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1.
J Vet Med Sci ; 86(7): 796-800, 2024 Jul 02.
Artigo em Inglês | MEDLINE | ID: mdl-38839352

RESUMO

The control of digital dermatitis (DD) among cattle is crucial; however, effective and environmentally-sound control measures have yet to be identified. From the monitoring data of DD which were recorded during regular hoof trimmings in a farm in Hokkaido, Japan, we detected a decrease in the DD prevalence in a herd where an anaerobic bacterial fermentation enhancer (ABFE) was distributed. The possible effect of ABFE was analyzed using a retrospective repeated cross-sectional design. The prevalence of DD decreased over time in the ABFE-distributed group. Furthermore, a selected regression model indicated the time-dependent enhancement of the decreasing trend. While potential coincidental factors may influence, this study provides a basis for further research on the preventive effect of ABFE against DD.


Assuntos
Doenças dos Bovinos , Dermatite Digital , Fermentação , Animais , Bovinos , Estudos Retrospectivos , Dermatite Digital/microbiologia , Dermatite Digital/prevenção & controle , Doenças dos Bovinos/microbiologia , Doenças dos Bovinos/prevenção & controle , Japão , Estudos Transversais , Bactérias Anaeróbias , Casco e Garras/microbiologia
2.
Heliyon ; 9(6): e17065, 2023 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-37484309

RESUMO

In neurodegenerative diseases, the condensation of FUS and TDP-43 with RNA granules in neurons is linked to pathology, including synaptic disorders. However, the effects of FUS and TDP-43 on RNA granule factors remain unclear. Here, using primary cultured neurons from the mouse cerebral cortex, we show that excess cytoplasmic FUS and TDP-43 accumulated in dendritic RNA granules, where they increased the dynamics of a scaffold protein RNG105/caprin1 and dissociated it from the granules. This coincided with reduced levels of mRNA and translation around the granules and synaptic loss in dendrites. These defects were suppressed by non-dissociable RNG105, suggesting that RNG105 dissociation mediated the defects. In contrast to the model where FUS and TDP-43 co-aggregate with RNA granule factors to repress their activity, our findings provide a novel pathogenic mechanism whereby FUS and TDP-43 dissociate RNA scaffold proteins from RNA granules which are required for local translation that regulates synapse formation.

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