{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,23]],"date-time":"2026-02-23T20:10:28Z","timestamp":1771877428612,"version":"3.50.1"},"reference-count":0,"publisher":"Rockefeller University Press","issue":"5","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1990,5,1]]},"abstract":"<jats:p>mAb-based approaches were used to identify cell surface components involved in the development and function of the frog olfactory system. We describe here a 205-kD cell surface glycoprotein on olfactory receptor neurons that was detected with three mAbs: 9-OE, 5-OE, and 13-OE. mAb 9-OE immunoreactivity, unlike mAbs 5-OE and 13-OE, was restricted to only the axons and terminations of the primary sensory olfactory neurons in the frog nervous system. The 9-OE polypeptide(s) were immunoprecipitated and tested for cross-reactivity with known neural cell surface components including HNK-1, the cell adhesion molecule L1, and the neural cell adhesion molecule (N-CAM). These experiments revealed that 9-OE-reactive molecules were not L1 related but were a subset of the 200-kD isoforms of N-CAM. mAb 9-OE recognized epitopes associated with N-linked carbohydrate residues that were distinct from the polysialic acid chains present on the embryonic form of N-CAM. Moreover, 9-OE N-CAM was a heterogeneous population consisting of subsets both with and without the HNK-1 epitope. Thus, combined immunohistochemical and immunoprecipitation experiments have revealed a new glycosylated form of N-CAM unique to the olfactory system. The restricted spatial expression pattern of this N-CAM glycoform suggests a possible role in the unusual regenerative properties of this sensory system.<\/jats:p>","DOI":"10.1083\/jcb.110.5.1729","type":"journal-article","created":{"date-parts":[[2004,5,15]],"date-time":"2004-05-15T00:18:20Z","timestamp":1084580300000},"page":"1729-1743","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":78,"title":["Olfactory neurons express a unique glycosylated form of the neural cell adhesion molecule (N-CAM)."],"prefix":"10.1083","volume":"110","author":[{"given":"B","family":"Key","sequence":"first","affiliation":[{"name":"Division of Basic Research, Children's Hospital Reserch Foundation, Cincinnati, Ohio 45229."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R A","family":"Akeson","sequence":"additional","affiliation":[{"name":"Division of Basic Research, Children's Hospital Reserch Foundation, Cincinnati, Ohio 45229."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[1990,5,1]]},"container-title":["The Journal of cell biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/110\/5\/1729\/1463797\/1729.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/110\/5\/1729\/1463797\/1729.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,22]],"date-time":"2023-07-22T01:10:24Z","timestamp":1689988224000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/110\/5\/1729\/28423\/Olfactory-neurons-express-a-unique-glycosylated"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,5,1]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1990,5,1]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.110.5.1729","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,5,1]]}}}