Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1995-9-21
pubmed:abstractText
Axons derived from young ganglion cells in the periphery of the retinae of larval and adult goldfish are known to fasciculate with one another and their immediate forerunners, creating the typical age-related order in the retinotectal pathway. Young axons express the E587 antigen, a member of the L1 family of cell adhesion molecules. Repeated injections of Fab fragments from a polyclonal E587 antiserum (E587 Fabs) into the eye of 3.4 cm goldfish disrupted the orderly fascicle pattern of RGC axons in the retina which was preserved in controls. Instead of bundling tightly, RGC axons crossed one another, grew between fascicles and arrived at the optic disk in a broadened front. When added to RGC axons growing in vitro, E587 Fabs neutralized the preference of growth cones to elongate on lanes of E587 protein, caused defasciculation of axons which normally prefer to grow along each other when explanted on polylysine, and prevented clustering of E587 antigen at axon-axon contact sites. Monoclonal E587 antibody disturbed axonal fasciculation moderately but led to a 30% reduction in growth velocities when axons tracked other axons. Therefore we conclude that E587 antigen mediates axonal recognition, selective fasciculation and the creation of the age-related order in the fish retina.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1431836, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1494955, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1574117, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1577862, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1618903, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1638134, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1809354, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1873027, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1941096, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-1991792, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2190790, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2317872, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2344405, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2351964, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2397757, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2474006, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2627373, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-2627381, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-3055291, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-3308110, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-3543026, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-3677174, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-3712001, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-3746418, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-450061, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-6325602, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-6470771, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-7346585, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-7407853, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-7823673, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-7826641, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-7958430, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-8376980, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-8386532, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-915041, http://linkedlifedata.com/resource/pubmed/commentcorrection/7642712-915042
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
130
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
969-76
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Fish E587 glycoprotein, a member of the L1 family of cell adhesion molecules, participates in axonal fasciculation and the age-related order of ganglion cell axons in the goldfish retina.
pubmed:affiliation
Faculty of Biology, University of Konstanz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't