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Purified caspase\u201014 revealed the highest activity on WEHD\u2010methylcoumaryl\u2010amide (MCA), although YVAD\u2010MCA, another caspase\u20101 substrate, was poorly hydrolyzed. The purified protein was a heterodimer with 17 and 11\u2009kDa subunits. N\u2010terminal and C\u2010terminal analyses demonstrated that the large subunit consisted of Ser<jats:sup>6<\/jats:sup>\u2010Asp<jats:sup>146<\/jats:sup> and N\u2010terminal of small subunit was identified as Lys<jats:sup>153<\/jats:sup>. We successfully developed an antiserum (anti\u2010h14D146) directed against the Asp<jats:sup>146<\/jats:sup> cleavage site, which reacted only with active caspase\u201014 but not with procaspase\u201014. Furthermore we confirmed that anti\u2010h14D146 did not show any reactivity to the active forms of other caspases. Immunohistochemical analysis demonstrated that anti\u2010h14D146 staining was mostly restricted to the cornified layer and co\u2010localized with some of the TUNEL positive\u2010granular cells in the normal human epidermis. UV radiation study demonstrated that caspase\u20103 was activated and co\u2010localized with TUNEL\u2010positive cells in the middle layer of human epidermis. In contrast, we could not detect caspase\u201014 activation in response to UV. Our study revealed tightly regulated action of caspase\u201014, in which only the terminal differentiation of keratinocytes controls its activation process. J. Cell. Biochem. 109: 487\u2013497, 2010. \u00a9 2009 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcb.22425","type":"journal-article","created":{"date-parts":[[2009,12,3]],"date-time":"2009-12-03T21:09:36Z","timestamp":1259874576000},"page":"487-497","source":"Crossref","is-referenced-by-count":19,"title":["Purification and characterization of active caspase\u201014 from human epidermis and development of the cleavage site\u2010directed 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