Publications by authors named "M Misaka"

We aimed to characterize the change in the incidence of stillbirth (IS) in Japanese Black cattle during and after animal movement restrictions and suspended insemination because of a foot-and-mouth disease (FMD) outbreak in Miyazaki Prefecture in 2010. Calving data from 2006 to 2018 were collected from approximately 900 farms. Post-FMD period was divided into three based on the median IS per month (1.

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The objective of this study was to investigate the effect of herd size on stillbirth and dystocia rates; the relationships between herd size, calving season, parity, and gestation length in Japanese Black cattle were also explored. Data were collected for 41,184 calvings from 15,512 animals on 905 farms between 2006 and 2010. In this study, herds were classified into three groups based on size: small (1−10 cows), medium (11−50 cows), and large (≥51 cows).

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Calf mortality severely affects productivity in the beef industry. The present study was conducted to assess the calf mortality risk (CMR) in Japanese Black calves and investigate potential associations between calf/cow information and the CMR. Records for calves born between April 2006 and March 2010 were extracted from an existing database, which included production data on commercial cow-calf operations in Miyazaki, Japan.

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We have demonstrated that gene delivery of a fusion protein of mouse interferon (IFN) γ with mouse serum albumin (IFNγ-MSA) was effective in prolonging the circulation half-life of IFNγ in mice. However, the fusion to MSA greatly reduced the biological activity of IFNγ to less than 1%. In this study, we designed IFNγ fusion proteins with a 20 amino-acid long albumin-binding peptide (ABP) to prolong the in vivo half-life of IFNγ without reducing its biological activity.

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Gene delivery of mouse interferon (IFN) γ has been shown to inhibit metastatic tumor growth and onset of atopic dermatitis in mouse models. In this study, we tried to increase the circulation half-life of IFNγ after its gene delivery by designing a novel fusion protein of IFNγ with mouse serum albumin (MSA). Western blot analysis confirmed that IFNγ-MSA was expressed as a fusion protein, but hardly formed dimer as IFNγ did.

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