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• W821566695 abstract "(abs. nos. S5-3-S5-6) ISBRA-88 ABSTRACTS USE OF DNA PROBES TO INVESTIGATE MOLECULAR GENE- TIC CHANGES IN ALCOHOL DEHYDROGENASE (ADH) AND LINKED GENES IN HUMAN HEPATOMAS. Moyra Smith*,K. Yoshiyama*. J. Murraytf.K. Buetow+ •University of California,Irvine, #Univ. of Iowa, +Fox Chase Cancer Center, Philadelphia, PA. Availability of DNA probes has allowed us to define the chromosomal assignment, genetic vari- ation and genetic linkage relationships of human ADH. Gene probes have also been used to examine the molecular genetic basis of altered expression of ADH in different tissues at different stages of fetal development and in human hepatomas. We mapped ADH genes to the region 4q21-4q25. ADH genes are genetically closely linked to the epi- dermal growth factor (EGF) gene. ADH genes are also linked at a greater distance to the genes for albumin and alpha fetoprotein. These linkage relationships are of particular interest in light of the altered expression of albumin, alpha feto- protein and ADH In hepatomas and the important role of epidermal growth factor and its receptor (EGFR) in the growth and regeneration of liver cells. Our studies demonstrated that deletions occur on one member of the chromosome 4 pair in a significant proportion of hepatomas leading to allele loss of ADH and/or EGF and certain other 4Q markers. We are examining other regions of the genome of hepatomas for allele loss. At this time, the only other chromosome region in which we have demonstrated allele loss is in the EGFR region, chromosome 7pl. Induclble, NADP-speclflc Rat Aldehyde Dehydrogeoases: A Novel Structural Type. John Hempel, Kim Harper and Ronald Lindahl. Univ. of Pittsburgh and Univ. of Alabama NADP-speclflc rat AlDHs induced in hepato- cellular carcinoma and by TCDD treatment are Identical, 452 anino acid chains. Relative to 500-resldue NAD-AlDHs of hunan/equine/bovine liver cytosol/mltochondria (with nlnlnun ~70Z positional identity) the N-terainus is at position 57 and the C-terainus extends 16 residues beyond that of NAD'AIDH. Vs. human Ej identities at 127/437 positions (29Z) are achieved after placement of 9 gaps (totalling 15 positions) in NADP'AIDH and 2 gaps (7 positions) in E}. Identltes are well spread across the alignment:, with some degree of clustering in positions 186-245 of E j . This segment encompasses presently identified active site residues of NAD'AIDH, Cys-302 and Glu-268, and the putative coenzyme-binding fold identified by Gly distributions. Only one other cystelne residue Is conserved vs. Ej or Z^: Cys-275. Many predicted reverse turns occur in comparable segments, some not conserved in sequence. Con- servation of tertiary structure is also implicated by the high conservation of glycine residues (20/48 In Ej), often required sterically for chain bending. These characteristics indicate a clear but distant relationship between NADP-AlDHs and NAD'AIDH and reveal a new class of this enzyme. Supported by AA06985 BIOCHEMICAL AND MOLECULAR GENETIC STUDIES RELATED TO CHANGES IN ALDEHYDE DEHYDROGENASE ISOZYMES IN ALCOHOLISM D.P. Agarwal and H. W. Goedde, Institute of Human Genetics, University of Hamburg, Hamburg 54, Fed. Rep. Germany A comparative biochemical and molecular genetic study of human liver and erythrocyte ALDH was undertaken to elucidate the cause and mechanism underlying the loss in ALDH enzyme activity in alcoholism. Wo have previously reported that there is a considerable similarity in biochemi- cal and molecular properties of human liver cytosolic aldehyde dehydrogenase and erythrocyte aldehyde dehydrogenase (ALDH). According to our earlier studies a significant depletion in liver and erythrocyte ALDH activity takes place in chronic alcohol abuse. A lack of correlation between reduced erythxocyto ALDH activity and the degree of alcohol-related liver damage was observed. The results to be presented indicate that altered catalytic, molecular and inmunological properties of red cell ALDH in acute and chronic alcohol abuse represent an inactivation of the enzyme molecules and not a suppressed synthesis of the enzyme. An involvement of a disturbed glutathione metabolism in the loss of ALDH acti- vity in alcohol abuse is currently being in- vestigated since our preliminary results indicate a significantly lower red cell glutathione concentration in alcoholics. Downloaded from by guest on May 21, 2015 MOLECULAR GENETICS OF ALCOHOL-METABOLIZING ENZYMES: Akira Yoshida, Department of Biochemical Genetics, Beckman Research Institute of the City of Hope, Duarte, California 91010, USA Three genes for ADH (Class I) are on chro- mosome-4. These genes have a similar organization and a high degree of resemblance (about 95X) in their coding sequences, suggesting the recent divergence of these loci. However, each of the three subunits and the Oriental-type subunit has unique structures in the vicinity of the active kinetic properties. The size heterogeneity and developmental changes of expression were observed in their mRNA. The gene for the cytosolic ALDHj is on chromosome-9, and that for the mitochrondrial ALDH2 is on chromosome-12. The degree of resem- blance between the two is 66% at the cDNA level and 69X at the protein level. The ALDH2 gene is about 45 kbp long and contains 13 exons which encode 517 amino acid residues. The Oriental atypical ALDH2,, associated with diminished catalytic activity, has a base transition in the 12th exon, resulting in a Glu-*-Lys substitution at the 14th position of the COOH-terminal. Using specific synthetic oligonucleotide probes, geno- types of the ADH and ALDH loci of Japanese with alcoholic liver diseases were determined. Strong association of the diseases with ALDH^ was found. Genetic background of other alcohol-related problems can be explored by this approach. All" @default.
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• W821566695 date "1988-01-01" @default.
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• W821566695 title "USE OF DNA PROBES TO INVESTIGATE MOLECULAR GENETIC CHANGES IN ALCOHOL-DEHYDROGENASE (ADH) AND LINKED GENES IN HUMAN HEPATOMAS" @default.
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