Source:http://linkedlifedata.com/resource/pubmed/id/10358094
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0007452,
umls-concept:C0010031,
umls-concept:C0010422,
umls-concept:C0017262,
umls-concept:C0020792,
umls-concept:C0022157,
umls-concept:C0027303,
umls-concept:C0221908,
umls-concept:C0459875,
umls-concept:C0851827,
umls-concept:C1171362,
umls-concept:C1383501,
umls-concept:C1515670,
umls-concept:C1701901
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| pubmed:issue |
24
|
| pubmed:dateCreated |
1999-7-6
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| pubmed:databankReference | |
| pubmed:abstractText |
Recently, metabolic enzymes have been observed in both the lens and corneal epithelium at levels greatly exceeding what is necessary for normal metabolic functions. These proteins have been termed taxon-specific crystallins and are thought to play a role in maintaining tissue transparency. We report here that cytosolic NADP+-dependent isocitrate dehydrogenase (ICDH) represents a new corneal crystallin. Using suppression subtractive hybridization, we identified a gene (with a deduced amino acid sequence that showed 94% identity to rat cytosolic NADP+-dependent ICDH) that is preferentially expressed in bovine corneal epithelium. Northern blots established that its mRNA level in the corneal epithelium was 31-, 39-, 133-, 230-, and 929-fold more than in the liver, bladder epithelium, stomach epithelium, brain, and heart, respectively. This mRNA was detected primarily in corneal epithelial basal cells by in situ hybridization. SDS-polyacrylamide gel electrophoresis, two-dimensional gel analysis, and Western blotting showed that this protein was overexpressed in the corneal epithelium, constituting approximately 13% of the total soluble bovine corneal epithelial proteins. Enzyme assays showed a corresponding overabundance of this protein in bovine corneal epithelium. Taken together, these data indicate that bovine cytosolic ICDH fulfills the criteria for a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency.
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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 |
Jun
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
11
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| pubmed:volume |
274
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
17334-41
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10358094-Amino Acid Sequence,
pubmed-meshheading:10358094-Animals,
pubmed-meshheading:10358094-Base Sequence,
pubmed-meshheading:10358094-Cattle,
pubmed-meshheading:10358094-Cell Compartmentation,
pubmed-meshheading:10358094-Crystallins,
pubmed-meshheading:10358094-Cytosol,
pubmed-meshheading:10358094-DNA, Complementary,
pubmed-meshheading:10358094-Epithelium, Corneal,
pubmed-meshheading:10358094-Gene Library,
pubmed-meshheading:10358094-Humans,
pubmed-meshheading:10358094-In Situ Hybridization,
pubmed-meshheading:10358094-Isocitrate Dehydrogenase,
pubmed-meshheading:10358094-Mice,
pubmed-meshheading:10358094-Molecular Sequence Data,
pubmed-meshheading:10358094-Rabbits,
pubmed-meshheading:10358094-Rats,
pubmed-meshheading:10358094-Sequence Analysis, DNA,
pubmed-meshheading:10358094-Sequence Homology, Amino Acid,
pubmed-meshheading:10358094-Species Specificity,
pubmed-meshheading:10358094-Tissue Distribution
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| pubmed:year |
1999
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| pubmed:articleTitle |
Identification of a cytosolic NADP+-dependent isocitrate dehydrogenase that is preferentially expressed in bovine corneal epithelium. A corneal epithelial crystallin.
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| pubmed:affiliation |
Department of Dermatology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|