{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T13:08:10Z","timestamp":1774789690919,"version":"3.50.1"},"reference-count":40,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2004,10,11]],"date-time":"2004-10-11T00:00:00Z","timestamp":1097452800000},"content-version":"vor","delay-in-days":4181,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Neuroscience Research"],"published-print":{"date-parts":[[1993,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We have extended our studies on the content of white matter derived coated vesicles (WMCVs) to show that they are enriched in membrane\u2010bound carbonic anhydrase. Within the myelin complex membrane\u2010bound carbonic anhydrase is concentrated in the periaxolemmal domain; however, this protein is enriched almost sevenfold in the bilayer of coated vesicles even relative to this myelin membrane region. These data suggest that some vesicles are derived from a site at which this enzyme is highly localized. The enrichment observed for membrane\u2010bound carbonic anhydrase is unique since other periaxolemmal proteins such as CNPase and plasmolipin are only present in equal amounts in periaxolemmal\u2010myelin fractions and WMCVs. Based on their known localization, the presence of CNPase coupled with the absence of MAG in WMCVs suggest that these vesicles are derived from the paranodal region. The identification in WMCVs of periaxolemmal\u2010myelin proteins associated with ion and fluid movement, such as carbonic anhydrase, Na<jats:sup>+<\/jats:sup>, K<jats:sup>+<\/jats:sup> ATPase, and the putative K<jats:sup>+<\/jats:sup> channel protein plasmolipin, prompted us to examine the status of these vesicles in triethyl tin (TET)\u2010induced myelin edema. Coated vesicles and other membrane fractions were isolated from whole brains of control and TET\u2010treated rats. Whole brains were used so we could compare the effects of TET on WMCV proteins with the effect on proteins enriched in gray matter coated vesicles. The results indicated that TET had no detectable effect on compact or periaxolemmal\u2010myelin, however, Western blot analysis showed that WMCV proteins, such as carbonic anhydrase, CNPase, and plasmolipin, were virtually absent or greatly diminished from the whole brain coated vesicle fraction. In contrast, gray matter coated vesicle proteins such as synaptophysin, SV2, and the general vesicle protein, cation\u2010independent mannose\u20106\u2010phosphate receptor were unchanged. These results indicate that coated vesicles may be a useful probe for membrane changes associated with leukopathologies. \u00a9 1993 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jnr.490350110","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T18:49:45Z","timestamp":1117306185000},"page":"83-91","source":"Crossref","is-referenced-by-count":14,"title":["Identification of membrane\u2010bound carbonic anhydrase in white matter coated vesicles: The fate of carbonic anhydrase and other white matter coated vesicle proteins in triethyl tin\u2010induced leukoencephalopathy"],"prefix":"10.1002","volume":"35","author":[{"given":"V. 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