|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
8
|
|
pubmed:dateCreated |
2000-3-30
|
|
pubmed:abstractText |
Peripherin/Rds is a tetraspanning membrane protein that has been implicated in photoreceptor outer segment morphogenesis and inherited retinal degenerative diseases. Together with the structurally related protein, Rom-1, it forms a complex along the rims of rod and cone disc membranes. We have compared the oligomeric structure of these proteins from nonreduced and dithiothreitol reduced membranes by velocity sedimentation, SDS-gel electrophoresis, immunoaffinity chromatography, and chemical cross-linking. Under reducing conditions peripherin/Rds and Rom-1 existed as homomeric and heteromeric core complexes devoid of intermolecular disulfide bonds. Under nonreducing conditions core complexes associated through intermolecular disulfide bonds to form oligomers. One intermediate-size oligomer contained monomers and disulfide-linked dimers of peripherin/Rds and Rom-1, while larger oligomers consisted only of disulfide-linked peripherin/Rds dimers when analyzed on nonreducing SDS gels. Consistent with this result, disc membranes contained twice as much peripherin/Rds as Rom-1. Peripherin/Rds individually expressed in COS-1 cells also formed disulfide-linked oligomers bridged through Cys-150 residues, whereas Rom-1 showed little tendency to form oligomers. These results indicate that peripherin/Rds and Rom-1 associate noncovalently to form multisubunit core complexes. Peripherin/Rds containing core complexes interact through specific intermolecular disulfide bonds to form oligomers which may play a crucial role in photoreceptor disc morphogenesis and retinal degenerative diseases.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fixatives,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaral,
http://linkedlifedata.com/resource/pubmed/chemical/Intermediate Filament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/peripherin
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
25
|
|
pubmed:volume |
275
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
5370-8
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:10681511-Animals,
pubmed-meshheading:10681511-COS Cells,
pubmed-meshheading:10681511-Cattle,
pubmed-meshheading:10681511-Centrifugation,
pubmed-meshheading:10681511-Chromatography, Affinity,
pubmed-meshheading:10681511-Cross-Linking Reagents,
pubmed-meshheading:10681511-Disulfides,
pubmed-meshheading:10681511-Dithiothreitol,
pubmed-meshheading:10681511-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10681511-Ethylmaleimide,
pubmed-meshheading:10681511-Eye Proteins,
pubmed-meshheading:10681511-Fixatives,
pubmed-meshheading:10681511-Glutaral,
pubmed-meshheading:10681511-Intermediate Filament Proteins,
pubmed-meshheading:10681511-Kinetics,
pubmed-meshheading:10681511-Membrane Glycoproteins,
pubmed-meshheading:10681511-Membrane Proteins,
pubmed-meshheading:10681511-Models, Chemical,
pubmed-meshheading:10681511-Nerve Tissue Proteins,
pubmed-meshheading:10681511-Protein Conformation,
pubmed-meshheading:10681511-Protein Structure, Quaternary,
pubmed-meshheading:10681511-Rod Cell Outer Segment,
pubmed-meshheading:10681511-Sulfhydryl Reagents,
pubmed-meshheading:10681511-Time Factors
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
Disulfide-mediated oligomerization of Peripherin/Rds and Rom-1 in photoreceptor disk membranes. Implications for photoreceptor outer segment morphogenesis and degeneration.
|
|
pubmed:affiliation |
Department of Biochemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
