ABSTRACT
The domestic dog has been given considerable attention as a system for investigating the genetics of human diseases. Population diversity and breed structure are unique features that make dogs particularly amenable to genetic studies. Dogs show distinguished features of breed-specific homogeneity, which is associated with striking interbreed heterogeneity. This review discusses the significance of studying the genetic maps, genome-wide association studies (GWAS), and usefulness of this species as an animal model. Most canine genetic disorders are similar to those of humans, including inherited, psychiatric, and genetic disorders. In addition to revealing new candidate genes, canine models allow access to experimental resources, such as cells, tissues, and even live animals, for research and intervention purposes.
Le chien domestique a reçu une attention considérable en tant que système d'investigation de la génétique des maladies humaines. La diversité de la population et la structure de la race sont des caractéristiques uniques qui rendent les chiens particulièrement propices aux études génétiques. Les chiens présentent des caractéristiques distinctes d'homogénéité spécifique à la race, qui est associée à une hétérogénéité interraciale frappante. Cette revue traite de l'importance de l'étude des cartes génétiques, des études d'association à l'échelle du génome (GWAS) et de l'utilité de cette espèce en tant que modèle animal. La plupart des troubles génétiques canins sont similaires à ceux des humains, y compris les troubles héréditaires, psychiatriques et génétiques. En plus de révéler de nouveaux gènes candidats, les modèles canins permettent d'accéder à des ressources expérimentales, telles que des cellules, des tissus et même des animaux vivants, à des fins de recherche et d'intervention.(Traduit par Docteur Serge Messier).
Subject(s)
Dog Diseases , Genome-Wide Association Study , Humans , Animals , Dogs , Genome-Wide Association Study/veterinary , Genome , Genomics , Breeding , Dog Diseases/geneticsABSTRACT
ABSTRACT Lectins are non-immunogenic carbohydrate-recognizing proteins that bind to glycoproteins, glycolipids, or polysaccharides with high affinity and exhibit remarkable ability to agglutinate erythrocytes and other cells. In the present study, ten Fusarium species previously not explored for lectins were screened for the presence of lectin activity. Mycelial extracts of F. fujikuroi, F. beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarnatum, and F. tabacinum manifested agglutination of rabbit erythrocytes. Neuraminidase treatment of rabbit erythrocytes increased lectin titers of F. nisikadoi and F. tabacinum extracts, whereas the protease treatment resulted in a significant decline in agglutination by most of the lectins. Results of hapten inhibition studies demonstrated unique carbohydrate specificity of Fusarium lectins toward O-acetyl sialic acids. Activity of the majority of Fusarium lectins exhibited binding affinity to D-ribose, L-fucose, D-glucose, L-arabinose, D-mannitol, D-galactosamine hydrochloride, D-galacturonic acid, N-acetyl-d-galactosamine, N-acetyl-neuraminic acid, 2-deoxy-D-ribose, fetuin, asialofetuin, and bovine submaxillary mucin. Melibiose and N-glycolyl neuraminic acid did not inhibit the activity of any of the Fusarium lectins. Mycelial extracts of F. begoniae, F. nisikadoi, F. anthophilum, and F. incarnatum interacted with most of the carbohydrates tested. F. fujikuroi and F. anthophilum extracts displayed strong interaction with starch. The expression of lectin activity as a function of culture age was investigated. Most species displayed lectin activity on the 7th day of cultivation, and it varied with progressing of culture age.
Subject(s)
Humans , Animals , Mycelium , Fusarium/metabolism , Fusarium/chemistry , Lectins/metabolism , Hemagglutination Tests , Erythrocytes/drug effects , Carbohydrate Metabolism , Fusarium/growth & development , Hemagglutination , Lectins/pharmacologyABSTRACT
Lectins are non-immunogenic carbohydrate-recognizing proteins that bind to glycoproteins, glycolipids, or polysaccharides with high affinity and exhibit remarkable ability to agglutinate erythrocytes and other cells. In the present study, ten Fusarium species previously not explored for lectins were screened for the presence of lectin activity. Mycelial extracts of F. fujikuroi, F. beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarnatum, and F. tabacinum manifested agglutination of rabbit erythrocytes. Neuraminidase treatment of rabbit erythrocytes increased lectin titers of F. nisikadoi and F. tabacinum extracts, whereas the protease treatment resulted in a significant decline in agglutination by most of the lectins. Results of hapten inhibition studies demonstrated unique carbohydrate specificity of Fusarium lectins toward O-acetyl sialic acids. Activity of the majority of Fusarium lectins exhibited binding affinity to d-ribose, l-fucose, d-glucose, l-arabinose, d-mannitol, d-galactosamine hydrochloride, d-galacturonic acid, N-acetyl-d-galactosamine, N-acetyl-neuraminic acid, 2-deoxy-d-ribose, fetuin, asialofetuin, and bovine submaxillary mucin. Melibiose and N-glycolyl neuraminic acid did not inhibit the activity of any of the Fusarium lectins. Mycelial extracts of F. begoniae, F. nisikadoi, F. anthophilum, and F. incarnatum interacted with most of the carbohydrates tested. F. fujikuroi and F. anthophilum extracts displayed strong interaction with starch. The expression of lectin activity as a function of culture age was investigated. Most species displayed lectin activity on the 7th day of cultivation, and it varied with progressing of culture age.
