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(Received for publication, October 26, 1994; and in revised form, June 5, 1995) From the The transglutaminase 1 (TGase 1) enzyme is required for the
formation of a cornified cell envelope in epidermal keratinocytes. We
show here that in addition to its membrane-anchored form, soluble forms
of it are also important in keratinocytes. Proliferating cells contain
soluble full-length enzyme of 106 kDa, but terminally differentiating
cells contain a soluble 67-kDa form often complexed with a 33-kDa
protein as well. The amino terminus of the 67 kDa form is residue 93 of
the TGase 1 protein, corresponding to the site of proteolytic
activation of the factor XIIIa TGase. The amino terminus of the 33-kDa
protein is residue 573, corresponding to the site of a second
proteolytic cleavage site of factor XIIIa, and of the site for
proteolytic activation of the TGase 3 enzyme. The specific activity of
the 67/33-kDa soluble complex is twice that of the soluble 67-kDa form
and 10 times that of full-length TGase 1. The half-lives of the 67/33-
and 106-kDa forms are about 7 or 20 h, respectively. Thus the TGase 1
enzyme is complex, since it exists in keratinocytes as multiple soluble
forms, either intact or proteolytically processed at conserved sites,
and which have varying specific activities and likely functions.
Volume 270,
Number 30,
Issue of July 28, pp. 18026-18035, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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