Blood in the respiratory tract during slaughter with and without stunning in cattle

Bovine respiratory tracts were examined For blood following shechita without stunning, halal slaughter without stunning, and captive bolt stunning with sticking. In all three methods the cattle were in the upright (standing) position at the start of bleeding. Those that had not been stunned continued to breathe during the early part of bleeding whilst those that were stunned were not breathing. Nineteen percent of the shechita, 58% of the halal and 21% of the stunned plus stuck cattle had blood lining the inner aspect of the trachea, Thirty six percent, 69% and 31% had blood in the upper bronchi, respectively. Ten percent, 19% and 0% had fine bright red blood-tinged foam in the trachea, respectively. it was concluded that concerns about suffering from airway irritation by blood could apply in animals that are either not stunned before slaughter or do not lose Consciousness rapidly whilst blood is present in the respiratory tract. (c) 2008 Elsevier Ltd. All rights reserved

Isoform-selective interaction of the adaptor protein Tks5/FISH with Sos1 and dynamins

The adaptor protein Tks5/FISH (tyrosine kinase substrate 5/five SH3 domains, hereafter termed Tks5) is a crucial component of a protein network that controls the invasiveness of cancer cells and progression of Alzheimer's disease. Tks5 consists of an amino-terminal PX domain that is followed by five SH3 domains (SH3A-E), and two different splice variants are expressed. We identified son of sevenless-1 (Sos1) as a novel binding partner of Tks5 and found colocalization of Tks5 with Sos1 in human epithelial lung carcinoma (A549) cells and in podosomes of Src-transformed NIH 3T3 cells. We observe synergistic binding of SH3A and SH3B to Sos1 when peptide arrays are used, indicating that the tandem SH3A and SH3B domains of Tks5 can potentially bind in a superSH3 binding mode, as was described for the homologous protein p47phox. These results are further corroborated by pull-down assays and isothermal titration calorimetry showing that both intact SH3 domains are required for efficient binding to the entire proline-rich domain of Sos1. The presence of a basic insertion between the SH3A and SH3B domains in the long splice variant of Tks5 decreases the affinity to Sos1 isoforms about 10-fold as determined by analytical ultracentrifugation. Furthermore, it leads to an alteration in the recognition of binding motifs for the interaction with Sos1: While the insertion abrogates the interaction with the majority of peptides derived from the proline-rich domains of Sos1 and dynamin that are recognized by the short splice isoform, it enables binding to a different set of peptides including a sequence comprising the splice insertion in the long isoform of Sos1 (Sos1_2). In the absence of the basic insertion, Tks5 was found to bind a range of Sos1 and dynamin peptides including conventional proline-rich motifs and atypical recognition sequences. Hereby, the tandem SH3 domains in Tks5 employ two distinct types of binding modes: One class of peptides is recognized by single SH3 domains, whereas a second class of peptides requires the presence of both domains to bind synergistically. We conclude that the tandem SH3A and SH3B domains of Tks5 constitute a versatile module for the implementation of isoform-specific protein-protein interactions

Religious Slaughter in Europe

Halal and Shechita slaughter were assessed in 135 European abattoirs. Shechita is carried out without stunning in all abattoirs, while 65% of cattle abattoirs, 50% small ruminants and 50% poultry abattoirs use preslaughter stunning for Halal Slaughter