-dichlorofluorescein diacetate probe. Immunoassays demonstrated no induction of thymine dimers in cell cultures and corneal tissues. A transient increased expression of 8-OHdG, genes and proteins related to oxidative stress (OGG1, GPX, NFE2L2), was determined in ocular cells and corneas by HPLC, qRT-PCR and Western blot analysis. Conclusions A short application of APCP appears to be an efficient and rapid ocular disinfectant for bacteria and fungi without significant damage on ocular cells and tissues, although the treatment of conjunctival fibroblasts and keratocytes caused a time-restricted generation of intracellular ROS and oxidative stress-related responses.

Line blot could be a suitable serological test in the diagnostic workup for myositis, and it represents a reliable alternative to more time-consuming procedures. Continuous effort is recommended in order to improve its accuracy.

␣-Sarcoglycan is a component of the sarcoglycan complex of dystrophin-associated proteins. Mutations of any of the sarcoglycan genes cause specific forms of muscular dystrophies, collectively termed sarcoglycanopathies. Importantly, a deficiency of any specific sarcoglycan affects the expression of the others. Thus, it appears that the lack of sarcoglycans deprives the muscle cell of an essential, yet unknown function. In the present study, we provide evidence for an ecto-ATPase activity of ␣-sarcoglycan. ␣-Sarcoglycan binds ATP in a Mg Dystrophin is a large cytoskeletal protein associated with a complex of integral and peripheral membrane proteins collectively termed DAPs.1 Dystrophin is a long filamentous protein comprising four distinct structural domains: the amino-terminal domain, which binds F-actin, the rod-like central domain; the cysteine-rich domain, which binds the cytoplasmic portion of ␤-dystroglycan and syntrophins; and the carboxyl-terminal domain (1). The DAPs complex is composed of three subcomplexes: syntrophins, dystroglycans, and sarcoglycans (2, 3). Syntrophins are peripheral membrane proteins of unknown function that bind the carboxyl terminus of dystrophin (4, 5). Dystroglycans consist of two proteins derived from a common precursor protein: ␣-dystroglycan, a peripheral glycoprotein that binds extracellular matrix proteins like laminin-2 (merosin) and, in the neuromuscular junction, laminin-4 (agrin); and ␤-dystroglycan, an intrinsic membrane protein that binds dystrophin at its cytoplasmic tail and ␣-dystroglycan at the opposite end (6, 7). Therefore, the dystroglycans represent the link between the subsarcolemmal actin cytoskeleton and the extracellular matrix through dystrophin. Five sarcoglycans have been described: ␣-sarcoglycan (adhalin, 50 kDa), ␤-sarcoglycan (43 kDa), ␥-and ␦-sarcoglycans (35 kDa) (8 -10), and ⑀-sarcoglycan (11, 12). The function of the sarcoglycans remains unknown.Dystrophin is defective in Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy. In patients with DMD and in the mdx mouse, an animal model for DMD, all of the components of the DAPs are severely reduced at the sarcolemma (13, 14), even though they are almost normal at the neuromuscular junction (15).Mutations in the ␣-sarcoglycan gene, which is located on chromosome 17q21 (10), were demonstrated in limb girdle muscular dystrophy-2D (LGMD-2D), an autosomal recessive muscular dystrophy that affects both females and males (16,17). In LGMD-2D, ␤-and ␥-sarcoglycan were also absent or greatly reduced, whereas dystrophin and the dystroglycan complex were preserved (18). Similar modifications were also found in the skeletal muscle of the cardiomyopatic hamster, an animal model of this disease (19). Recently, mutations in the genes that encode for ␤-, ␥-, and ␦-sarcoglycan, located on chromosomes 4q12, 13q12, and 5q33-34, were discovered in LGMD-2E, -2C, and -2F, respectively (9,20,21). These mutations caused the absence not only of the respective protein product but also of the other three components...