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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0007452,
umls-concept:C0009015,
umls-concept:C0015392,
umls-concept:C0017262,
umls-concept:C0017822,
umls-concept:C0024660,
umls-concept:C0032105,
umls-concept:C0178539,
umls-concept:C0185117,
umls-concept:C0376315,
umls-concept:C0459736,
umls-concept:C1299003,
umls-concept:C2911684
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pubmed:issue |
2
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pubmed:dateCreated |
1994-1-26
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pubmed:databankReference | |
pubmed:abstractText |
In the anterior segment of the mammalian eye, the ocular ciliary epithelium produces the aqueous humor, a fluid that nourishes and protects the avascular tissues from oxidative stress. This report details the results of a study of molecular cloning, sequencing, and expression of plasma glutathione peroxidase (GPx-P) from the bovine ocular ciliary epithelium. The bovine GPx-P cDNA contains an open reading frame of 226 amino acids with a calculated molecular weight of 24,860. The corresponding amino acid sequence showed an overall identity of 88% with the human GPx-P, 88.5% with the rat GPx-P, and 46.4% with the cellular bovine glutathione peroxidase (GPx-1). The levels of GPx-P and GPx-1 transcripts in ocular tissues were analyzed and the ciliary epithelium was found to express the highest levels of GPx-P transcripts in human and bovine eyes, whereas the cornea of calf eyes expressed the highest levels of GPx-1 transcripts. Surprisingly, the lens, on which oxidants have profound effects leading to cataract formation, expressed the lowest levels of GPx-P and GPx-1 transcripts in human donor eyes. These results provide new evidence of differential gene expression of the GPx-P and GPx-1 forms in the mammalian eye and stresses the functional role of the ocular ciliary epithelium in protecting the anterior segment of the eye from oxidative damage.
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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 |
Aug
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
114
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
284-91
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:8262911-Amino Acid Sequence,
pubmed-meshheading:8262911-Animals,
pubmed-meshheading:8262911-Base Sequence,
pubmed-meshheading:8262911-Cattle,
pubmed-meshheading:8262911-Ciliary Body,
pubmed-meshheading:8262911-Cloning, Molecular,
pubmed-meshheading:8262911-DNA, Complementary,
pubmed-meshheading:8262911-Epithelium,
pubmed-meshheading:8262911-Eye,
pubmed-meshheading:8262911-Gene Expression,
pubmed-meshheading:8262911-Glutathione Peroxidase,
pubmed-meshheading:8262911-Humans,
pubmed-meshheading:8262911-Molecular Sequence Data,
pubmed-meshheading:8262911-Polymerase Chain Reaction,
pubmed-meshheading:8262911-Restriction Mapping,
pubmed-meshheading:8262911-Selenium,
pubmed-meshheading:8262911-Sequence Homology, Amino Acid,
pubmed-meshheading:8262911-Sequence Homology, Nucleic Acid
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pubmed:year |
1993
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pubmed:articleTitle |
Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular ciliary epithelium: expression of the plasma and cellular forms within the mammalian eye.
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pubmed:affiliation |
Department of Ophthalmology and Visual Science, 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.,
Research Support, Non-U.S. Gov't
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