{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T16:19:16Z","timestamp":1758817156309},"reference-count":42,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2004,2,19]],"date-time":"2004-02-19T00:00:00Z","timestamp":1077148800000},"content-version":"vor","delay-in-days":5284,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[1989,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Microvilli were isolated from cultured human JEG\u20103 choriocarcinoma cells using a gentle shearing method. The protein components of the isolated microvilli were examined by sodium dodecylsulfate\u2010polyacrylamide gel electrophoresis (SDS\u2010PAGE) and immunoblotting. The major M<jats:sub>r<\/jats:sub> 42,000 and M<jats:sub>r<\/jats:sub> 100,000 polypeptide bands reacted with anti\u2010actin and anti\u2010\u03b1\u2010actinin antisera, respectively. Extraction of the isolated JEG\u20103 microvilli with Triton X\u2010100 left an insoluble cytoskeletal residue containing mainly actin, \u03b1\u2010acinin, and polypeptides of M<jats:sub>r<\/jats:sub> 200,000, 55,000 and 35,000. The M<jats:sub>r<\/jats:sub> 35,000 polypeptide remained insoluble only at high concentrations of free Ca<jats:sup>2+<\/jats:sup>. Immunoblotting analysis of the JEG\u20103 microvilli indicated that they were devoid of tropomyosin, although the total JEG\u20103 protein lysates gave a strong positive reaction with anti\u2010tropomyosin, antiserum. The different subcellular localization of cytovillin and tropomyosin was also shown by indirect immunofluorescence microscopy. Cytovillin, an M<jats:sub>r<\/jats:sub> 75,000 microvillus\u2010specific membrane protein of JEG\u20103 cells, existed in an oligomeric form (dimer or trimer) as shown by gel filtration of Triton X\u2010100 solubilized microvillar proteins and by native polyacrylamide gel electrophoresis of purified cytovillin. Disulfide bridges were not involved in the aggregation, because the mobility of cytovillin was similar under reducing and nonreducing conditions in SDS\u2010PAGE. Cytovillin was shown to be closely related to ezrin, a minor component of chicken intestinal brush border microvilli.<\/jats:p>","DOI":"10.1002\/jcb.240410102","type":"journal-article","created":{"date-parts":[[2004,12,30]],"date-time":"2004-12-30T15:51:51Z","timestamp":1104421911000},"page":"1-12","source":"Crossref","is-referenced-by-count":17,"title":["Cytovillin and other microvillar proteins of human choriocarcinoma 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