01.08.2014 Views

2008 Proceedings - St. Cloud State University

2008 Proceedings - St. Cloud State University

2008 Proceedings - St. Cloud State University

SHOW MORE
SHOW LESS

You also want an ePaper? Increase the reach of your titles

YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.

Abstracts<br />

Session A All Disciplines Ballroom<br />

Characterization of Truncated Human Class-3 Aldehyde Dehydrogenases (ALDH3A1)<br />

Cyclophosphmide and ifosfamide (also known as oxazaphosphorines) are the most common drugs used to treat breast cancer and various<br />

forms of leukemia. Human class-3 aldehyde dehydrogenase (ALDH3A1) is one of several enzymes responsible for the detoxification of<br />

oxazaphosphorines. ALDH3A1 exhibits polymorphism and so far three isoforms of ALDH3A1 have been identified. One of the forms is a<br />

truncated form. The gene coding for the truncated ALDH3A1 has been cloned into an expression vector and 13 clones containing the<br />

truncated ALDH3A1 gene have been identified. These clones have been further screened to identify truncated ALDH3A1 protein by<br />

immunoblot analysis. We are now in the process of purification of truncated ALDH3A1 protein to further characterize it with reference to its<br />

ability to detoxify cyclophosphamide.<br />

Presentation Index: A29<br />

Time: 9:00 a.m.<br />

Department: Chemistry<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Ogbon, Enite<br />

Sreerama, Lakshmaiah<br />

Human ALDH3A1 Genetic Polymorphism Analysis<br />

Aldehyde dehydrogenases (ALDH) are a family of enzymes that are involved in detoxification of oxazaphosphorines, class of anticancer<br />

drugs. Certain human ALDHs, e.g., ALDH1A1 and ALDH3A1 in particular have been investigated in the process of detoxification of<br />

oxazaphosphorines. Three genetic variants of ALDH3A1 have been identified and their genetic identities have been recently established.<br />

Two of the 3 genetic variants, tentatively named as nALDH3A1 (found in normal tissues), and tALDH3A1 (found in tumor tissues) differ<br />

from each other by 2 bases. The genetic differences in ALDH3A1 also create differences in detoxification of cyclophosphamide and<br />

ifosfamide. Whether these genetic variants are commonly found in general human population is the subject of this investigation. Genetic<br />

polymorphism analysis indicates that these variants are present in normal human populations. The results of these investigations will have<br />

an impact on the therapy, detection, diagnosis, chemoprevention, fundamental molecular biology and/or genesis of cancer.<br />

Presentation Index: A30<br />

Time: 9:00 a.m.<br />

Department: Chemistry<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Antunez, Giovanni<br />

Sreerama, Lakshmaiah<br />

Synthesis and Characterization of Vanadium-naringenin Complexes with Potential Insulin Mimicking Properties<br />

Research on vanadium and flavanoid complexes is paving the way as a promising therapeutic agent in diabetes. Diabetes currently<br />

affects about 170 million people around the world and this number is expected to increase 300 million by the year 2030. Diabetes results<br />

from the lack of insulin secretion due to auto-immune mediated destruction of pancreatic â cells or the resistance in cells to uptake insulin<br />

leading to unregulated blood glucose levels. Research on both vanadium and flavanoids has shown promising insulin mimicking<br />

properties. Naringenin also known as 4', 5, 7 – Trihyroxyflavanone is one such flavanoid. Vandium-naringenin complex, a red – brown<br />

compound, was synthesized by a 2:1 ratio of naringenin to vanadyl acetylacetonate in methanol. Infrared spectroscopy analysis indicated<br />

a shift in the C=O and the C=C to a higher energy peak indicating the coordination of the naringenin to the vanadium center with some<br />

change to the configuration of the complex. Mass spectroscopy analysis showed a peak corresponding to naringenin which indicated the<br />

presence of naringenin in the synthesized compound. A solution study on this compound was also carried out as it allows us to gain a<br />

better understanding of the biochemical behavior of this compound in animal studies. This was done using vanadium NMR spectroscopy<br />

and behavior of this complex in solution was observed.<br />

Presentation Index: A31<br />

Time: 9:00 a.m.<br />

Department: Chemistry<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Fernando, Koshali<br />

Mahroof-Tahir, Mohammad<br />

Fasting-Induced Changes in Plasma Motilin Levels in Dairy Goats<br />

Motilin is a peptide hormone produced by cells in the gastrointestinal tract of many mammals. Its secretion increases during fasting and<br />

the peptide has been implicated in migrating myoelectric complex, a type of smooth muscle contractions that occurs during fasting and that<br />

spans the segment of the gut beginning in the stomach and ending in the terminal ileum. A majority of studies determining the effect of<br />

fasting on motilin has been done in monogastrics. As part of our on-going studies into nutritional regulation of reproduction, we sought to<br />

characterize the effect of fasting on plasma motilin levels in the goat. We tested the hypothesis that fasting will increase plasma motilin in<br />

dairy goats. Six dairy goats were fed ad-libitum for 48 hours and blood samples were obtained from an indwelling catheter for 4 hours at<br />

10 minute intervals. Thereafter, goats were fasted for 48 hours and provided with water and blood samples were obtained for 4 hours at<br />

the same frequency. Plasma motilin concentrations were determined using radioimmunoassay. Results indicate that motilin is secreted in<br />

the dairy goat in a pulsatile manner. Fasting for 48 hours tended to increase (P = .06) motilin levels. These data suggest that fasting for<br />

48 hours may be insufficient to cause a significant increase in plasma motilin in ruminants.<br />

Presentation Index: A32<br />

Time: 9:00 a.m.<br />

Department: Biological Sciences<br />

Project Sponsor(s):<br />

<strong>St</strong>udent Presenter(s): Mboko, Wadzanai<br />

Gazal, Oladele<br />

<strong>St</strong>. <strong>Cloud</strong> <strong>St</strong>ate <strong>University</strong> <strong>St</strong>udent Research Colloquium 26<br />

April 22, <strong>2008</strong>

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!