Autor: |
Kilic, Fusun, Salas-Marco, Joe, Garland, John, Sinensky, Michael |
Předmět: |
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Zdroj: |
ETSU Faculty Works. |
Druh dokumentu: |
Text |
DOI: |
10.1016/S0014-5793(97)00989-7 |
Popis: |
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. |
Databáze: |
Networked Digital Library of Theses & Dissertations |
Externí odkaz: |
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