title: Integrative sequence and tissue expression profiling of chicken and mammalian aquaporins.
abstract: BACKGROUND
  Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyond transmembrane water transport. The availability of non-mammalian vertebrate animal models has the potential to provide insight into the emergence of diverse function in the aquaporins. The domesticated chicken (Gallus gallus) is the premier avian model for biological research; however, only a limited number of studies have compared chicken and mammalian aquaporins. The identification of aquaporins that share functional motifs or are expressed in the same tissues in human and chicken could allow the further functional analyses of homologous aquaporins in both species. We hypothesize that integrative analyses of protein sequences and body site expression of human, mouse, rat and chicken aquaporins has the potential to yield novel biological hypotheses about the unexpected cellular roles of aquaporins beyond transmembrane water transport.
  
  
  RESULTS
  A total of 76 aquaporin transcript models derived from 47 aquaporin genes were obtained for human, mouse, rat and chicken. Eleven body sites (brain, connective tissue, head, heart, liver, muscle, ovary, pancreas, small intestine, spleen and testis) were identified in which there is suggested expression of at least one mammalian and one chicken aquaporin. This study demonstrates that modern on-line analysis tools, a novel matrix integration technique, and the availability of the chicken genome for comparative genomics and expression analysis enables hypothesis generation in several important areas including: (i) alternative transcription and speciation effects on the conservation of functional motifs in vertebrate aquaporins; (ii) the emergence of basolateral targeting in mammalian species; (iii) the potential of the cysteine-rich AQP11 as a possible target in the pathophysiology of neurodegenerative disorders such as autism that involve Purkinje cells; and (iv) possible impairment of function of pancreas-expressed AQP12 during pancreatotropic necrosis in avian influenza virus infection.
  
  
  CONCLUSIONS
  The investigation of aquaporin function in chicken and mammalian species has the potential to accelerate the discovery of novel knowledge of aquaporins in both avian and mammalian species.
authors.affiliation: Center for Bioinformatics & Computational Biology, Department of Biology, Jackson State University, Jackson, MS 39217, USA. raphael.isokpehi@jsums.edu
authors.forename: Raphael D
authors.initials: RD
authors.lastname: Isokpehi
authors.forename: Rajendram V
authors.initials: RV
authors.lastname: Rajnarayanan
authors.forename: Cynthia D
authors.initials: CD
authors.lastname: Jeffries
authors.forename: Tolulola O
authors.initials: TO
authors.lastname: Oyeleye
authors.forename: Hari H P
authors.initials: HH
authors.lastname: Cohly
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020346:Aquaporins / Q000235:genetics*; D002645:Chickens / Q000235:genetics*; D055028:Comparative Genomic Hybridization; D020869:Gene Expression Profiling; D006801:Humans; D051379:Mice / Q000235:genetics; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000235:genetics; D051381:Rats / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D020346:Aquaporins; D020033:Protein Isoforms