L 1991), changes in ion channel function (Yeung et al. 2004), or alterations
L 1991), adjustments in ion channel function (Yeung et al. 2004), or Protein A Magnetic Beads Storage alterations in cell signaling (Thomas et al. 1998). Our findings help the more possibility that alterations in myofiber morphology may possibly contribute to a lower in CDCP1, Mouse (Biotinylated, HEK293, His-Avi) muscle function also as an apparent elevated susceptibility to harm by demonstrating alterations on AP temporal properties, decreased AP-induced global Ca2+ signals in MDX fibers, and substantial asymmetries inside the amplitude of APinduced Ca2+ signals in branched segments of malformed myofibers as well as a rise in the susceptibility to mechanical pressure. We and others (Head et al. 1990; Chan et al. 2007) have shown that the architecture of dystrophic muscle myofibers becomes far more abnormal with age, which may well clarify why, despite the constant lack of dystrophin, MDX skeletal muscle generates less precise force and becomes more susceptible to damage with age (Chan et al. 2007). The finding that myofibers with abnormal morphology are functionally weak and more simply broken (Head et al. 1990) supports this notion. The pathophysiological implications of these alterations in myofiber excitability, Ca2+ signaling, biomechanics and contractility as well as the underlying mechanisms, might be the following goals of future studies.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 two, : , 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 2, 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.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; [email protected] Animal Biotechnology Division, National Institute of Animal Science (NIAS), Rural Improvement Administration (RDA), 1500, Kongjwipatjwi-ro, Iseomyeon, Wanju 55365, Korea; [email protected] 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 with the viral RNA genome by way 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 potential of 3D8 scFv to penetrate into epithelial cells from bronchial cavity via the respiratory mucosal layer was confirmed by immunohistochemistry, qRT-PCR, and histopathological examination. The antiviral activity of 3D8 scFv against H1N1 vir.
