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Blocking protein improves nuclear blebbing in mouse fibroblasts containing a targeted Hutchinson-Gilford Progeria syndrome mutation.
* By Shao H. Yang, Julia I. Toth, Yan Hu, Salemiz Sandoval, Stephen G. Young, and Loren G. Fong, David Geffen School of Medicine, UCLA; Margarita Meta, University of California, San Francisco; Pravin Bendale and Michael H. Gelb, University of Washington, Seattle; Martin O. Bergo, Sahlgrenska University Hospital, Sweden
After creating a gene-targeted mouse model of Hutchinson-Gilford Progeria Syndrome (HGPS), the authors set out to prove that the inhibition of a process called protein farnesylation with farnesyltransferase inhibitors (FTIs) can block the damage to the nuclear envelope caused by the mutant protein progerin. The studies suggest the cells can be repaired using this approach.
The mutant prelamin A in HGPS, commonly called progerin, is caused by a mutation in LMNA that results in the deletion of 50 amino acids within prelamin A and prevents normal processing to mature lamin A. The presence of progerin in cells adversely affects the integrity of the nuclear lamina, resulting in misshapen nuclei and nuclear blebs.
Fong and his group examined the effects of an FTI on this process and found that it resulted in a striking improvement on nuclear shape (reduced misshapen and damaged nuclei).
"These studies suggest a possible treatment strategy for Progeria" says co-author Dr. Steven Young, "raising the hope that FTIs might ultimately prove useful for treating Progeria."