The University of Toledo Department of Bilogical Sciences

WOLFE HALL (Room 3246) Saturday, April 9, 2005

(click on the presenter name for abstract)

Time	Speaker	Presentation Title
9:00	Dr. Patricia Komuniecki	Welcome
9:05	Plenary Lecture- "The Pro-inflammatory Cytokine-induced GTPase, mGBP-2: Role in Altering Cell Growth annd the Interactions of Cells with their Environment" Dr. Deborah Vestal, Department of Biological Sciences, The University of Toledo
9:50	Coffee Break
10:00	Morgan Sammons	"The Role of DEK in NF-kB/p65 Transcritional Activation" Advisor: Dr. Brian Ashburner, Department of Biological Sciences, The University of Toledo
10:20	Rachel Mintz	"Interferon-Induced mGBP-2 Increases GSTpi Enzyme Activity" Advisor: Dr. Deborah Vestal, Department of Biological Sciences, The University of Toledo
10:40	Andrea Wierman	"The Role of p38 and NF-kB in Pancreatic Cancer" Advisor: Dr. Brian Ashburner, Department of Biological Sciences, The University of Toledo
11:00	Timour Baslan	"Potential Role of Anterior Gradient-2 (hAG2) in Prostate Cancer Progression" Advisor: Dr. Lirim Shemshedini, Department of Biological Sciences, The University of Toledo
11:20	Pizza lunch
12:00	Bruce Benton	"The Induction of Mutations in the Cell Adhesion Gene, mua-10, of C. elegans " Advisor: Dr. John D. Plenefisch, Department of Biological Sciences, The University of Toledo
12:20	Robin Davidson	"Regulation of NF-kB by p38 Map Kinase therough CBP CoActivator Protein" Advisors: Dr. Brian Ashburner, Department of Biological Sciences, The University of Toledo
12:40	Amy Shipley	"Cholinesterase Activities in Songbirds from Farm Fields of Northeast Arkansas" Advisor: Dr. James Bednarz, Department of Biological Sciences, Arkansas State University and Dr. Patricia Komuniecki, Department of Biological Sciences, The University of Toledo
1:00	Eric Cole	"Identification of p38 Phosphorylation Site(s) on CBP" Advisor: Dr. Brian Ashburner, Department of Biological Sciences, The University of Toledo
1:20	Awards ceremony

Abstract 10th URS

Timour Baslan
“Potential Role of Anterior Gradient-2 (Hag2) IN Prostate Cancer Progression”
Advisor: Dr. Lirim Shemshedini, Department of Biological Sciences, The University of Toledo

Prostate cancer is characterized by a transition from an androgen-dependent stage to the more aggressive form of hormone-refractory stage (androgen-independent). The mechanisms that underlie such a cross over are not completely understood. The key to establishing future effective therapies lies in a more complete understanding of the androgen-independent transition. Reported here are novel expression patterns in prostate cancer model cell lines and tissue samples that suggest an involvement of anterior gradient-2 (Hag2) in cancer progression. hAG2 expression was found to be elevated in P100 cells (androgen-independent LNCaP cell lines) as compared to androgen-dependent LNCap cells. Also, hhAG2 was found to be expressed only in malignant carcinoma tissues, while no detectable levels were observed in normal or benign hyperplasia tissue samples. Furthermore, RNAi knockdown of Hag2 in androgen independent cells (p100) resulted in reduced proliferation. Together, our results suggest a potential role for hAG2 in prostate cancer progression from androgen responsiveness to the androgen independent stage.

Bruce Benton
“The Induction of Mutations in the Cell Adhesion Gene, mua-10, of C elegans”

The organism Caenorhabditis elegans is a model for understanding cell adhesion in development and growth. Many of the genes coding for cell adhesion proteins in C. elegans are homologous to similar genes found in humans and therefore, a better understanding of these genes, and the related proteins, in C. elegans may result in a better understanding of cell adhesion in humans. Defects in cell adhesion proteins results in variety of human diseases. Once of the genes coding for a cell adhesion protein in C. elegans is mua-10 (muscle attachment protein), which currently has only a single allele, rh267. This allele results in muscle detachment in the head region resulting in a phenotypic bend caused by the detachment of the muscle from the epidermis on one side and is seen in less than 60 percent of the animals. It is not clear whether this is an unusual or characteristic allele, making the analysis of this allele difficult. The induction of new mutations in this gene may result in a more pronounced phenotype or a higher penetrance allowing for a better understanding of the function of the related protein. I have been performing a non-complementation screen in order to identify additional alleles of this gene.

Erin Cole
"Identification of p38 Phosphorylation Site(s) on CBP”
Advisor: Dr. Brian Ashburner, Department of Biological Sciences, The University of Toledo

The transcription factor Nuclear Factor-kappaB (NF-kB) regulates inflammation, immune response, cell cyle progression and apoptosis. After translocation from the cytoplasm to the nucleus NF-kB promotes gene activity by recruiting transcriptional activators. CREB binding protein (CBP), a histone acetyltransferase (HAT), is an important coactivator of NF-kappaB activity that has been shown to associate with the NF-kB complex to upregulate gene expression. Preliminary evidence also indicates that p38 MAP kinase interacts and phosphorylates CBP. The aim of this research is to characterize these phosphorylation sites. We have identified four of the potential sites and have successfully completed site-directed mutagenesis to help determine whether they are phosphorylated by p38. Our overall goal is to determine the phosphorylation sites of CBP and apply this knowledge to better distinguish p38’s function to regulate NF-kB activity.

3rd URS Photos

Student Presenters

Front Row (L-R): Robin Davidson, Andrea Wierman, Rachael Mintz, Amy Shipley
Back Row (L-R): Dr. Emilio Duran, Dr. Patricia Komuniecki, Morgan Sammons, Eric Cole, Timour Baslan, Bruce Benton, Dr. Deborah Vestal

Winners

Morgan Sammons (1st place), Rachael Mintz (2nd place), Robin Davidson (3rd place)

last updated 29 Dec 2005
please contact brenda.leady@utoledo.edu with comments or concerns

Department of Biological Sciences