{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T04:58:25Z","timestamp":1791089905200,"version":"4.1.0"},"reference-count":76,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2004,10,11]],"date-time":"2004-10-11T00:00:00Z","timestamp":1097452800000},"content-version":"vor","delay-in-days":4089,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Neuroscience Research"],"published-print":{"date-parts":[[1993,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Mammalian peripheral nervous system (PNS) myelin contains several glycoproteins with molecular weights of 19 to 28 kDa, including the major 28 kDa P0 glycoprotein and a recently cloned protein called PMP22. Some glycoproteins in this M<jats:sub>r<\/jats:sub> range in humans, cats and some other mammals react with HNK1, a mouse monoclonal antibody that identifies a carbohydrate epitope shared between the immune system and a number of adhesion proteins in the nervous system. A variety of antibodies to PO, PMP\u201022, and the carbohydrate determinants reacting with HNK1 were used to characterize immunochemically these 19 to 28 kDa glycoproteins of cat PNS myelin. The HNK1\u2010reactive components include P0 and two slightly smaller 23 to 26 kDa proteins that are immunologically related to PO. However, HNK1 reacts most strongly with a lower molecular weight glycoprotein that does not react with the antibodies to P0 and was identified as PMP\u201022. Since the carbohydrate structure reacting with HNK1 is generally expressed on adhesion molecules, this result suggests that PMP\u201022 may function in cell\u2010cell or membranemembrane interactions. Furthermore, the related human anti\u2010MAG monoclonal lgM antibodies from patients with neuropathy also react strongly with PMP\u201022, suggesting that it may be a target antigen in the pathogenesis of this disease. Purified PNS and CNS myelin from bony fish (toadfish and trout) were also shown to contain major glycoproteins, in the same 19 to 28 kDa M<jats:sub>r<\/jats:sub> range, that react very strongly with HNK1. It is known that fish myelin has major proteins of this size that are immunologically and structurally related to mammalian P0, and it is demonstrated here that one of the strongly HNK1\u2010positive proteins reacted well with an antiserum raised to bovine P0. The presence of high levels of the adhesion\u2010related HNK1 epitope on these major myelin proteins of fish suggests that this carbohydrate structure may have played a role in the molecular evolution of myelin. \u00a9 1993 Wiley\u2010Liss, Inc.<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"#note1\"\/><jats:fn><jats:p>This article is a US Government work and, as such, is in the public domain in the United States of America.<\/jats:p><\/jats:fn>\n<\/jats:p>","DOI":"10.1002\/jnr.490350511","type":"journal-article","created":{"date-parts":[[2005,1,1]],"date-time":"2005-01-01T01:51:03Z","timestamp":1104544263000},"page":"546-558","source":"Crossref","is-referenced-by-count":57,"title":["Immunoreactivity of PMP\u201022, P0, and other 19 to 28 kDa glycoprotens in peripheral nerve myelin of mammals and fish with HNK1 and related antibodies"],"prefix":"10.1002","volume":"35","author":[{"given":"J. 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