The purpose of this R13 proposal is a requests funds for graduate and post doctoral students to attend an international meeting called Enzymology and Molecular Biology of Carbonyl Metabolism. This will be the fifteenth meeting the applicant has organized and it will be held in Lexington, Kentucky July 6-10, 2010. The three enzyme families discussed at the meeting are alcohol dehydrogenase, aldehyde dehydrogenase and carbonyl reductase. The topics range from the physiological role of the enzymes to their involvement in cellular events. Enzyme mechanism and gene regulation are discussed as well as the role of the enzymes in drug metabolism and detoxification reactions. Graduate and post doctoral students have always attended the meeting, as has an occasional undergraduate student, where they present posters while senior scientists are invited to make oral presentations. All are invited to submit a manuscript for publication in a special edition of a journal. No funds are requested to support senior scientist as each of them have to pay their own way. Because of the difficulty in securing research support it is feared that many laboratories will not be able to send qualified students to the meeting as they have in the past. Typically 25 students have attended the meeting along with 50-60 senior scientists. If stipends are available students will be able to attend this meeting where students and senior scientists interact freely and, in the past, formed many collaborations and secured future post doctoral positions.

Public Health Relevance

The """"""""Carbonyl"""""""" meeting is the only meeting devoted to this topic and most of the major scientists investigating the physiological and enzymological importance of carbonyl metabolism attend the meeting. The enzymes are involved in biotransformations, drug and xenobiotic metabolism. The purpose of the proposal is to obtain funds to support graduate and post doctoral student participation at this international meeting.

Agency
National Institute of Health (NIH)
Institute
National Institute on Alcohol Abuse and Alcoholism (NIAAA)
Type
Conference (R13)
Project #
1R13AA019612-01
Application #
7916092
Study Section
Health Services Research Review Subcommittee (AA)
Program Officer
Gentry, Thomas
Project Start
2010-04-15
Project End
2010-09-30
Budget Start
2010-04-15
Budget End
2010-09-30
Support Year
1
Fiscal Year
2010
Total Cost
$30,660
Indirect Cost
Name
Purdue University
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907
Oraldi, M; Saracino, S; Maggiora, M et al. (2011) Importance of inverse correlation between ALDH3A1 and PPAR? in tumor cells and tissue regeneration. Chem Biol Interact 191:171-6
Makia, Ngome L; Bojang, Pasano; Falkner, K Cameron et al. (2011) Murine hepatic aldehyde dehydrogenase 1a1 is a major contributor to oxidation of aldehydes formed by lipid peroxidation. Chem Biol Interact 191:278-87
Hernandez-Tobias, Aida; Julian-Sanchez, Adriana; Pina, Enrique et al. (2011) Natural alcohol exposure: is ethanol the main substrate for alcohol dehydrogenases in animals? Chem Biol Interact 191:14-25
Chakraborty, Mahul; Fry, James D (2011) Drosophila lacking a homologue of mammalian ALDH2 have multiple fitness defects. Chem Biol Interact 191:296-302
Strickland, Kyle C; Holmes, Roger S; Oleinik, Natalia V et al. (2011) Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes. Chem Biol Interact 191:122-8
Endo, Satoshi; Matsunaga, Toshiyuki; Ohta, Chisato et al. (2011) Roles of rat and human aldo-keto reductases in metabolism of farnesol and geranylgeraniol. Chem Biol Interact 191:261-8
Baba, Shahid P; Hellmann, Jason; Srivastava, Sanjay et al. (2011) Aldose reductase (AKR1B3) regulates the accumulation of advanced glycosylation end products (AGEs) and the expression of AGE receptor (RAGE). Chem Biol Interact 191:357-63
Mindnich, Rebekka; Drury, Jason E; Penning, Trevor M (2011) The effect of disease associated point mutations on 5?-reductase (AKR1D1) enzyme function. Chem Biol Interact 191:250-4
Star?evi?, S; Kocbek, P; Hribar, G et al. (2011) Biochemical and biological evaluation of novel potent coumarin inhibitor of 17?-HSD type 1. Chem Biol Interact 191:60-5
Brocker, Chad; Cantore, Miriam; Failli, Paola et al. (2011) Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity. Chem Biol Interact 191:269-77

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