These texts were produced by a student taking part in the “Writing Labs” that I regularly offer at the MDC. These individual workshops give students a chance to write about science for a nonspecialist audience. Usually I have the students write two short articles: one regarding their own research, or a project closely related to it, and another regarding work they are less familiar with. Generally they have more distance from the latter paper and do a better job. It’s a good exercise that has a lot of secondary pay-offs: not only do students develop general writing skills, it helps them structure their thinking about their own work and present it more clearly. More on that later.
Finally, I’ll publish some of their work on the blog so that they can rack up “publication credits.” If you want to make a career in science communications, you need to be ready to show some examples of your work. We’re developing other places for students and scientists to publish such pieces. (See, for example, http://www.scienceinschool.org/ – the magazine for science teachers I helped develop while at the EMBL.
This is the “unfamiliar research” article from a student who very generously allowed me to publish both versions of her text on the site.
I haven’t included the “work” stage, where we analyzed and restructured the content, fixed grammatical errors, etc. First I’ll let the texts speak for themselves.
If you’re interested in doing such an exercise, or knowing more, get in touch!
Aging: one protein,
multiple molecular defects
While we all look to reverse the signs of aging, scientists have been for long trying to pinpoint the molecular mechanisms behind it. A two people work in Science, 19th of May 2006, by NIH researchers Paola Scaffidi and Tom Misteli, have identified an important player that, solely, could lead cells to aging-associated defects.
As society pressurizes for long-lasting young-looks, teenager stamina and increased life-spam science tries to come up with solutions for this first-world problem. Developments in aesthetic and plastic medicines and increased awarenessess in anti-aging food diets have been helping the most concerned preventing premature aging and minimizing the aging signs. Although many theories have been proposed by scientists of how molecular mechanisms are disrupted throughout one’s lifetime, we are far from understanding the source of the problem. In this paper, Scaffidi has revealed that Lamin A, a protein located at the nucleus envelope (structure separating the DNA packed nucleus from the cytoplasm) participates in the aging process by disrupting relevant cellular functions.
The authors have compared skin cells from normal aging individuals with premature aging HGPS (Hutchinson-Gilford progeria syndrome) disease patients. HGPS is a rare disease that leads to premature dead (mid teens, early twenties). Growth defects are accompanied with accelerated aging processes such as hair loss, atherosclerosis, wrinkled skin, etc. The genetics behind this disease is a mutation in the Lamin A gene, an integrative constitutive of the nuclear envelope. This structure is responsible for the organisation of chromatin (DNA and proteins called histones) and regulation of gene activity (usually “off” when associated with the lamina).
Lamin A was also found to be mutated in normal aging cells. Scaffidi showed that, like in HGPS, the nucleus presents an irregular shape, abnormal amounts of proteins associated with the nuclear envelope structure and an accumulation of DNA errors by disruption of repairing mechanisms (upon each cell cycle, where mother cells generate two daughter cells, the DNA is checked and repaired by appropriate mechanisms). As researchers revert these phenomena’s by inhibiting the mutated Lamin A protein version, it opens new avenues for the research of therapeutics against mutated Lamin A.
Using HGPS as a model system seems to be helping scientists figuring out clues into the normal aging mechanisms. As the scientific knowledge on aging grows, the players are slowly being unravelled raising a robust set of potential targets which usefulness, solo or in a cocktail, could be further explored.
On growing old:
From a wrinkled cell nucleus
to the symptoms of aging
A protein that is mutated in an extreme rapid-aging disease also shows defects during normal aging processes
Most of us would like to enjoy a long-lasting youthful appearance, the stamina of a teenager, and an increased lifespan. The causes of aging lie in molecular processes within our cells which scientists have been trying to pin down for a long time. In a paper in the May 19, 2006 edition of Science, NIH researchers Paola Scaffidi and Tom Misteli identify an important protein that, on its own, seems to lead to age-associated defects in cells.
Developments in plastic surgery and “aesthetic medicine,” as well as an increased awarenessess of the contributions of diet, have played the largest role in preventing premature aging and minimizing its symptoms. Scientists have proposed a number of theories to account for the way molecular mechanisms are disrupted throughout one’s lifetime to cause aging, but we are far from understanding the real sources of the problem. Now Scaffidi and Misteli reveal that a single protein participates in the process by disrupting a number of important cellular functions.
Their work focuses on a protein called Lamin A. It is found in nearly every human cell and makes up part of the nuclear envelope, a membrane that surrounds the DNA in the cell nucleus and separates it from the surrounding cellular compartment called the cytoplasm. As well as giving the envelope a regular shape, Lamin A helps organize DNA in the nucleus and control the activity of genes. It binds to strands of chromatin (a mixture of DNA and the proteins that are attached to it), which usually keeps nearby genes “switched off.”
The authors came across Lamin A when comparing skin cells from normal aging individuals with those of people who suffer from a type of extreme premature aging called HGPS (Hutchinson-Gilford progeria syndrome). HGPS is a rare disease that leads to premature death in a patient’s teens or early twenties. Those with the syndrome suffer the symptoms of accelerated aging such as hair loss, atherosclerosis, wrinkled skin, etc. Several years ago scientists discovered that patients with this disease have a mutation in the Lamin A gene.
Scaffidi and Misteli now show that Lamin A is also mutated in normal aging cells. As in HGPS, the nucleus presents an irregular shape. They also found that that cells produce abnormal amounts of proteins associated with the nuclear envelope structure. Additionally, the cells display an accumulation of DNA errors by disrupting mechanisms involved in DNA repair. (Normally, each time mother cells generate two daughter cells, the DNA is checked and repaired by appropriate mechanisms.) The scientists inhibited the mutated version of Lamin A protein by providing cells with a healthy version. This procedure reversed the defects caused by the mutation. So the work opens new avenues for research into therapies that target mutated forms of Lamin A, which might correct – or at least slow down – some of the problems associated with normal aging.
This makes HGPS a model system that may help scientists figure out normal aging mechanisms. As our scientific knowledge on aging grows, new molecular players are being identified, revealing a set of potential targets whose usefulness will be explored in further work.
Scaffidi P, Misteli T. Lamin A-dependent nuclear defects in human aging. Science. 2006 May 19;312(5776):1059-63.