NDLI: Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome.

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Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome.

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Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Davies, Brandon S. J. Yang, Shao H. Farber, Emily Lee, Roger Buck, Suzanne B. Andres, Douglas A. Spielmann, H. Peter Agnew, Brian J. Tamanoi, Fuyuhiko Fong, Loren G. Young, Stephen G.
Description	Country affiliation: United States Author Affiliation: Davies BS ( Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.)
Abstract	Hutchinson-Gilford progeria syndrome (HGPS) is caused by the synthesis of a truncated prelamin A, commonly called progerin, that contains a carboxyl-terminal farnesyl lipid anchor. The farnesyl lipid anchor helps to target progerin to membrane surfaces at the nuclear rim, where it disrupts the integrity of the nuclear lamina and causes misshapen nuclei. Several lines of evidence have suggested that progerin's farnesyl lipid anchor is crucial for the emergence of disease phenotypes. Because a geranylgeranyl lipid is approximately 45-fold more potent than a farnesyl lipid in anchoring proteins to lipid membranes, we hypothesized that a geranylgeranylated version of progerin might be more potent in eliciting disease phenotypes. To test this hypothesis, we used gene targeting to create mice expressing geranylgeranylated progerin (Lmna(ggHG/+)). We then compared Lmna(ggHG/+) mice, side-by-side, with otherwise identical mice expressing farnesylated progerin (Lmna(HG/+)). Geranylgeranylation of progerin in Lmna(ggHG/+) cells and farnesylation of progerin in Lmna(HG/+) cells was confirmed by metabolic labeling. Contrary to our expectations, Lmna(ggHG/+) mice survived longer than Lmna(HG/+) mice. The Lmna(ggHG/+) mice also exhibited milder bone disease. The steady-state levels of progerin, relative to lamin C, were lower in Lmna(ggHG/+) mice than in Lmna(HG/+) mice, providing a potential explanation for the milder disease in Lmna(ggHG/+) mice.
File Format	HTM / HTML
ISSN	00222275
e-ISSN	15397262
DOI	10.1194/jlr.M800424-JLR200
Journal	The Journal of Lipid Research
Issue Number	1
Volume Number	50
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2009-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Bone Diseases Pathology Nuclear Proteins Physiology Progeria Genetics Protein Precursors Animals Metabolism Genotype Lamin Type A Lipids Chemistry Mice Mice, Transgenic Models, Biological Models, Genetic Molecular Sequence Data Syndrome Tissue Distribution Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Endocrinology

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Increasing the length of progerin’s isoprenyl anchor does not worsen bonedisease or survival in mice with Hutchinson-Gilford progeria syndrome

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RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: implications for Hutchinson-Gilford progeria syndrome

Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome.

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Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome.