Epo’s neuroprotective and neuroregenerative functions mediated through janus kinases (JAK)/signal transducers and activators of transcription (STAT) transduction pathways and regulation of Epo and Epo receptor expression in the nervous system by hypoxia inducible factor (HIF) have been documented in a variety of in vitro and in vivo studies and homologs of the human Epo gene are present in fish, amphibians and mammals. The present study reproduces the hallmarks of Epo-mediated mammalian neuroprotection in the grasshopper nervous system. Recombinant human Epo (rhEpo) increases the survival of dissociated grasshopper brain neurons

under normoxic and hypoxic selleck chemicals conditions and promotes the regeneration of neurites in vitro. In addition, reestablishment of sound source localization after unilateral tympanic nerve crush injury was accelerated and more complete after application of rhEpo, demonstrating in vivo support of auditory receptor cell axon regeneration. Immunoblots of central nervous tissue extracts from mouse, grasshopper, crayfish and leech labeled protein bands of similar to 38 kDa, fitting to the molecular weight of Epo reported in earlier studies. These results indicate that a ligand/receptor system that shares structural

and functional similarities with mammalian Epo and Epo receptor exerts neuroprotective and neuroregenerative effects in insects. With both upstream (HIF check details system) and downstream (JAK/STAT pathway) elements of the mammalian Epo system being present in insects and other invertebrates, Epo-like signaling involved in tissue protection appears to be an ancient beneficial function shared by vertebrates and invertebrates. (C) 2011 IBRO. Published by Elsevier Ltd. All rights reserved.”
“Arenaviruses are enveloped RNA

viruses with a nonlytic life cycle that cause acute and persistent infections. Here, we investigated the role of the host cell’s unfolded protein response (UPR) in infection of the prototypic arenavirus lymphocytic choriomeningitis virus (LCMV). In mammalian cells, the endoplasmic reticulum (ER) chaperone protein Neratinib supplier GRP78/BiP functions as the principal sensor for the induction of the UPR and interacts with three mediators: kinase/endonuclease inositol-requiring protein 1 (IRE1), PKR-like ER kinase (PERK), and activating transcription factor 6 (ATF6). Acute infection with LCMV resulted in a selective induction of the ATF6-regulated branch of the UPR, whereas pathways controlled by PERK and IRE1 were neither activated nor blocked. Expression of individual LCMV proteins revealed that the viral glycoprotein precursor (GPC), but not that of other viral proteins, was responsible for the induction of ATF6.