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저자： 업로드：2017-09-01 조회수：
It may seem paradoxical, but studying what goes wrong in rare diseases can provide useful insights into normal health. Researchers probing the premature aging disorder Hutchinson-Gilford progeria syndrome (HGPS) have uncovered an errant protein process in the disease that could help healthy people as well as progeria sufferers live longer.
Now, investigators at the
Salk Institute have uncovered an errant protein process in HGPS that could help
healthy people, as well as progeria sufferers, live longer. Findings from the
new study, published today in Nature
Communications in an article entitled “Nucleolar
Expansion and Elevated Protein Translation in Premature Aging”, showed that protein synthesis is
overactive in people with progeria. These new findings add to a growing body of
evidence that reducing protein synthesis can extend lifespan, and thus may
offer a useful therapeutic target to counter both premature and normal aging.
"The production of proteins is an extremely energy-intensive process for cells," explained senior study investigator Martin Hetzer, Ph.D., vice president and chief science officer at the Salk Institute. "When a cell devotes valuable resources to producing protein, other important functions may be neglected. Our work suggests that one driver of both abnormal and normal aging could be accelerated protein turnover."
HGPS is a very rare genetic disease, causing people to age eight to ten times faster than normal and leading to premature death. The rare mutation occurs in one of the structural proteins in the cell nucleus - lamin A - but it has been unclear how a single defective protein in the nucleus causes the myriad rapid-aging features seen in the disease.
The Salk researchers were initially interested in whether the mutation was making the lamin A protein less stable and shorter lived. After measuring protein turnover in cultured cells from skin biopsies of both progeria sufferers and healthy people, they found that it wasn't just lamin A that was affected by the disease.
“We analyzed all the proteins of the nucleus, and instead of seeing rapid turnover in just mutant lamin A and maybe a few proteins associated with it, we saw a really broad shift in overall protein stability in the progeria cells," noted lead study investigator Abigail Buchwalter, Ph.D., a staff scientist at the Salk Institute. "This indicated a change in protein metabolism that we hadn't expected."
In addition to the rapid turnover
of proteins, the r
