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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1992-8-7
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pubmed:databankReference | |
pubmed:abstractText |
We have used molecular and biochemical techniques to analyze Na,K-ATPase from a simple metazoan, Hydra vulgaris. First we isolated and characterized cDNA clones encoding the Na,K-ATPase alpha subunit from a Hydra lambda gt11 cDNA library. The open reading frame predicts a protein of 1031 amino acids that bears a high degree of primary sequence and secondary structure similarity to mammalian, avian, and arthropod alpha subunits. The predicted Hydra alpha subunit contains charged residues at the termini of the H1-H2 extracellular domain, suggesting that the Hydra alpha subunit may be resistant to cardiac glycoside inhibition. Biochemical analysis of partially purified Hydra Na,K-ATPase reveals both high- and low-affinity components of ouabain-inhibitable ATPase activity. Our results suggest that the evolutionary ancestor of all metazoans possessed a Na,K-ATPase alpha subunit that was highly conserved with respect to its vertebrate counterparts. Further, expression of a ouabain-resistant Na,K-ATPase activity in Hydra suggests that cardiac glycoside resistance arose randomly during evolution of the Na,K-ATPase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1043-4674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
339-48
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1320398-Amino Acid Sequence,
pubmed-meshheading:1320398-Animals,
pubmed-meshheading:1320398-Base Sequence,
pubmed-meshheading:1320398-Biological Evolution,
pubmed-meshheading:1320398-Cloning, Molecular,
pubmed-meshheading:1320398-DNA,
pubmed-meshheading:1320398-Humans,
pubmed-meshheading:1320398-Hydra,
pubmed-meshheading:1320398-Molecular Sequence Data,
pubmed-meshheading:1320398-Ouabain,
pubmed-meshheading:1320398-Protein Conformation,
pubmed-meshheading:1320398-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1320398-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:1320398-Species Specificity
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pubmed:year |
1992
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pubmed:articleTitle |
Molecular cloning and characterization of Na,K-ATPase from Hydra vulgaris: implications for enzyme evolution and ouabain sensitivity.
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pubmed:affiliation |
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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