Linked Life Data

15936174

Source:http://linkedlifedata.com/resource/pubmed/id/15936174

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2005-9-12
pubmed:abstractText
Genetic manipulation of diphosphoinositol polyphosphate synthesis impacts many biological processes (reviewed in S.B. Shears, Biochem. J. 377, 2004, 265-280). These observations lacked a cell-signalling context, until the recent discovery that bis-diphosphoinositol tetrakisphosphate ([PP]2-InsP4 or "InsP8") accumulates rapidly in mammalian cells in response to hyperosmotic stress (X. Pesesse, K. Choi, T. Zhang, and S. B. Shears J. Biol. Chem. 279, 2004, 43378-43381). We now investigate how widely applicable is this new stress-response. [PP]2-InsP4 did not respond to mechanical strain or oxidative stress in mammalian cells. Furthermore, despite tight conservation of many molecular stress responses across the phylogenetic spectrum, we show that cellular [PP]2-InsP4 levels do not respond significantly to osmotic imbalance, heat stress and salt toxicity in Saccharomyces cerevisiae. In contrast, we show that [PP]2-InsP4 is a novel sensor of mild thermal stress in mammalian cells: [PP]2-InsP4 levels increased 3-4 fold when cells were cooled from 37 to 33 degrees C, or heated to 42 degrees C. Increases in [PP]2-InsP4 levels following heat-shock were evident <5 min, and reversible (t(1/2)=7 min) once cells were returned to 37 degrees C. These responses were blocked by pharmacological inhibition of the ERK/MEK pathway. Additional control processes may lie upstream of [PP]2-InsP4 synthesis, which was synergistically activated when heat stress and osmotic stress were combined. Our data add to the repertoire of signaling responses following thermal challenges, a topic of current interest for its possible therapeutic value.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1533-41
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15936174-Acid Anhydride Hydrolases, pubmed-meshheading:15936174-Animals, pubmed-meshheading:15936174-Cell Line, pubmed-meshheading:15936174-Cricetinae, pubmed-meshheading:15936174-Heat-Shock Response, pubmed-meshheading:15936174-Humans, pubmed-meshheading:15936174-Keratinocytes, pubmed-meshheading:15936174-MAP Kinase Kinase Kinases, pubmed-meshheading:15936174-MAP Kinase Signaling System, pubmed-meshheading:15936174-Myocytes, Smooth Muscle, pubmed-meshheading:15936174-Osmotic Pressure, pubmed-meshheading:15936174-Oxidative Stress, pubmed-meshheading:15936174-Phosphotransferases (Phosphate Group Acceptor), pubmed-meshheading:15936174-Saccharomyces cerevisiae, pubmed-meshheading:15936174-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15936174-Signal Transduction, pubmed-meshheading:15936174-Stress, Mechanical, pubmed-meshheading:15936174-p38 Mitogen-Activated Protein Kinases
pubmed:year
2005
pubmed:articleTitle
Signal transduction during environmental stress: InsP8 operates within highly restricted contexts.
pubmed:affiliation
Inositide Signaling Group, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, PO Box 12233, NC 27709, USA.
pubmed:publicationType
Journal Article, Comparative Study