Abstract

The purpose of this renewal for an ADAMHA Research Scientist Award is to enable the applicant to have the time to expand his research interest to include the applications of molecular biological techniques to study alcohol related problems. These problems primarily will be related to the elucidation of the active site of liver mitochondrial aldehyde dehydrogenase and to an understanding of why the enzyme is N-terminally acetylated. The other major aspect will be the transport of newly synthesized enzyme into mitochondria with an emphasis on the signal peptide and the membrane receptor. The effect of ethanol on the process will be studied at the membrane level. Yeast will also be used as a model to mimic the effects of ethanol on the membrane and hence transport problem.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute on Alcohol Abuse and Alcoholism (NIAAA)
Type
Research Scientist Award (K05)
Project #
5K05AA000028-15
Application #
2042672
Study Section
Biochemistry, Physiology and Medicine Subcommittee (ALCB)
Project Start
1983-12-01
Project End
1993-11-30
Budget Start
1992-12-01
Budget End
1993-11-30
Support Year
15
Fiscal Year
1993
Total Cost
Indirect Cost

  Institution

Name
Purdue University
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907

  Publications

Hurley, T D; Yang, Z; Bosron, W F et al. (1993) Crystallization and preliminary X-ray analysis of bovine mitochondrial aldehyde dehydrogenase and human glutathione-dependent formaldehyde dehydrogenase. Adv Exp Med Biol 328:245-50
Sanny, C G; Weiner, H (1987) Inactivation of horse liver mitochondrial aldehyde dehydrogenase by disulfiram. Evidence that disulfiram is not an active-site-directed reagent. Biochem J 242:499-503
Weiner, H; McMichael, M; Lindahl-Hellstrom, E et al. (1987) Use of polyclonal antibodies to study properties of mammalian aldehyde dehydrogenases. Alcohol Alcohol Suppl 1:187-91
Weiner, H (1987) Subcellular localization of acetaldehyde oxidation in liver. Ann N Y Acad Sci 492:25-34
McMichael, M; Hellstrom-Lindahl, E; Weiner, H (1986) Identification and selective precipitation of human aldehyde dehydrogenase isozymes using antibodies raised to horse liver aldehyde dehydrogenase isozymes. Alcohol Clin Exp Res 10:323-9
Tank, A W; Deitrich, R A; Weiner, H (1986) Effects of induction of rat liver cytosolic aldehyde dehydrogenase on the oxidation of biogenic aldehydes. Biochem Pharmacol 35:4563-9
Svanas, G W; Weiner, H (1985) Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver. Arch Biochem Biophys 236:36-46
Svanas, G W; Weiner, H (1985) Use of cyanamide to determine localization of acetaldehyde metabolism in rat liver. Alcohol 2:111-5
Hellstrom-Lindahl, E; Weiner, H (1985) Effects of disulfiram on the oxidation of benzaldehyde and acetaldehyde in rat liver. Biochem Pharmacol 34:1529-35
Svanas, G W; Weiner, H (1985) Enzymatic requirement for cyanamide inactivation of rat liver aldehyde dehydrogenase. Biochem Pharmacol 34:1197-204