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The purpose of the present experiment was to determine if the calcium\u2010activated protease m\u2010calpain (EC 3.4.22.17) was responsible for truncation of human AQP0. AQP0 was isolated from young human donors, incubated with recombinant m\u2010calpain, and the cleavage sites on the released peptides were determined by on\u2010line electrospray ionization mass spectrometry. We found that four cleavage sites on human AQP0 could be tentatively assigned to m\u2010calpain. This is the first evidence for possible calpain activity in human lens. Because the cause(s) of 17 other cleavage sites was unknown, the data also suggested that other, as yet unknown, proteases or non\u2010enzymatic mechanisms are more active than calpain in human lens.<\/jats:p>","DOI":"10.1016\/j.febslet.2005.11.004","type":"journal-article","created":{"date-parts":[[2005,11,22]],"date-time":"2005-11-22T12:31:07Z","timestamp":1132662667000},"page":"6745-6748","source":"Crossref","is-referenced-by-count":11,"title":["Degradation of human aquaporin 0 by m\u2010calpain"],"prefix":"10.1002","volume":"579","author":[{"given":"H.","family":"Ma","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Azuma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T.R.","family":"Shearer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,11,21]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.proghi.2004.03.001"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi0496034"},{"key":"e_1_2_6_4_1","first-page":"175","article-title":"Characterization of human lens major intrinsic protein structure","volume":"41","author":"Schey K.L.","year":"2000","journal-title":"Invest. 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