title: Regulation of prelamin A endoprotease activity by prelamin A.
abstract: 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 assemble into the nuclear lamina. We call the enzyme which catalyzes this endoproteolytic step the 'prelamin A endoprotease'. In this study, we begin characterization of the regulation of prelamin A endoprotease. In particular, we address the question as to whether prelamin A endoprotease activity is constitutive in cells or responds to expression of prelamin A. To do this, we compared the activity of this novel endoprotease in cells which express prelamin A with those that do not. Our data shows that the enzymatic activity of prelamin A endoprotease is enhanced by the expression of prelamin A.
authors.affiliation: Department of Biochemistry and Molecular Biology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City 37614-0581, USA. kilic@access.etsu-tn.edu
authors.forename: F
authors.initials: F
authors.lastname: Kilic
authors.forename: J
authors.initials: J
authors.lastname: Salas-Marco
authors.forename: J
authors.initials: J
authors.lastname: Garland
authors.forename: M
authors.initials: M
authors.lastname: Sinensky
mesh_terms: D002855:Chromatography, Thin Layer; D003907:Dexamethasone / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D018922:HL-60 Cells; D006367:HeLa Cells; D006801:Humans; D034904:Lamin Type A; D034882:Lamins; D008856:Microscopy, Fluorescence; D009687:Nuclear Proteins / Q000096:biosynthesis*; D011498:Protein Precursors / Q000096:biosynthesis*; D014407:Tumor Cells, Cultured; D015854:Up-Regulation
chemical_list: D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins; D011498:Protein Precursors; C090764:prelamin A; D003907:Dexamethasone; D010450:Endopeptidases; C104823:prelamin A endoprotease