Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1995-11-6
pubmed:databankReference
pubmed:abstractText
The Drosophila ninaA gene encodes photoreceptor-specific cyclophilin thought to play a critical role in rhodopsin folding or transport during its synthesis or maturation in the most abundant subclass of photoreceptors. Cyclophilins comprise a highly conserved family of proteins which are the primary targets of the potent immunosuppressive drug, cyclosporin A (CsA), and which display peptidyl prolyl cis-trans-isomerase (PPIase) activity. In an attempt to identify mammalian cyclophilins with properties similar to the NinaA protein, a probe derived from the ninaA cDNA was used to screen bovine retina cDNA libraries. The screen identified two major alternatively spliced forms of cDNA that would encode proteins containing a region of high homology to other cyclophilins and that are expressed specifically in the retina. These proteins represent a new class of cyclophilins with novel structural features and greatly reduced PPIase and CsA binding activities in comparison to other known cyclophilins. Tissue in situ hybridization and immunolocalization of the proteins showed that the RNA and protein products are expressed in photoreceptors as well s other retinal neurons. However, among photoreceptors, the proteins are found predominantly in cones. Thus, mammalian retinas do contain cyclophilins that are retina-specifically and photoreceptor class-preferentially expressed. The results suggest that, in cones, the main function of these proteins is, like the NinaA protein, to facilitate proper folding or intracellular transport of opsins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23179-88
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7559465-Alternative Splicing, pubmed-meshheading:7559465-Amino Acid Isomerases, pubmed-meshheading:7559465-Amino Acid Sequence, pubmed-meshheading:7559465-Animals, pubmed-meshheading:7559465-Base Sequence, pubmed-meshheading:7559465-Blotting, Southern, pubmed-meshheading:7559465-Carrier Proteins, pubmed-meshheading:7559465-Cattle, pubmed-meshheading:7559465-Chaperonins, pubmed-meshheading:7559465-Cloning, Molecular, pubmed-meshheading:7559465-Cyclosporins, pubmed-meshheading:7559465-DNA, Complementary, pubmed-meshheading:7559465-Drosophila, pubmed-meshheading:7559465-Drosophila Proteins, pubmed-meshheading:7559465-Gene Expression, pubmed-meshheading:7559465-Gene Library, pubmed-meshheading:7559465-Genes, Insect, pubmed-meshheading:7559465-Humans, pubmed-meshheading:7559465-In Situ Hybridization, pubmed-meshheading:7559465-Insect Hormones, pubmed-meshheading:7559465-Kinetics, pubmed-meshheading:7559465-Membrane Proteins, pubmed-meshheading:7559465-Molecular Chaperones, pubmed-meshheading:7559465-Molecular Sequence Data, pubmed-meshheading:7559465-Organ Specificity, pubmed-meshheading:7559465-Peptidylprolyl Isomerase, pubmed-meshheading:7559465-Retina, pubmed-meshheading:7559465-Retinal Cone Photoreceptor Cells, pubmed-meshheading:7559465-Rod Cell Outer Segment, pubmed-meshheading:7559465-Sequence Homology, Amino Acid
pubmed:year
1995
pubmed:articleTitle
Retina-specifically expressed novel subtypes of bovine cyclophilin.
pubmed:affiliation
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't