Although the domestic dog's origin is still unclear, this lineage is believed to have been domesticated from an extinct population of gray wolves, which is expected to be more closely related to dogs than to other populations of gray wolves. Here, we sequence the whole genomes of nine Japanese wolves (7.5-100x: Edo to Meiji periods) and 11 modern Japanese dogs and analyze them together with those from other populations of dogs and wolves.
View Article and Find Full Text PDFIn this study using computed tomography (CT), the volumes of the internal cranial cavities, such as the braincase, frontal sinus and tympanic cavity, and the ratio of the volume of each cavity to the skull volume in Japanese wolves were quantified, and CT images of the frontal sinus were observed. The results were then compared with those of other wolf subspecies, including Akita, a dog breed, to clarify the characteristics of the internal cranial cavities in Japanese wolves. The present study revealed that the Japanese wolf had a relatively larger braincase volume and a relatively smaller frontal sinus volume than the wolf ssp.
View Article and Find Full Text PDFThe taxonomic status of extinct Japanese or Honshu wolves () has been disputed since the name was first proposed by Temminck in 1839 on the basis of specimens stored in Leiden, the Netherlands. Points of controversy include whether the type specimen of (Jentink c: RMNH.MAM.
View Article and Find Full Text PDFGenetics of pigs has been well studied in Europe and Asia, but most of previous studies of molecular phylogeny of Sus scrofa have been based on sequences of both wild and domestic forms. In this study we analysed genetic traits of Sus scrofa from 13 regions in Asia (including previously undisclosed Eastern Caucasus and Trans-Baikal regions) using purely wild boar samples. Mitochondrial control region and Y-chromosome genes (AMELY & USP9Y) were employed to resolve phylogeographic relationships.
View Article and Find Full Text PDFSerum amyloid A (SAA) is both an amyloidogenic protein of amyloid A amyloidosis and an acute phase protein in most animal species. Although SAA isoforms, such as SAA1, 2, 3, and 4, have been identified in cattle, their biological functions are not completely understood. Previous studies using mice indicated that SAA3 mRNA expression increased by stimulation with Escherichia coli and lipopolysaccharide (LPS) in colonic epithelial cells, and subsequently the SAA3 protein enhanced the expression of mucin2 (MUC2) mRNA, which is the major component of the colonic mucus layer.
View Article and Find Full Text PDFA monoclonal antibody (mAb) G2 possesses an unusual characteristic of reacting with at least three proteins (ATP6V1C1, SEPT3, and C6H10orf76) other than its original antigen, chicken prion protein (ChPrP). The epitopes on ChPrP and ATP6V1C1 have been identified previously. In this study, we identified the epitope in the third protein, SEPT3.
View Article and Find Full Text PDFSerum amyloid A (SAA) is the major acute-phase protein and a precursor of amyloid A (AA) in AA amyloidosis in humans and animals. SAA isoforms have been identified in a wide variety of animals, such as SAA1, SAA2, SAA3, and SAA4 in mouse. Although the biological functions of SAA isoforms are not completely understood, recent studies have suggested that SAA3 plays a role in host defense.
View Article and Find Full Text PDFBiochem Biophys Res Commun
September 2017
The monoclonal antibody, G2, specifically binds to the immunogen peptide derived from the chicken prion protein, Pep18mer, and two chicken proteins derived peptides, Pep8 and Pep395; G2 binds with equal affinity to Pep18mer. The amino acid sequences of the three peptides are completely different, and so the recognition mechanism of G2 is unique and interesting. We generated a single-chain Fv (scFv) antibody of G2, and demonstrated its correct folding with an antigen binding function similar to intact G2 antibody.
View Article and Find Full Text PDFAA amyloidosis is a protein misfolding disease characterized by extracellular deposition of amyloid A (AA) fibrils. AA amyloidosis has been identified in food animals, and it has been postulated that AA amyloidosis may be transmissible to different animal species. Since the precursor protein of AA fibrils is serum amyloid A (SAA), which is an inflammatory acute phase protein, AA amyloidosis is considered to be associated with inflammatory diseases such as rheumatoid arthritis.
View Article and Find Full Text PDFA Canis skull, right half of the mandible and part of the left half of the mandible were subjected to three-dimensional (3D) computed tomography (CT) observation and mitochondrial DNA (mtDNA) analysis in order to determine whether the specimens belonged to the extinct Japanese wolf, Canis lupus hodophilax (Temminck, 1839). Osteometric analysis of the skull and right half of the mandible revealed that the material (JW275) was indeed typical of the Japanese wolf. Sequence analysis of a 600-bp mtDNA region revealed that the JW275 belonged to haplotype Group B, which is characterized by an 8-bp deletion in the mtDNA control region.
View Article and Find Full Text PDFOrf virus infection has been prevalent continuously in the population of wild Japanese serows (Capricornis crispus), goat-like grazing cloven-hoofed mammal species that live mainly in mountainous areas of Japan. Currently, definitive diagnosis of infection requires time-consuming laboratory work. To diagnose rapidly on-site, we developed a field-friendly procedure for the detection of orf virus from oral cavity lesions.
View Article and Find Full Text PDFObjective: To investigate pathogenesis and kinetics of experimentally induced murine AA amyloidosis seeded with homologous (murine) and heterologous (bovine) AA fibrils.
Methods: Experimental AA amyloidosis was induced by administration of inflammatory stimulus and preformed AA fibrils to a total of 111 female C57/Black mice. In this longitudinal study, heterologous (bovine) as well as homologous (murine) AA fibrils were injected intraperitoneally to mice in various combinations.
The mitochondrial DNA (mtDNA) control region (198- to 598-bp) of four ancient Canis specimens (two Canis mandibles, a cranium, and a first phalanx) was examined, and each specimen was genetically identified as Japanese wolf. Two unique nucleotide substitutions, the 78-C insertion and the 482-G deletion, both of which are specific for Japanese wolf, were observed in each sample. Based on the mtDNA sequences analyzed, these four specimens and 10 additional Japanese wolf samples could be classified into two groups- Group A (10 samples) and Group B (4 samples)-which contain or lack an 8-bp insertion/deletion (indel), respectively.
View Article and Find Full Text PDFRinsho Biseibutshu Jinsoku Shindan Kenkyukai Shi
June 2016
Temperature-stability of loop-mediated isothermal amplification (LAMP) reagents was determined for their use in on-site diagnosis, such as in farms/pastures. Bst and Csa DNA polymerases and the reagents that were stored at different temperatures (4 or 25°C) for 1, 2, or 4 days were used for the LAMP assay to detect orf virus DNA as a model. After storage at 4 and 25°C for 2 days, the enzymes and reagents were found to retain sufficient activity to carry out successful DNA amplification.
View Article and Find Full Text PDFAmyloid A (AA) amyloidosis is a protein misfolding disease characterized by extracellular deposition of AA fibrils. AA fibrils are found in several tissues from food animals with AA amyloidosis. For hygienic purposes, heating is widely used to inactivate microbes in food, but it is uncertain whether heating is sufficient to inactivate AA fibrils and prevent intra- or cross-species transmission.
View Article and Find Full Text PDFAvian amyloid A (AA) amyloidosis is commonly observed in adult birds with chronic inflammation, such as that caused by bacterial infection. We previously described vaccine-associated AA amyloidosis in juvenile chickens. In this study, the prevalence of amyloid deposition was measured in mature healthy chickens that survived a previous outbreak of avian AA amyloidosis while they were juveniles.
View Article and Find Full Text PDFA number of studies have suggested that macrophages, dendritic cells, and follicular dendritic cells play an important role in the propagation of PrP(Sc). Both accumulation and proteolysis of PrP(Sc) have been demonstrated in peripheral macrophages. Macrophages may act as reservoirs for PrP(Sc) particles if the cells die during transient PrP(Sc) propagation.
View Article and Find Full Text PDFAmyloidosis is a collective term for a group of disorders that induce functional impairment of organs and occurs through the accumulation of amyloid, or misfolded protein in beta-sheets. AA amyloidosis is a lethal systemic amyloidosis with SAA as the precursor protein, and is observed in various animal species, including humans. AA amyloidosis can be induced artificially by continuously administering inflammatory stimuli in experimental animal models.
View Article and Find Full Text PDFA portable cordless incubator was developed for on-site visual diagnosis of parapoxvirus infection on farms and in areas with no electricity or laboratory equipment. The battery-powered thermoregulator can maintain a stable temperature for more than 1 h. The incubator successfully amplified parapoxvirus DNA isolated from sheep and wild Japanese serows (Capricornis crispus) by loop-mediated isothermal amplification (LAMP).
View Article and Find Full Text PDFThe grey wolves (Canis lupus) originally inhabited major parts of the Northern hemisphere, but many local populations became extinct. Two lineages of wolves in Japan, namely, Japanese or Honshu (C. l.
View Article and Find Full Text PDFBackground: Cross-species transmission of AA amyloidosis between primates and other animals has not been previously reported.
Methods: Eight geriatric squirrel monkeys were intravenously administered chimpanzee, bovine, or chicken amyloid fibrils and simultaneously received inflammatory stimulation.
Results: AA amyloid deposition was not detected in any of the monkeys histopathologically or immunohistochemically.
Background: Wild boar, Sus scrofa, is an extant wild ancestor of the domestic pig as an agro-economically important mammal. Wild boar has a worldwide distribution with its geographic origin in Southeast Asia, but genetic diversity and genetic structure of wild boar in East Asia are poorly understood. To characterize the pattern and amount of genetic variation and population structure of wild boar in East Asia, we genotyped and analyzed microsatellite loci for a total of 238 wild boar specimens from ten locations across six countries in East and Southeast Asia.
View Article and Find Full Text PDFWe previously generated a monoclonal antibody (mAb), G2, by immunizing mice with Residues 174-247 of the chicken prion protein (ChPrP(C) ). In this study, we found that G2 possessed an extremely unusual characteristic for a mAb; in particular, it could react with at least three proteins other than ChPrP(C) , the original antigenic protein. We immunoscreened a complementary DNA library from chicken brain DNA and found three proteins (SEPT3, ATP6V1C1, and C6H10orf76) that reacts with G2.
View Article and Find Full Text PDFSerum amyloid A (SAA) proteins are acute-phase proteins and are classified into multiple isoforms; however, the biological functions of each SAA isoform are not fully understood. In this study, to clarify the roles of SAA3 in the intestine, we characterized mRNA expression in mouse colonic epithelial CMT-93 cells treated with rotavirus, Toxoplasma, Staphylococcus aureus, and Escherichia coli, as well as lipopolysaccharide (LPS) and recombinant murine SAAs (rSAAs). E.
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