Painting the big protein picture
by Lauren Bertin

[Article featured in The Bennington Free Press, September 2009]

Science is often thought of as the search for knowledge, an endless pursuit of truth; yet, a bulk of scientific development is driven by five simple letters: M-O-N-E-Y. A majority of the research is geared toward the direct production of the most marketable drugs. Much research revolves around treating the symptoms of certain diseases, rather than understanding the basic mechanisms that encompass the human body. For example in the 1980's, scientists would go out of their way to tie their research to HIV in order to receive funding. And even President Obama feeds into this type of commercialized research by saying that there will be "a cure for cancer in our time." First off let me correct the president by saying that there will not be 'a' cure, but there is a need for multiple cures for cancers. Moreover, many cancers may only in the end be preventable or treatable. This gap in system of scientific advancement is a major problem that must be bridged back together to see the bigger picture.

Heat shock proteins (HSP) originally were discovered in the 1960's. Since then research about these major proteins has drastically increased. Many proteins comprised in this category, which are also called chaperones due to their ability to 'watch over' other proteins--much as an adult would with children--, are essential in not only all humans, but also in all other organisms. These heat shock proteins literally manage the structures of other proteins, especially when the cell is under extreme stress. While scientists have learned a great deal about these proteins, much remains unknown about their unique functions.

Scientists have begun to think about the possibility of blocking chaperones' functions. Yes, inhibiting one of the most vital proteins in our body. Why? Because there's a new hot word for scientists to add to their grant applications: cancer. The National Cancer Institute provides us with a case in point, "Blocking the activity of a HSP called Hsp90 is being studied in the treatment of cancer."

However, biology faculty member at Bennington College Amie McClellan explains, "We know little about these cellular targets... it is dangerous to inhibit Hsp90 if you don't know what it's doing." But you must be asking yourself at this point how an 'art school' such as Bennington College could possibly figure out any further functions of Hsp90 to fill in the rest of the pieces to this huge protein puzzle. To override this common misconception about Bennington, this semester some major achievements may be made in our laboratories.

McClellan, during her postdoctoral position at Stanford, discovered her passion for Hsp90 and would eventually bring this research to Bennington College. After being part of a high stress research environment, she knew that small liberal arts college would be the perfect place for her to, as she says, "change the next generation, rather than one tiny area of biology." So far she has had success at uncovering the basic fundamentals of HSPs, including the identification of many more of Hsp90's functions and further understanding of the relationship Hsp90 has with other HSPs (Hsp70). While some might believe that studying such molecular complex entities could be challenging at Bennington, this is not the case. In addition to bringing with her a collection of yeast samples to study these heat shock proteins, the college fully supports her work. In fact, she not only has one experiment going on this semester, but three. All of which may fill the gaps, which other scientists are overlooking. Anne Marie Kessler, post baccalaureate, and Claire Davis, senior, are investigating what happens to certain proteins that have not been properly 'chaperoned'. These proteins with incorrect structures are often disposed of in the cell; however, scientists know very little about this process. Tambu Kudze is continuing her previous work characterizing a novel Hsp90 co-chaperone, or a fellow protein that assists Hsp90 in its roles in the cell. Sabina Shrestha is probing the association between human protein and major components of the cytoskeleton, microtubles, to elucidate the effects of blocking certain chaperone proteins, such as Hsp90.

Worrying too much about the five letter M-word (money) is causing some scientists to overlook important and possibly very dangerous mechanisms that could occur in our bodies when inhibiting these proteins. Thanks to McClellan and a few of our very own Bennington students, the scientific community will have the option of focusing on a different set of five characters: H-s-p-9-0. If McClellan's suspicions are right, that option just could save us from having to use some unpleasant four letter words in an Hsp90 inhibited future.