Under the guidance of her mentor, chemistry teacher, and manuscript co-author, Lynda Blankenship, Figge examined 246 different BRCA-1 sequence mutations found in humans considered at high risk for breast or ovarian cancer. The genetic information for those people was provided from many different clinical settings and compiled in the NIH Breast Cancer Information Database ”a repository of genetic sequences for a multitude of genes found in breast cancer patients.

Figge ™s analysis of the NIH data revealed that among the known BRCA-1 mutations, sites within the genetic coding that were likely targets of mutation were the same sites conserved among humans, dogs, rats and mice. Furthermore, Figge documented that among the conserved amino acids that make up the BRCA-1 protein in the four species, the amino acids that were most likely to be mutated were those that are hydrophobic. Mutated BRCA-1 proteins that exchange hydrophobic amino acid residues for more water-loving types of amino acids may undergo structural changes that lead to loss of function. The mutations found in the abnormal BRCA-1 versions may lead to proteins that are bent out of shape and unable to perform as tumor suppressers.

Perhaps these missense mutations disturb important features of the BRCA-1 protein and play a role in breast and ovarian cancer formation, Figge said.

In addition to her current publication, Figge entered her research last year at the 13th annual Greater Capital Region Science and Engineering Fair and Science Congress at Rensselaer Polytechnic Institute. Her science was deemed worthy of advancing to the Intel International Science and Engineering Fair in May 2004 in Cleveland, Ohio. At the Intel fair, Figge won a special first place prize from the Endocrine Society.

As a contribution to the pool of knowledge upon which researchers build additional understanding of biomedical science, Figge ™s discovery may help clinicians determine the level of risk for a woman who carries specific versions of mutated BRCA-1 gene.

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