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pubmed-article:2161380pubmed:abstractTextCyclic GMP-phosphodiesterase (cGMP-PDE) plays a key role in the normal functioning of retinal rod photoreceptor cells. The enzyme is composed of alpha- and beta-catalytic subunits which are inhibited by two identical gamma-subunits. A cDNA encoding the gamma-subunits (PDE gamma) from human retina has been cloned and sequenced. The 1012-bp cDNA has a coding region of 261 bp which is highly homologous to those of the PDE gamma cDNAs from bovine and mouse retinas. Comparison of the deduced amino acid sequences of the proteins from the three species indicates that PDE gamma has been very well conserved through evolution. The mRNA encoded by the cloned cDNA is 1.0 kb long, is similar in size to the corresponding mRNAs from mouse, dog and bovine retinas and is not detected in ground squirrel retina. The PDEG gene has been assigned to human chromosome 17, probably in the region q21.1.lld:pubmed
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pubmed-article:2161380pubmed:articleTitleIsolation and characterization of cDNA encoding the gamma-subunit of cGMP phosphodiesterase in human retina.lld:pubmed
pubmed-article:2161380pubmed:affiliationJules Stein Eye Institute, UCLA School of Medicine 90024.lld:pubmed
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