The maturation of lamin A is completed by the endoproteolytic cleavage
of its farnesylated precursor protein, prelamin A, In the absence of
this cleavage, prelamin A can neither give rise to lamin A nor assembl
e into the nuclear lamina, We call the enzyme which catalyzes this end
oproteolytic step the 'prelamin A endoprotease'. In this study, we beg
in characterization of the regulation of prelamin A endoprotease. In p
articular, we address the question as to whether prelamin A endoprotea
se activity is constitutive in cells or responds to expression of prel
amin A, To do this, me compared the activity of this novel endoproteas
e in cells which express prelamin A with those that do not, Our data s
hows that the enzymatic activity of prelamin A endoprotease is enhance
d by the expression of prelamin A. (C) 1997 Federation of European Bio
chemical Societies.