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Cytological, histological, and bacteriologic examinations were conducted of the contents of the large intestine in dogs with carcinoma of the rectosigmoid. Pyocin was isolated from a total of 42 (79.0 per cent) of 52 lesions. In cases of penetrating tumors (72.7 per cent), the lesions were characterized by marked inflammation of the mucosa, severe acute enterocolitis, signs of tumor invagination, and pronounced malignant infiltration of the wall. In cases of polypoid tumors (55.6 per cent), chronic enterocolitis accompanied by focal chronic inflammation of the mucosa, the presence of tumor capillaries and marked fibrosis of the mucosa, which was less pronounced than that in penetrating lesions, was observed. Invaginated carcinoma in the rectosigmoid is likely to develop only if chronic inflammation of the mucosa has started. In this case, the carcinoma grows along the mucosal surface, thus increasing the risk of perforation.Nick Kapusta
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The cellular prion protein PrP(C) is a transmembrane glycoprotein. Its main fold, the beta-sandwich, consists of two outer strands, each comprising six anti-parallel beta-strands, and two inner strands, comprising three anti-parallel beta-strands. Here we investigated the folding and aggregation potential of the beta-sandwich fold using five different algorithms. Our results indicate that the beta-sandwich is intrinsically disordered, and that the propensity to misfold is higher than that of the beta-barrel and alpha-helical folds. Furthermore, we showed that this folding instability is primarily due to a combination of aspartic acid and glutamic acid content in the inner strands. This led us to propose the beta(DE)triplet as a protein-misfolding signature. We also found that this instability is enhanced by N-linked glycosylation, providing a possible explanation for its functional role in PrP(C). These observations allow us to propose that amyloidogenicity in proteins with the beta-sandwich fold is achieved by the cooperative formation of beta(DE) triplets, followed by beta-strand rearrangements. Finally, by ranking the amino acid sequences based on their propensity to misfold, we demonstrate the potential utility of this approach in the prediction of protein folding.Ideal to dress up a 5th of 7th birthday party.
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