Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-4-1
pubmed:abstractText
The possible role of rhodopsin in the binding and phagocytosis of rod outer segments (ROS) by cultured bovine retinal pigment epithelial (RPE) cells was studied using both quantitative phagocytosis assays and electron microscopy. In inhibition studies an immunoaffinity purified 2-39 N-terminal rhodopsin glycopeptide, a synthetic 1-16 peptide analogue of rhodopsin and purified, unsealed ROS disc membranes were found to be ineffective in inhibiting the binding of 125I-labeled ROS to RPE cells. A two-fold excess of unlabeled intact ROS, however, inhibited 125I-labeled ROS binding to RPE cells by over 40%. In another series of experiments, rhodopsin on the surface of fixed ROS was densely labeled with gold-dextran particles conjugated to an N-terminal-specific (rho 4D2) rhodopsin monoclonal antibody or its F(ab')2 fragment in an effort to block binding and phagocytosis by RPE cells. As visualized by both transmission and scanning electron microscopy using secondary and backscatter electron imaging, these antibody-gold-dextran-labeled ROS were effectively phagocytized by RPE cells. These results provide compelling evidence that rhodopsin in the ROS plasma membrane does not function as the ligand for recognition by RPE cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0146-0404
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
419-28
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Evidence against the role of rhodopsin in rod outer segment binding to RPE cells.
pubmed:affiliation
Department of Biochemistry, University of British Columbia, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't