| Autor: |
Lorenz, Bettina, Migliaccio, Carmela, Lichtner, Peter, Meyer, Carsten, Strom, Tim M, DUrso, Michele, Becker, Jörg, Ciccodicola, Alfredo, Meitinger, Thomas |
| Předmět: |
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| Zdroj: |
European Journal of Human Genetics; May98, Vol. 6 Issue 3, p283, 8p |
| Abstrakt: |
Rod-specific cGMP phosphodiesterase (PDE) is a key enzyme of the phototransduction cascade, and mutations in its catalytic subunits have been associated with retinal degenerative diseases. The bovine δ-subunit solubilises the normally membrane-bound PDE and is the only subunit expressed in extraocular tissues. We isolated the human and mouse orthologs, and found 78% identity at the DNA level and 98% identity at the protein level. The Caenorhabditis elegans homolog shows 69% identity at the protein level. The human PDED gene consisted of 5 exons spanning at least 30 kb of genomic DNA. Northern blot analysis showed a 1.3 kb transcript in human retina, heart, brain, placenta, liver, and skeletal muscle. Fluorescence in situ hybridisation (FISH) and radiation hybrid mapping localised the human PDED gene to chromosome 2q37. A preliminary screen of all 5 exons in 20 unrelated patients with autosomal recessive retinitis pigmentosa revealed no PDED mutations. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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