Trophinin is a membrane protein that mediates apical cell adhesion between trophoblastic cells and luminal epithelial cells of the endometrium and is implicated in the initial attachment during the process of human embryo implantation. The present study identified novel trophinin gene transcripts, which encode proteins structurally distinct from trophinin protein in the mouse. We designated these proteins "magphinins," because they share consensus amino acid sequences with MAGE (melanoma-associated antigen) superfamily proteins. Among many MAGE proteins, magphinins are closely related to NRAGE, which mediates p75 neurotrophin receptor-dependent apoptosis, and necdin, which is a strong suppressor of cell proliferation in post-mitotic neurons. There are three major forms of magphinins, i.e. magphinin-␣, -, and -␥, in the mouse, which are formed due to alternative usage of different exons. Northern blot analysis revealed that magphinins are expressed in brain, ovary, testis, and epididymis. In addition, Western blot analysis and in vitro translation experiments showed that magphinins expressed in the mouse ovary and testis are translation products utilizing the second initiation AUG codon and contain an active nuclear localization signal. Ectopic expression of magphinins in mammalian cells resulted in nuclear localization of magphinin and suppressed cell proliferation. Immunohistochemistry of the mouse ovary and testis showed that magphinin proteins are distributed in the cytoplasm of the male and female germ cells, whereas these proteins are translocated to the nucleus at a specific stage of gametogenesis. These results strongly suggest that magphinins regulate cell proliferation during gametogenesis in the mouse.Mammals retain distinctions with regard to the strategies used to protect and nourish their offspring during development, namely by the process of embryo implantation and placentation. The process of implantation varies markedly between species (1), and genes involved in this process display remarkably high spontaneous mutational rates (2), suggesting a strong adaptive selection pressure. The study of human embryo implantation at the molecular level is hampered by the fact that in vivo studies with an implanting embryo in place are difficult to perform and are generally considered ethically unacceptable. To overcome this problem, we established an in vitro cell culture system using two human cell lines, trophoblastic teratocarcinoma HT-H and endometrial adenocarcinoma SNG-M. These two cell types adhered with each other at their respective apical cell membranes and exhibited morphologies resembling the cells at the initial adhesion steps of embryo implantation (3, 4).Using this model system, we identified a unique protein, trophinin, by means of expression cloning. Thus a mammalian expression cDNA library constructed from HT-H cells was transfected into COS cells, and COS cells that became adhesive to SNG-M cells were selected. When COS cells acquired trophinin and trophinin-associated cytoplasmic protein...
Hemagglutinin (H) gene of two CDV isolates, the Haku93 and Haku00 strains, from masked palm civets was molecularly analyzed. H genes of both two CDVs contained one open reading frame encoding 607 amino acids. Nucleotide and predicted amino acid sequences of H gene of the CDV Haku93 and Haku00 revealed high similarity to those of recent field isolates such as the Yanaka and Tanu96, while they showed limited identity to those of old vaccine strains. Potential N-linked glycosylation sites in both Haku93 and Haku00 were identical to other recent CDV isolates. Phylogenetic analysis revealed that the CDV strains derived from masked palm civets were classified into the group of recent Japanese CDV isolates.
ABSTRACT. Cytotoxic T-lymphocyte (CTL) responses to hemagglutinin (H) protein of canine distemper virus (CDV) were evaluated in dogs using the replication-deficient adenovirus protein expression system. Skin fibroblasts were isolated from two dogs and were infected with recombinant adenovirus bearing the CDV-H gene (Ade-CDVH). CTL assay was performed using fibroblasts expressing CDV-H protein as target cells and peripheral blood lymphocytes (PBL) collected from the same dogs one week after immunization of CDV as effector cells. Specific cytotoxic activity was observed against autologous but not heterologous fibroblasts expressing Canine distemper virus (CDV) belongs to the genus Morbillivirus family Paramyxoviridae and induces fatal diseases including encephalitis with demyelination, diarrhea and respiratory disorders in dogs. CDV infection had been well controlled by vaccination. However, epidemics of CDV infection have been appeared in the last decade even in vaccinated dogs [6,7].Cytotoxic T lymphocytes (CTL) play an important role in the immune system for the clearance and protection against morbilliviruses [3,22]. CTL epitopes and responses to measles virus (MV) infection have been well studied in a mouse model. The major target antigen for CTL in mice was identified as the nucleocapsid (N) protein by several groups, which can induce cross reactive CTL between MV and CDV [1-3, 15, 19]. In addition, it was also reported that H protein of MV [1] and CDV [21] could be one of the CTL epitopes in mice. However, Jaye et al. reported that the fusion (F) and hemagglutinin (H) proteins were important targets for measles CTL responses in humans, a natural host of MV, receiving measles polypetides [11]. On the other hand, CTL responses in infection with another morbillivirus, rinderpest virus (RPV), were also analyzed in mice and cattle, the latter of which is a natural host of RPV. A CTL response against RPV N protein was detected and a CTL epitope within the N protein was identified in the mouse model [13]. However, the role of N protein in protection and induction of CTL responses against RPV infection in cattle was limited [16]. The CTL response against H protein in cattle is more effective and its effect lasts for at least two years [17,20]. These discrepant results suggested that the CTL response in the mouse model does not always reflect that in the natural host, and analyses concerning the development of CTL activity using the virus and the natural host are required.Restriction of the major histocompatibility complex (MHC) in CTL assay makes it difficult to develop an assay system in outbred animals. Recently, an easy method to produce recombinant adenoviruses based on a replicationdeficient adenovirus vector was established, and this method has been shown to be useful for delivery of vectors for gene therapy and protein expression [12,14]. The adenovirus vector possesses useful characteristics such as high level of protein expression, broad host cell range, applicability to non-replicating cells including neu...
BackgroundHaemaphysalis longicornis ticks represent an ectoparasitic health threat to dogs. This study evaluated the immediate and persistent efficacy of orally administered fluralaner for control of this tick.MethodsTwenty-four dogs were sorted into 4 groups based on their tick carrying capacity measured in a preliminary challenge. Two days before treatment, dogs were challenged with Haemaphysalis longicornis and then at the time of treatment dogs received with oral fluralaner at 10, 25 or 50 mg/kg respectively to 3 of the groups, while the remaining group was sham treated. Ticks were counted and categorized on all dogs 2 days after treatment (4 days after challenge). Tick challenges were repeated at 28, 56, 84 and 112 days following treatment with tick counts 48 hours following each challenge. Tick control efficacy was evaluated by comparing the mean (geometric) total live attached and dead engorged ticks on each fluralaner treated group with the sham treated dogs.ResultsOral fluralaner is highly acaricidal for H. longicornis that feed on treated dogs. The mean efficacy rate in dogs treated with fluralaner at the commercial dose range of 25 to 50 mg/kg was greater than 90% at 114 days after treatment, whereas efficacy at this time in dogs treated at 10 mg/kg was 79%.ConclusionsFluralaner administered orally to dogs within the commercial dose range at 25 to 50 mg/kg is effective for up to 114 days against laboratory challenge with H. longicornis ticks.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.