2008 Proceedings - St. Cloud State University

Abstracts
Session T All Disciplines Ballroom
Anticancer Activity of Ru-Benzimidazol Metal Complexes
One of the mostly widely used inorganic compounds is Cisplatin. Cisplatin-based therapies are used throughout the world to treat testicular
and ovarian cancers. The discovery of other metal complexes as anticancer drugs for their use to treat drug resistant tumors and
development of alternative therapies has gained importance. In this regard we have developed several ruthenium-benzimidazole
compounds and assayed for their anticancer activities. Tested in this study were ligand 3 [2-phenyl benzimidazole] and its corresponding
complex RU 3 [(Rucl3(PhBzIH)3]; ligand 6 [1-m-hydroxbenzyl-2-m-hydroxy phenyl benzimidazole] and its corresponding complex RU 9
[RuCl3(m-HPhBBzI)2]; Ligand 7 (1-p-hydroxybenzyl-2-p-hydroxy phenyl benzimidazole] and its corresponding complex RU 8
[RuCl3,(CO)2(p-HphBBzI)2]. Two human breast adenocarcinoma cell lines MCF-7/0 and MCF-7/OttA were used for testing anticancer
activities. These ruthenium complexes tested exhibit a range of anticancer activities; LC50 values- 50-150 µM. Ruthenium itself is not toxic
to the cells.
Presentation Index: T47
Time: 2:00 p.m.
Department: Chemistry
Project Sponsor(s):
Student Presenter(s): Mahroof, Taqdees
Sreerama, Lakshmaiah
The Role of CDC-4 in the Degradation of PGC-1 and Human Diseases
PGC-1 is a human protein that plays a role in energy metabolism. Misregulation of this protein has been shown to play a role in diabetes,
obesity and certain neurological disorders. Two forms of this protein are known, PGC-1á and PGC-1â. We recently demonstrated that
another human protein known as CDC-4 targets PGC-1á for degradation by adding ubiquitin to it. This ubiquitylation leads to destruction of
the PGC-1á protein and may be linked to some human diseases. Much like PGC-1á, PGC-1 has similar CDC-4 binding sites and
physically binds to CDC-4. Here we are testing whether CDC-4 also adds ubiquitin to PGC-1â.
Presentation Index: T48
Time: 2:00 p.m.
Department: Biological Sciences
Project Sponsor(s):
Student Presenter(s): Schwinn, Andrew; Zimdars, Laraine
Olson, Brian
The First Annotation of the Glycine and Serine Biosynthetic Pathways of Ammonifex Degensii
Ammonifex degensii is an obligate anaerobic chemolithoautotrophic (obtains energy from inorganic compounds and carbon from carbon
dioxide) bacteria isolated from a volcanic hot spring in East Asia in 1994. Ammonifex is the archetype of a new genus (ammonium maker).
Ammonifex degensii is an extremely thermophilic gram negative rod shaped bacterium with optimal growth occurring at 70 degrees C and
a pH of 7.5. The genome of ammonifex degensii is 85% complete, funded by the Department of Energy Joint Genome Program. Saint
Cloud State University is part of a consortium of institutions that make up the Collaborative Undergraduate Genomic Annotation Team.
SCSU has undertaken the responsibility of using comparative genomics to identify the amino acid biosynthetic pathways. Glycine is a
nonpolar aliphatic amino acid and is the smallest of the 20 amino acids. Serine is a polar uncharged amino acid that differes from glycine
by a hydroxyl group. We hypothesize that these amono acids have biosynthetic pathways in ammonifes degensii, and that we will be able
to identify the genes responsible for the synthesis of these amino acids using a comparative genomics approach.
Presentation Index: T49
Time: 2:00 p.m.
Department: Biological Sciences
Project Sponsor(s):
Student Presenter(s): Petersen, David; Paudel, Omkar; Kone, Nabi; Chin, Fei T Kvaal, Christopher
Identification and Characterization of Aldehyde Dehydrogenase in Fathead Minnow Tissues
Ethylene glycol ethers (EGEs) are monoalkyl or aryl ethers of ethylene glycol and are widely used solvents in industrial and household
products. EGEs are metabolized by aldehyde dehydrogenases (ALDHs) to their corresponding acids and it is believed to be the rate
determining step in the EGE metabolism. In mammals, the acid metabolites cause various toxicities including carcinogenesis and
mutagenesis. EGEs are discharged into waterways with relatively high concentration and aquatic animals such as fathead minnows and
frogs are exposed to these chemicals. Our studies show that EGE toxicities are likely to be seen in the above aquatic animals. Both
fathead minnows and frogs have been shown to contain ALDHs and they catalyze oxidation of EGE aldehydes. The identity of these
ALDHs is currently being investigated using in various tissues of fathead minnows.
Presentation Index: T50
Time: 2:00 p.m.
Department: Chemistry
Project Sponsor(s):
Student Presenter(s): Paudel, Omkar
Sreerama, Lakshmaiah
St. Cloud State University Student Research Colloquium 64
April 22, 2008