L 1991), alterations in ion channel function (Yeung et al. 2004), or alterations in cell signaling (Thomas et al. 1998). Our findings support the more possibility that adjustments in myofiber morphology might contribute to a reduce in muscle function as well as an apparent improved susceptibility to harm by demonstrating alterations on AP temporal properties, decreased AP-induced international Ca2+ signals in MDX fibers, and considerable asymmetries inside the amplitude of APinduced Ca2+ signals in branched segments of malformed myofibers too as a rise inside the susceptibility to mechanical pressure. We and other people (Head et al. 1990; Chan et al. 2007) have shown that the architecture of dystrophic muscle myofibers becomes much more abnormal with age, which could explain why, regardless of the constant lack of dystrophin, MDX skeletal muscle generates much less certain force and becomes a lot more susceptible to damage with age (Chan et al. 2007). The obtaining that myofibers with abnormal morphology are functionally weak and more simply damaged (Head et al. 1990) supports this notion. The pathophysiological implications of these alterations in myofiber excitability, Ca2+ signaling, biomechanics and contractility as well because the underlying mechanisms, will probably be the following objectives of future research.Conflict of InterestThere are no competing interests or conflicts of interests for any authors.
ArticlePreventive Activity against Influenza (H1N1) Virus by Intranasally Delivered RNA-Hydrolyzing Antibody in Respiratory Epithelial Cells of MiceSeungchan Cho 1, : , Ha-Na Youn 2, : , Phuong Mai Hoang 1, : , Sungrae Cho 1 , Kee-Eun Kim 1 , Eui-Joon Kil 1 , Gunsup Lee 1 , Mun-Ju Cho 1 , Juhyun Hong 1 , Sung-June Byun 3 , Chang-Seon Song two, and Sukchan Lee 1, Received: 7 July 2015 ; Accepted: 14 September 2015 ; Published: 21 September 2015 Academic Editor: Curt Hagedorn2 :Division of Genetic Engineering, Sungkyunkwan University, 2066, Seobu-ro, Jangan-gu, Suwon 16419, Korea; seungchan1007@gmail (S.Outer membrane C/OmpC, Klebsiella pneumoniae (His, myc) C.); hmphuong2802@gmail (P.M.H.); sungle89@gmail (S.C.); happykke6@naver (K.-E.K.); meitantei007@naver (E.-J.K.); asteroid1975@gmail (G.L.); munju2004@naver (M.-J.C.); rsef741@gmail (J.H.) Avian Disease Laboratory, College of Veterinary Medicine, Konkuk University, 120, Neungdong-ro, Gwangjin-gu, Seoul 05029, Korea; yellow0891@daum.FOLR1 Protein medchemexpress net Animal Biotechnology Division, National Institute of Animal Science (NIAS), Rural Improvement Administration (RDA), 1500, Kongjwipatjwi-ro, Iseomyeon, Wanju 55365, Korea; pcs1778@korea.PMID:23614016 kr Correspondence: [email protected] (C.-S.S.); [email protected] (S.L.); Tel.: +82-2-710-9396 (C.-S.S.); +82-31-290-7866 (S.L.); Fax: +82-2-2077-7322 (C.-S.S.); +82-31-290-7870 (S.L.) These authors contributed equally to this operate.Abstract: The antiviral impact of a catalytic RNA-hydrolyzing antibody, 3D8 scFv, for intranasal administration against avian influenza virus (H1N1) was described. The recombinant 3D8 scFv protein prevented BALB/c mice against H1N1 influenza virus infection by degradation in the viral RNA genome by means of its intrinsic RNA-hydrolyzing activity. Intranasal administration of 3D8 scFv (50 /day) for 5 days before infection demonstrated an antiviral activity (70 survival) against H1N1 infection. The antiviral capacity of 3D8 scFv to penetrate into epithelial cells from bronchial cavity by means of the respiratory mucosal layer was confirmed by immunohistochemistry, qRT-PCR, and histopathological examination. The antiviral activity of 3D8 scFv against H1N1 vir.