Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1989-10-25
pubmed:databankReference
pubmed:abstractText
Cells generally respond to long-term hyperosmotic stress by accumulating nonperturbing organic osmolytes. Unlike bacteria, in which molecular mechanisms involved in the increased accumulation of osmolytes have been identified, those in multicellular organisms are virtually unknown. In mammals, during antidiuresis, cells of the renal inner medulla are exposed to high and variable extracellular NaCl. Under these conditions, the cells contain a high level of sorbitol and other osmolytes which help balance the high extracellular osmolality. PAP-HT25 is a continuous line of cells derived from rabbit renal inner medulla. When medium osmolality is increased by raising the NaCl concentration, these cells accumulate sorbitol. The sorbitol is synthesized from glucose in a reaction catalyzed by aldose reductase. When the medium is made hyperosmotic, aldose reductase activity increases because of a larger increase in the amount of enzyme. This increase is produced by the accelerated rate of synthesis of aldose reductase protein. The purpose of the present studies was to examine the mechanism of this increase in aldose reductase protein by measuring the relative abundance of aldose reductase mRNA. A cDNA clone coding for rabbit kidney aldose reductase was isolated. Antisense RNA probes transcribed from this clone hybridized specifically with a 1.5-1.6 kilobase mRNA in Northern blots. Cells grown chronically in hyperosmotic medium had a relative abundance of this specific mRNA which was six times that of cells grown in isoosmotic medium. When cells grown in isoosmotic medium were switched to hyperosmotic medium, the level of aldose reductase mRNA peaked (18-fold) at 18-24 h. The induction of aldose reductase mRNA by osmotic stress was reversible. Our finding of increased abundance of a specific mRNA in direct response to hyperosmotic stress represents the first report of such an effect in animals.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16815-21
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2506183-Aldehyde Reductase, pubmed-meshheading:2506183-Amino Acid Sequence, pubmed-meshheading:2506183-Animals, pubmed-meshheading:2506183-Base Sequence, pubmed-meshheading:2506183-Blotting, Northern, pubmed-meshheading:2506183-Cell Line, pubmed-meshheading:2506183-Cloning, Molecular, pubmed-meshheading:2506183-DNA, pubmed-meshheading:2506183-Gene Expression Regulation, pubmed-meshheading:2506183-Genes, pubmed-meshheading:2506183-Kidney Medulla, pubmed-meshheading:2506183-Kinetics, pubmed-meshheading:2506183-Molecular Sequence Data, pubmed-meshheading:2506183-Osmolar Concentration, pubmed-meshheading:2506183-RNA, Messenger, pubmed-meshheading:2506183-Rabbits, pubmed-meshheading:2506183-Saline Solution, Hypertonic, pubmed-meshheading:2506183-Sodium Chloride, pubmed-meshheading:2506183-Sugar Alcohol Dehydrogenases, pubmed-meshheading:2506183-Transcription, Genetic
pubmed:year
1989
pubmed:articleTitle
Molecular cloning of cDNA coding for kidney aldose reductase. Regulation of specific mRNA accumulation by NaCl-mediated osmotic stress.
pubmed:affiliation
Laboratory of Kidney and Electrolyte Metabolism, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.