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1.
Transbound Emerg Dis ; 65(6): 1502-1513, 2018 Dec.
Article in English | MEDLINE | ID: mdl-29732720

ABSTRACT

Swine influenza viruses (SIVs) are important not only for pig farming, but also for public health. In fact, pandemic A(H1N1) 2009 viruses [A(H1N1)pdm09] were derived from SIVs. Therefore, timely characterization of locally circulating SIVs is necessary for understanding the global status of SIVs. To genetically characterize SIVs circulating in Japanese pig populations, we isolated 24 SIVs of three subtypes (17 H1N1, four H1N2 and three H3N2 strains) from 14 pig farms in Japan from 2013 to 2016. Genetic analyses revealed that the haemagglutinin (HA) and neuraminidase (NA) genes of the 17 H1N1 and the HA gene of one H1N2, A/swine/Aichi/02/2016 (H1N2), SIVs belonged to the A(H1N1)pdm09 lineage. More importantly, all of the remaining six gene segments (i.e., PB1, PB1, PA, NP, M and NS) of the 24 SIVs, regardless of the HA and NA subtype, were also classified as belonging to the A(H1N1)pdm09 lineage. These results indicate that gene segments of A(H1N1)pdm09 lineage are widely distributed in SIVs circulating in Japanese pig populations In addition, the NA gene of A/swine/Aichi/02/2016 (H1N2) shared less than 88.5% nucleotide identity with that of the closest relative A/swine/Miyagi/5/2003 (H1N2), which was isolated in Japan in 2003. These results indicate the sustained circulation of classical H1N2-derived SIVs with remarkable diversity in the NA genes in Japanese pig populations. These findings highlight the necessity of both intensive biosecurity systems and active SIV surveillance in pig populations worldwide for both animal and public health.


Subject(s)
Influenza A Virus, H1N1 Subtype/genetics , Influenza A Virus, H1N2 Subtype/isolation & purification , Influenza A Virus, H3N2 Subtype/isolation & purification , Orthomyxoviridae Infections/veterinary , Pandemics , Swine Diseases/epidemiology , Animals , Dogs , Genome, Viral/genetics , Humans , Japan , Madin Darby Canine Kidney Cells , Neuraminidase/genetics , Orthomyxoviridae Infections/epidemiology , Orthomyxoviridae Infections/virology , Phylogeny , Swine , Swine Diseases/virology , Viral Proteins/genetics
2.
Euro Surveill ; 20(20)2015 May 21.
Article in English | MEDLINE | ID: mdl-26027484

ABSTRACT

We isolated eight highly pathogenic H5N8 avian influenza viruses (H5N8 HPAIVs) in the 2014/15 winter season at an overwintering site of migratory birds in Japan. Genetic analyses revealed that these isolates were divided into three groups, indicating the co-circulation of three genetic groups of H5N8 HPAIV among these migratory birds. These results also imply the possibility of global redistribution of the H5N8 HPAIVs via the migration of these birds next winter.


Subject(s)
Animal Migration , Birds/virology , Genetic Variation , Influenza A virus/genetics , Influenza A virus/isolation & purification , Animals , Influenza A virus/classification , Influenza A virus/pathogenicity , Influenza in Birds/virology , Japan , Phylogeny , Seasons , Sequence Analysis, DNA
3.
Domest Anim Endocrinol ; 49: 14-9, 2014 Oct.
Article in English | MEDLINE | ID: mdl-25010023

ABSTRACT

We investigated the effect of sitagliptin, a dipeptidyl peptidase 4 inhibitor, on plasma incretin concentrations after glucose administration through an esophagostomy tube or feeding in healthy cats. Six cats were used for the glucose administration experiment and 5 cats were used for the feeding experiment. Glucose administration through an esophagostomy tube increased plasma glucagon-like peptide 1 (GLP-1) concentrations by 6-fold, whereas plasma glucose-dependent insulinotropic polypeptide (GIP) concentrations did not change. Feeding increased both plasma GLP-1 concentrations by 1.5-fold and GIP concentrations by 4.6-fold. Sitagliptin was administered through an esophagostomy tube (25 and 50 mg per cat) in the glucose administration experiment and orally (25 mg per cat) in the feeding experiment. Sitagliptin treatment potentiated the GLP-1 response to glucose by 1.5-fold (P < 0.05). In addition, postprandial plasma GLP-1 concentration was higher by 2-fold when sitagliptin was administered (P < 0.05). In contrast, administration of sitagliptin did not affect plasma GIP concentrations after glucose administration or feeding. Sitagliptin enhanced insulin secretion following glucose administration by 1.5-fold (P < 0.05); however, it did not influence the plasma glucose concentration. Furthermore, sitagliptin had no effect on the postprandial plasma glucose and insulin concentrations. In conclusion, this study provides no evidence that sitagliptin is beneficial for management of feline diabetes mellitus.


Subject(s)
Cats/blood , Glucose/pharmacology , Incretins/blood , Pyrazines/pharmacology , Triazoles/pharmacology , Administration, Oral , Animal Feed/analysis , Animals , Cats/physiology , Esophagostomy , Female , Gastric Inhibitory Polypeptide/genetics , Gastric Inhibitory Polypeptide/metabolism , Glucagon-Like Peptide 1/blood , Glucagon-Like Peptide 1/metabolism , Glucose/administration & dosage , Incretins/genetics , Incretins/metabolism , Male , Pyrazines/administration & dosage , Sitagliptin Phosphate , Triazoles/administration & dosage
4.
J Biol Chem ; 275(9): 6620-7, 2000 Mar 03.
Article in English | MEDLINE | ID: mdl-10692470

ABSTRACT

Canine red cells have a high affinity Na(+)/K(+)-dependent glutamate transporter. We herein demonstrate that this transport is mediated by the canine homologue of glutamate/aspartate transporter (GLAST), one of the glutamate transporter subtypes abundant in the central nervous system. We also demonstrate that GLAST is the most ubiquitous glutamate transporter among the transporter subtypes that have been cloned to date. The GLAST protein content was extremely reduced in variant red cells, low glutamate transport (LGlut) red cells characterized by an inherited remarkable decrease in glutamate transport activity. All LGluT dogs carried a missense mutation of Gly(492) to Ser (G492S) in either the heterozygous or homozygous state. The GLAST protein with G492S mutation was fully functional in glutamate transport in Xenopus oocytes. However, G492S GLAST exhibited a marked decrease in activity after the addition of cycloheximide, while the wild type showed no significant change, indicating that G492S GLAST was unstable compared with the wild-type transporter. Moreover, LGluT dogs, but not normal dogs, heterozygous for the G492S mutation showed a selective decrease in the accumulation of GLAST mRNA from the normal allele. Based on these findings, we conclude that a complicated heterologous combination of G492S mutation and some transcriptional defect contributes to the pathogenesis of the LGluT red cell phenotype.


Subject(s)
ATP-Binding Cassette Transporters/genetics , Erythrocytes/metabolism , Glutamic Acid/metabolism , ATP-Binding Cassette Transporters/metabolism , Amino Acid Sequence , Amino Acid Transport System X-AG , Animals , Biological Transport/drug effects , Biological Transport/genetics , Bone Marrow Cells , Brain , Cloning, Molecular , Dogs , Erythrocytes/pathology , Genetic Diseases, Inborn , Japan , Kinetics , Microinjections , Molecular Sequence Data , Mutation , Oocytes , Pedigree , RNA, Messenger/metabolism , Sequence Alignment , Xenopus
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