Animal & Avian Sciences

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    Characterization of Copy Number Variation’s Potential Role in Marek’s Disease
    (MDPI, 2017-05-09) Xu, Lingyang; He, Yanghua; Ding, Yi; Sun, Guirong; Carrillo, Jose Adrian; Li, Yaokun; Ghaly, Mona M.; Ma, Li; Zhang, Huanmin; Liu, George E.; Song, Jiuzhou
    Marek’s Disease (MD) is a highly contagious pathogenic and oncogenic disease primarily affecting chickens. Chicken Lines 63 and 72, as well as their recombinant congenic strains (RCS) with varied susceptibility to MD, are ideal models to study the complex mechanisms of genetic resistance to MD. In this study, we investigated copy number variation (CNV) in these inbred chicken lines using the Affymetrix Axiom HD 600 K SNP genotyping array. We detected 393 CNV segments across all ten chicken lines, of which 12 CNVs were specifically identified in Line 72. We then assessed genetic structure based on CNV and observed markedly different patterns. Finally, we validated two deletion events in Line 72 and correlated them with genes expression using qPCR and RNA-seq, respectively. Our combined results indicated that these two CNV deletions were likely to contribute to MD susceptibility.
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    Characterization of Chicken CAT-2 Isoforms
    (2007-08-20) Kirsch, Sandra B; Hamza, Iqbal; Humphrey, Brooke D; Animal Sciences; Digital Repository at the University of Maryland; University of Maryland (College Park, Md.)
    Lysine and arginine transport is primarily mediated by cationic amino acid transporters (CATs) in cells. The chicken CAT-2 (cCAT-2) transcript is alternatively spliced to three isoforms. Transcriptional and cellular localization experiments were utilized to study their regulation. The mRNA abundance of cCAT-2 isoforms was estimated in body tissues, and although differentially expressed, all tissues expressed each cCAT-2 isoform gene, indicating that alternative splicing was not tissue-specific. Both cCAT-2A and cCAT-2B proteins localized to the plasma membrane and cCAT-2C protein was retained in the cytosol. Chicken CAT-2A functions as a low affinity transporter with specificity for lysine and arginine. Chicken CAT-2B and cCAT-2C transporter functions were not detectable. Our data indicates that CAT-2 transporters are conserved in non-mammalian vertebrates, but cCAT-2 isoforms differ in their tissue distribution and transporter function from previously characterized CAT-2 transporters. These results also indicate a mechanism by which additional dietary lysine and arginine contribute to increased protein accretion in muscle tissue.