RESUMO
This study reports faecal prevalence of Clostridium perfringens in free range ducks in North East India for the first time. We also report C. perfringens type A carrying cpb2 and cpe and type C carrying cpb2 and cpe strains in these ducks. Notably, a high prevalence (17.5%) of enterotoxin carrying C. perfringens strains and low antimicrobial resistance were observed.
Assuntos
Antibacterianos/farmacologia , Infecções por Clostridium/veterinária , Clostridium perfringens/efeitos dos fármacos , Clostridium perfringens/genética , Farmacorresistência Bacteriana Múltipla , Patos/microbiologia , Enterotoxinas/genética , Animais , Proteínas de Bactérias/genética , Técnicas de Tipagem Bacteriana , Infecções por Clostridium/epidemiologia , Infecções por Clostridium/microbiologia , DNA Bacteriano/genética , Fezes/microbiologia , Índia/epidemiologia , Testes de Sensibilidade Microbiana , Tipagem Molecular , Reação em Cadeia da Polimerase , PrevalênciaRESUMO
Protein modification by arginylation regulates protein stability, function and interaction. The loss of arginylation disrupts a diverse set of fundamental cellular processes from proliferation to death. In the current study, role of arginylation in cell differentiation is investigated. Using in vitro preadipocyte differentiation model, it was observed that the inhibition or knockout (KO) of arginyltransferase 1 (ATE1) severely hindered differentiation of preadipocytes into mature adipocytes. Absence of arginylation inhibited expression of two key adipogenic transcription factors PPARγ and C/EBPα, and their downstream adipogenic genes (FABP4, GLUT4, PLN1). Arginylation did not affect the induction of C/EBPß and C/EBPδ, the up-stream regulators of PPARγ gene. However, absence of arginylation affected PPARγ protein expression, independent of its transcript level. The constitutive expression of PPARγ1 protein in Ate1 KO cells as well as ATE1 inhibitor treated wild type cells were dampened due to increased proteasome mediated degradation of PPARγ1 in the absence of arginylation in the cells. Taken together these observations suggested arginylation mediated transcriptional regulation of PPARγ and C/EBPα was downstream of C/EBPß and C/EBPδ, and that the arginylation mediated regulation of PPARγ protein expression may play a role in this process. The inhibition of arginylation in mature adipocytes also reduced expression of lipogenesis genes and decreased fat accumulation in differentiated adipocytes. Thus, the current study shows that arginylation is essential for preadipocyte differentiation and maturation which are thought to be key factors in the maintenance of adipose tissue homeostasis.