| pubmed-article:16449562 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16449562 | lifeskim:mentions | umls-concept:C0014906 | lld:lifeskim |
| pubmed-article:16449562 | lifeskim:mentions | umls-concept:C2262326 | lld:lifeskim |
| pubmed-article:16449562 | lifeskim:mentions | umls-concept:C0037378 | lld:lifeskim |
| pubmed-article:16449562 | lifeskim:mentions | umls-concept:C1552507 | lld:lifeskim |
| pubmed-article:16449562 | lifeskim:mentions | umls-concept:C1487128 | lld:lifeskim |
| pubmed-article:16449562 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:16449562 | pubmed:issue | Pt 4 | lld:pubmed |
| pubmed-article:16449562 | pubmed:dateCreated | 2006-2-1 | lld:pubmed |
| pubmed-article:16449562 | pubmed:abstractText | Entry into the hypometabolic state of estivation requires a coordinated suppression of the rate of cellular ATP turnover, including both ATP-generating and ATP-consuming reactions. As one of the largest consumers of cellular ATP, the plasma membrane Na+/K+-ATPase is a potentially key target for regulation during estivation. Na+/K+-ATPase was investigated in foot muscle and hepatopancreas of the land snail Otala lactea, comparing active and estivating states. In both tissues enzyme properties changed significantly during estivation: maximal activity was reduced by about one-third, affinity for Mg.ATP was reduced (Km was 40% higher), and activation energy (derived from Arrhenius plots) was increased by approximately 45%. Foot muscle Na+/K+-ATPase from estivated snails also showed an 80% increase in Km Na+ and a 60% increase in Ka Mg2+ as compared with active snails, whereas hepatopancreas Na+/K+-ATPase showed a 70% increase in I50 K+ during estivation. Western blotting with antibodies recognizing the alpha subunit of Na+/K+-ATPase showed no change in the amount of enzyme protein during estivation. Instead, the estivation-responsive change in Na+/K+-ATPase activity was linked to posttranslational modification. In vitro incubations manipulating endogenous kinase and phosphatase activities indicated that Na+/K+-ATPase from estivating snails was a high phosphate, low activity form, whereas dephosphorylation returned the enzyme to a high activity state characteristic of active snails. Treatment with protein kinases A, C or G could all mediate changes in enzyme properties in vitro that mimicked the effect of estivation, whereas treatments with protein phosphatase 1 or 2A had the opposite effect. Reversible phosphorylation control of Na+/K+-ATPase can provide the means of coordinating ATP use by this ion pump with the rates of ATP generation by catabolic pathways in estivating snails. | lld:pubmed |
| pubmed-article:16449562 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16449562 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16449562 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16449562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16449562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16449562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16449562 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16449562 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16449562 | pubmed:issn | 0022-0949 | lld:pubmed |
| pubmed-article:16449562 | pubmed:author | pubmed-author:StoreyKenneth... | lld:pubmed |
| pubmed-article:16449562 | pubmed:author | pubmed-author:RamnananChris... | lld:pubmed |
| pubmed-article:16449562 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16449562 | pubmed:volume | 209 | lld:pubmed |
| pubmed-article:16449562 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16449562 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16449562 | pubmed:pagination | 677-88 | lld:pubmed |
| pubmed-article:16449562 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:meshHeading | pubmed-meshheading:16449562... | lld:pubmed |
| pubmed-article:16449562 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16449562 | pubmed:articleTitle | Suppression of Na+/K+-ATPase activity during estivation in the land snail Otala lactea. | lld:pubmed |
| pubmed-article:16449562 | pubmed:affiliation | Institute of Biochemistry, College of Natural Sciences, Carleton University, 1125 Colonel By Drive, Ottawa, Ontario, Canada K1S 5B6. | lld:pubmed |
| pubmed-article:16449562 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16449562 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16449562 | lld:pubmed |
