Search

Sudden death syndrome (SDS) is a stress-related disease in broilers with no diagnostic clinical or necropsy findings. SDS is associated with ventricular tachycardia (VT) and ventricular fibrillation (VF); however, its pathogenesis is not precisely described at the molecular level. Dysfunction of ryanodine receptor 2 (RYR2), that controls rapid release of Ca2+ from the sarcoplasmic reticulum (SR) into the cytosol during muscle contraction, has been associated with VT and sudden cardiac death (SCD) in human patients with structurally normal heart, but there is no report describing abnormalities in RYR2 in diseased broilers. In order to advance our knowledge on the molecular mechanisms predisposing broilers to fatal arrhythmia, the present study was conducted to determine the occurrence of possible mutations and changes in the expression level of the chicken RYR2 gene (chRYR2) in broilers that died from SDS. An increase in mRNA expression level and nine novel point mutations in chRYR2 were found in relation to SDS. In conclusion, susceptibility to lethal cardiac arrhythmia in SDS may be associated with specific changes in intracellular Ca2+ cycling components such as RYR2 due to mutation and dysregulation. Finding the probable association of SDS with gene defects can be applied to select for chickens with lower susceptibility to SDS and decrease the poultry industry losses due to SDS mortality. RESEARCH HIGHLIGHTS Investigation of the occurrence of possible mutations and changes in the expression level of chicken RYR2 gene (chRYR2) in broilers that died from SDS. Increase in the mRNA expression level of chRYR2 in relation to SDS. Nine novel point mutations in chRYR2 of broilers that died from SDS. Possible connection between susceptibility to lethal cardiac arrhythmia in SDS and changes in intracellular Ca2+ cycling machinery, such as RYR2, due to mutation and dysregulation. [ABSTRACT FROM AUTHOR]

Sudden death syndrome (SDS) in broilers is a cardiac disease associated with ventricular tachycardia (VT) and ventricular fibrillation (VF); however, its pathogenesis at the molecular level is not precisely determined.Downregulation and mutations of calsequestrin 2 (CASQ2), a major intracellular Ca2+ buffer, have been associated with VT and sudden cardiac death (SCD) in humans but in chickens there is no report describing CASQ2 abnormalities in cardiac diseases.In order to better understand the molecular mechanisms predisposing the myocardium to fatal arrhythmia in broilers, the mRNA expression level of chicken CASQ2 gene (chCASQ2) in the left ventricle of dead broilers with SDS was determined and compared to healthy broilers using quantitative real-time PCR (qPCR). To determine the probable mutations in chCASQ2, PCR and direct sequencing were also done.Results showed a reduction in chCASQ2 expression in broilers dead by SDS. Three novel mutations (K289R, P308S, D310H) which are absent in healthy broilers were observed in chCASQ2.It is concluded that susceptibility to fatal cardiac arrhythmia in SDS may be associated with changes in intracellular Ca2+ balance due to mutation and downregulation of chCASQ2. [ABSTRACT FROM PUBLISHER]

1. The purpose of this investigation was to determine the activity, and compare the pattern of distribution, of rhodanese (thiosulphate: cyanide sulphurtransferase, EC. 2.8.1.1) in different tissues of male and female ostriches. 2. Tissue samples from male and female Blue Neck ostriches were assayed for rhodanese activity by the determination of thiocyanate formed by the action of the enzyme on thiosulphate and KCN. 3. Rhodanese was present in all tissues, and the highest activity was observed in the kidney and liver. Other tissues which contained significant activities of rhodanese were the duodenum, pancreas, heart, caecum and rectum. 4. Unlike other birds, the proventiculus does not appear to have an important role in cyanide detoxification in ostrich and, like mammals, the kidney and liver perform this function. 5. The results suggest that the main organs harbouring high rhodanese activity in the ostrich are associated with sites likely to be required in rhodanese mediated cyanide detoxification. [ABSTRACT FROM PUBLISHER]