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We found that the proteinase is not expressed by thymocytes and resting T cells but can be induced by lectin or antigen in combination with lymphokine sources <jats:italic>in vitro<\/jats:italic> in macrophage\u2010depleted unselected T cells as well as in both T cell subsets (Lyt\u20102<jats:sup>+<\/jats:sup>, L3T4<jats:sup>\u2212<\/jats:sup>and Lyt\u20102<jats:sup>\u2212<\/jats:sup>, L3T4<jats:sup>+<\/jats:sup>) separated by flow cyto\u2010fluorometry. Furthermore, it appears that cell\u2010associated proteinase activity is increasing with prolonged culture period of sensitized T lymphocytes and that it is higher in antigen\u2010activated as compared to lectin\u2010activated T cells. When tested for substrate specificity the T cell\u2010associated proteinase was shown to preferentially cleave model peptide substrates carrying L\u2010arginine at position P1 in combination with nonpolar amino acids at position P2 and P3. As concluded from its sensitivity to proteinase inhibitors the enzyme can be classified as a serine proteinase and by molecular sieving at high ionic strength it was shown to have a mol. mass of \u223c 50\u201360 kDa.<\/jats:p><jats:p>Analysis of <jats:italic>in vivo<\/jats:italic> activated T cells revealed that this particular proteinase was expressed in flow cytofluorometry sorted lymphocytic choriomeningitis virus\u2010specific Lyt\u20102<jats:sup>+<\/jats:sup>, L3T4<jats:sup>\u2212<\/jats:sup> cytolytic T lymphocytes but not in Lyt\u20102<jats:sup>\u2212<\/jats:sup>, L3T4<jats:sup>+<\/jats:sup>T cells presensitized with either <jats:italic>Listeria monocytogenes<\/jats:italic> or I\u2010A alloantigens.<\/jats:p><jats:p>The data demonstrate that the two T cell subsets (Lyt\u20102<jats:sup>+<\/jats:sup>, L3T4<jats:sup>\u2212<\/jats:sup>; Lyt\u20102<jats:sup>\u2212<\/jats:sup>,L3T4<jats:sup>+<\/jats:sup>) have distinct <jats:italic>in vitro<\/jats:italic> induction requirements for the expression of proteinase and that after activation of T cells <jats:italic>in vivo<\/jats:italic> the enzyme is preferentially associated with Lyt\u20102<jats:sup>+<\/jats:sup>, L3T4<jats:sup>\u2212<\/jats:sup>effector cells.<\/jats:p>","DOI":"10.1002\/eji.1830161215","type":"journal-article","created":{"date-parts":[[2007,2,28]],"date-time":"2007-02-28T22:41:48Z","timestamp":1172702508000},"page":"1559-1568","source":"Crossref","is-referenced-by-count":31,"title":["A specific serine proteinase is inducible in Lyt\u20102<sup>+<\/sup>, L3T4<sup>\u2212<\/sup> and Lyt\u20102<sup>\u2212<\/sup>, L3T4<sup>+<\/sup> T cells <i>in vitro<\/i> but is mainly associated with Lyt\u20102<sup>+<\/sup>, L3T4<sup>\u2212<\/sup> effector cells <i>in vivo<\/i>"],"prefix":"10.1002","volume":"16","author":[{"given":"Markus M.","family":"Simon","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ulli","family":"Fruth","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hans Georg","family":"Simon","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael D.","family":"Kramer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,11,22]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2736(81)90451-X"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI111985"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.136.12.4644"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0277-5379(85)90130-0"},{"key":"e_1_2_1_6_2","unstructured":"Simon M. 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