Dataset Information

Aquaporins in Saccharomyces: Characterization of a second functional water channel protein.

ABSTRACT: The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2. Aqy1p has been shown to be a functional aquaporin in some strains, such as Sigma1278b. AQY2 is disrupted by a stop codon in most strains; however, Sigma1278b has an intact ORF. Because Sigma1278b Aqy2p has an intracellular localization in Xenopus oocytes and in yeast, other strains of yeast were examined. Aqy2p from Saccharomyces chevalieri has a single amino acid in the third transmembrane domain (Ser-141) that differs from Sigma1278b Aqy2p (Pro-141). S. chevalieri Aqy2p is a functional water channel in oocytes and traffics to the plasma membrane of yeast. The Sigma1278b parental strain, the aqy1-aqy2 double null yeast, and null yeast expressing S. chevalieri Aqy2p were examined under various conditions. Comparison of these strains revealed that the aquaporin null cells were more aggregated and their surface was more hydrophobic. As a result, the aquaporin null cells were more flocculent and more efficient at haploid invasive growth. Despite its primary intracellular localization, Sigma1278b Aqy2p plays a role in yeast similar to Aqy1p and S. chevalieri Aqy2p. In addition, Aqy1p and Aqy2p can affect cell surface properties and may provide an advantage by dispersing the cells during starvation or during sexual reproduction.

SUBMITTER: Carbrey JM

PROVIDER: S-EPMC14698 | biostudies-literature | 2001 Jan

REPOSITORIES: biostudies-literature

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Aquaporins in Saccharomyces: Characterization of a second functional water channel protein.

Carbrey J M JM Bonhivers M M Boeke J D JD Agre P P

Proceedings of the National Academy of Sciences of the United States of America 20010101 3

The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2. Aqy1p has been shown to be a functional aquaporin in some strains, such as Sigma1278b. AQY2 is disrupted by a stop codon in most strains; however, Sigma1278b has an intact ORF. Because Sigma1278b Aqy2p has an intracellular localization in Xenopus oocytes and in yeast, other strains of yeast were examined. Aqy2p from Saccharomyces chevalieri has a single amino acid in the third transmembrane ...[more]

PMID: 11158584

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Project description:The study was to determine whether the expression of genes involved in intestinal water and ion transport would be affected by enterotoxigenic (ETEC) K88 both in vitro and in vivo. First, 36 male piglets (4 d old) were randomly allotted to either the control or the ETEC K88 group. Each group had 6 replicates with 3 piglets per replicate. All piglets were fed with the same diets for 17 d. On d 15, piglets in the ETEC K88 group were challenged with ETEC K88 (serotype O149:K91:K88ac) at 1 × 10 cfu per pig, whereas those in the control group received the same volume of sterile PBS. After being challenged with ETEC K88 for 72 h (d 18), 1 piglet from each replicate was selected for slaughter to collect samples from the jejunum, ileum, and colon. The mRNA expression and protein abundance of cystic fibrosis transmembrane conductance regulator (CFTR) in the ileum and colon were increased compared with that in the control group ( < 0.05). Furthermore, the mRNA expression of () in the ileum and colon was increased by ETEC K88 challenge ( < 0.05), whereas in the jejunum, both its mRNA and protein expression were increased by ETEC K88 treatment ( < 0.05). Additionally, an established porcine intestinal epithelial cell line (IPEC-J2) was used to investigate the effect and possible mechanism of ETEC K88 on expression of water channel aquaporins (AQP) and ion transporters. Cells (1.17 × 10 per well) were grown in 6-well plates and treated with ETEC K88 at a multiplicity of infection of 50:1 for 3 h. The mRNA expression of , , and () in IPEC-J2 cells was reduced after ETEC K88 treatment ( < 0.05). Further analyses using western blotting also demonstrated that ETEC K88 decreased the protein expression of AQP3, AQP9, and AQP11 in IPEC-J2 cells ( < 0.05). Moreover, the phosphorylation levels of protein kinase A (PKA) and cyclic adenosine monophosphate (cAMP)-response element binding protein (CREB) were decreased by ETEC K88 challenge ( < 0.05). The results indicate that ETEC K88 challenge induced differential expression of intestinal ion transporters and AQP in young piglets, probably by regulation of the cAMP-PKA signaling pathway. This study might provide new insights about the importance of fluid homeostasis in control of ETEC-induced diarrhea in young piglets.

Dataset Information

Aquaporins in Saccharomyces: Characterization of a second functional water channel protein.

Publications

Aquaporins in Saccharomyces: Characterization of a second functional water channel protein.

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