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The surface IgM (sIgM) complex isolated in digitonin contains two surface expressed polypeptides \u2010 the previously described Ig\u03b1 and Ig\u03b2 proteins \u2010 covalently linked to each other in a 48\/39\u2010kDa heterodimer. We show herein that the human sIgM complex isolated from the Burkitt's lymphoma cell line, Ramos, or from dense tonsillar B cells contains additional molecules \u2212160 kDa and 75 kDa in size \u2014 and enzymatic activities able to phosphorylate on tyrosine as well as serine\/threonine residues the 39\u2212, 48\u2212, 75\u2212 and 160\u2010kDa polypeptides. By specific immunoprecipitation with antibodies to <jats:italic>src<\/jats:italic>\u2010family kinases, we consistently detected p56<jats:sup>lyn<\/jats:sup> in the sIgM complex. In the Ramos cell line, both p56<jats:sup>lck<\/jats:sup> and p59<jats:sup>fyn<\/jats:sup> activity were also observed, although to a much lesser extent than p56<jats:sup>lyn<\/jats:sup>. These kinases are associated with sIgM before cell stimulation. As shown by two\u2010dimensional electrophoresis, they interact in a tight complex with multimeric forms of the Ig\u03b1 and Ig\u03b2 components. The kinases are active <jats:italic>in vitro<\/jats:italic> but must be highly regulated <jats:italic>in vivo:<\/jats:italic> Western blotting with anti\u2010phosphotyrosine antibodies revealed that stimulation of the AgR on viable B cells increased detectable phosphotyrosine residues on the components present in the sIgM complex. Based on these phosphorylation changes, the 39\u2212, 48\u2212, 75\u2212 and 160\u2010kDa molecules are likely to be functionally active elements in an IgM complex crucial for the transduction of the antigenic signal.<\/jats:p>","DOI":"10.1002\/eji.1830220820","type":"journal-article","created":{"date-parts":[[2007,3,1]],"date-time":"2007-03-01T17:58:41Z","timestamp":1172771921000},"page":"2093-2099","source":"Crossref","is-referenced-by-count":30,"title":["Characterization of molecular components associated with surface immunoglobulin M in human B lymphocytes: Presence of tyrosine and serine\/threonine protein kinases"],"prefix":"10.1002","volume":"22","author":[{"given":"Corinne","family":"Leprince","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevin E.","family":"Draves","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeffrey A.","family":"Ledbetter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Raul M.","family":"Torres","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edward A.","family":"Clark","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,12,6]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.iy.01.040183.000341"},{"key":"e_1_2_1_3_2","unstructured":"A. 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