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H W Goedde

Publications and source records attributed to H W Goedde.

At least 19 recordsLinked to original sources
PubMed1992

Mosaicism in 45,X Turner syndrome: does survival in early pregnancy depend on the presence of two sex chromosomes?

Cytogenetic and molecular genetic findings in 91 patients with Turner syndrome are reported. In 87 patients, chromosome studies were carried out both in lymphocyte and fibroblast cultures. Mosaicism was demonstrated in 58 of these patients (66.7%), whereas only 18 (20.7%) were apparent non-mosaic 45,X, and 11 patients (12.6%) showed non-mosaic structural aberrations of the X chromosome. Among the mosaic cases 16 (18.4% of all patients) displayed a second cell line containing small marker chromosomes. The association of Y-specific chromosomal material with the presence of marker chromosomes was demonstrated in 6 out of 7 mixoploid fibroblast cell lines by polymerase chain reaction amplification and by Southern-blot analysis. The observation of ring formation and morphological variability in vivo and in vitro, and the continuous reduction in the percentage of cells containing marker chromosomes in longterm cultivation experiments indicated an increased instability of marker chromosomes. The findings suggest that in vivo selection of structurally altered sex chromosomes exists. Thus, the observation of apparent non-mosaic 45,X chromosomal complements in liveborn individuals with Turner syndrome does not contradict the hypothesis that some degree of mosaicism is necessary for survival in early pregnancy.

Blotting, Southern↗
PubMed1992

Distribution of ADH2 and ALDH2 genotypes in different populations.

The distribution of the human liver alcohol dehydrogenase, ADH2, and aldehyde dehydrogenase, ALDH2, genotypes in 21 different populations comprising Mongoloids, Caucasoids, and Negroids was determined by hybridization of the amplified genomic DNA with allele-specific oligonucleotide probes. Whereas the frequency of the ADH1(2) allele was found to be relatively high in the Caucasoids, Mexican Mestizos, Brazilian Indios, Swedish Lapps, Papua New Guineans and Negroids, the frequency of the ADH2(2) gene was considerably higher in the Mongoloids and Australian Aborigines. The atypical ALDH2 gene (ALDH2(2)) was found to be extremely rare in Caucasoids, Negroids, Papua New Guineans, Australian Aborigines and Aurocanians (South Chile). In contrast, this mutant gene was found to be widely prevalent among the Mongoloids. Individuals possessing the abnormal ALDH2 gene show alcohol-related sensitivity responses (e.g. facial flushing), have the tendency not to be habitual drinkers, and apparently suffer less from alcoholism and alcohol-related liver disease.

Alcohol Dehydrogenase↗
PubMed1992

Pharmacogenetics of alcohol metabolism and alcoholism.

The pharmacogenetic differences among individuals in their capacity to metabolize ingested alcohol are possibly responsible for the large inter-individual and inter-ethnic variations observed in the outcome of alcohol use and misuse. Based on results of adoption, twin, and family studies it is now widely accepted that the vulnerability to alcoholism is determined by genetic factors as well as by environment. There is a constant search for biological markers and specific genes which could identify individuals genetically predisposed to alcohol abuse and alcoholism. Numerous 'candidate genes' for alcoholism have been suggested including the alcohol metabolizing enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). Both ADH and ALDH exhibit genetic heterogeneity. An atypical form of ADH (ADH2), which contains a variant beta 2 subunit instead of the usual beta 1 subunit, differs substantially from the usual form in its kinetic properties and is found more frequently among the Japanese, Chinese and other Mongoloid populations than in Caucasoids and Negroids. A widely prevalent genetic polymorphism has been observed for ALDH; about 50% of Japanese and Chinese livers possess an inactive ALDH (ALDH2 isozyme) whereas none of the Caucasian or Negroid populations show this isozyme abnormality. These metabolic polymorphisms seem to contribute to differences in the in vivo elimination rate of ethanol and acetaldehyde, and may explain differences in alcohol-related behaviour and its disease outcome. Taken together, Orientals who possess an atypical ALDH2 gene are more sensitive to acute responses to alcohol, tend to be discouraged from drinking alcohol, and consequently are at lower risk of developing alcohol-related disorders. However, more work is needed to support these findings. Recent advances in molecular genetics have made it possible to analyze directly the human genome. This may help in a better understanding of the complex genetic and environmental factors in alcohol abuse by providing prospects for identification of gene loci which may be responsible for predisposition to, and protection from, alcoholism.

Alcohol Dehydrogenase↗
PubMed1991

The ITI system in South Koreans and Iranians analysed by an improved classification procedure. Distribution of alleles and description of "new" phenotypes.

Phenotype and gene frequency distributions of the inter-alpha-trypsin inhibitor (ITI) system were analysed in populations from southern Korea and from Iran. The gene frequencies of the common alleles ITI*I and ITI*2 were 0.532 and 0.422, respectively, in southern Korea, and 0.612 and 0.354, respectively, in Iran. The postulated third allele, ITI*3, was found in the homozygous form. Gene frequencies of this rare allele were calculated to be 0.042 and 0.029 in Korea and Iran, respectively. Two additional rare alleles, ITI*4 and ITI*5, determine further phenotypes found in the population from Taejon (Korea) and Iran, respectively, in combination with the common ITI*2 allele. Gene frequencies of ITI*4 and ITI*5 were calculated to be 0.006 and 0.005, respectively. For phenotype classification, untreated sera were separated by isoelectric focusing (IEF) on polyacrylamide gels followed by immunoblotting.

Alpha-Globulins↗
PubMed1991

Monomorphism of formaldehyde dehydrogenase in different populations.

Blood samples from Koreans, Chinese, Hungarians and Germans were analyzed by isoelectric focusing on polyacrylamide gels and stained for formaldehyde dehydrogenase (FDH) activity. Three activity bands (one major and two minor) were observed in all blood samples studied. No distinct intra- and interpopulation differences were observed in the intensity of the three bands. Human autopsy liver samples also showed a similar three-activity band profile. An additional cathodic band was detected in a single case of autopsy liver extract from a Chinese subject. An apparent identity of FDH with the class III alcohol dehydrogenase was confirmed.

Aldehyde Oxidoreductases↗
PubMed1991

Growth studies on fibroblasts of patients with autosomal recessive Friedreich's ataxia.

Fibroblasts derived from patients with undisputed autosomal recessive Friedreich's ataxia were examined for their growth characteristics including plating efficiency, proliferation curves and cumulative number of population doublings. In comparison to cells of healthy controls, the cells from ataxia patients showed lower plating efficiency, growth rate and number of cumulative population doublings in these parameters. Cells of heterozygotes showed clonal growth and growth curves in the range of the healthy controls.

Biopsy↗
PubMed1990

Identification of three developmentally controlled isoforms of human myosin heavy chains.

A set of cDNA clones coding for myosin heavy chains (MHC) was isolated from a human fetal skeletal muscle library. We have demonstrated by restriction mapping and nucleotide sequence analysis that the cDNAs represent three distinct transcripts, presumably the products of different genes. Furthermore, the pattern of mRNA expression indicates that the corresponding genes are regulated in a tissue-specific and developmental-stage-specific manner. While the cDNA clone gtMHC-V exhibits extensive sequence similarity to the rat beta-myosin heavy chain, the two other clones, gtMHC-F and gtMHC-E are very similar to the rat genes encoding the perinatal and embryonic myosin heavy chains, respectively. The mRNA corresponding to clone gt-MHC-V is highly expressed in heart and adult fast skeletal muscle and to a lesser extent in fetal skeletal muscle and adult slow skeletal muscle. The mRNAs corresponding to clones gtMHC-F and gtMHC-E are abundantly present in fetal skeletal muscle and are not present or barely detectable in heart and adult skeletal muscle.

Adult↗
PubMed1990

[Genetically-induced variability of alcohol metabolism and its effect on drinking behavior and predisposition to alcoholism].

Alcoholism is one of the most challenging current health problems in the Western countries with far-reaching medical, social, and economic consequences. There are a series of factors that interact in predisposing or protecting an individual against alcoholism and alcohol-related disorders. This article surveys the state of our knowledge concerning the biochemical and genetic variations in alcohol metabolism and their implications in alcohol sensitivity, alcohol drinking habits, and alcoholism in different racial/ethnic groups. The major pathway for the degradation of ethanol is its oxidation to hydrogen and acetaldehyde--to which many of the toxic effects of ethanol can be attributed. Variations in alcohol and acetaldehyde metabolism via genetically determined polymorphisms in alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) seem to play an important role in individual and racial differences in acute and chronic reactions to alcohol, alcohol drinking habits, as well as vulnerability to organ damage after chronic alcohol abuse. Alcohol sensitivity and associated discomfort symptoms accompanying alcohol ingestion may be determinental for the significantly low incidence of alcoholism among the Japanese, Chinese and other Orientals of Mongoloid origin. An abnormal ALDH isozyme has been found to be widely prevalent among individuals of the Mongoloid race and is mainly responsible for the acute sensitivity to alcohol commonly observed in this race. Persons sensitive to alcohol by virtue of their genetically controlled ALDH isozyme deficiency may be discouraged from drinking large amounts of alcohol in their daily life due to the initial adverse reaction experienced after drinking alcohol. Indeed, a significantly low incidence of the mitochondrial ALDH isozyme deficiency has been observed in alcoholics as compared to psychiatric patients, drug dependents and healthy controls in Japan. How far any variation in ADH and/or ALDH activity among individuals of Caucasian origin will have similar effects has yet to be studied.

Alcohol Dehydrogenase↗
PubMed1990

Characterization of long-term cell cultures of human chorion villi and fibroblasts using antibodies to cytoskeletal proteins.

In long-term cultures of chorion villi the expression of cytoskeletal proteins--vimentin, cytokeratin, actin, tropomyosin and vinculin--was studied using immunoreactivity to antibodies. Vimentin was detected in all cells of chorionic villi cultures despite their morphological appearance. In comparison to fibroblast cultures from human skin biopsies with bundle-like vimentin structures, chorionic villi cells showed fine ramified vimentin filaments. Some of the chorionic villi cells with typical fibroblastoid appearance also had cytokeratin filaments. No differences were observed in the distribution of vinculin. Tropomyosin structure and actin filaments could be detected in cultures of chorionic villi whereas fibroblasts showed only an intense diffuse staining.

Antibodies, Monoclonal↗
PubMed1989

Genotyping of mitochondrial aldehyde dehydrogenase in blood samples using allele-specific oligonucleotides: comparison with phenotyping in hair roots.

Deficiency of mitochondrial aldehyde dehydrogenase (ALDH I) is an inborn error of metabolism that is responsible for acute alcohol sensitivity (flushing response) observed only in Orientals of Mongoloid origin. Our previous studies using electrophoretic enzyme detection have shown that this deficiency is prevalent among Japanese, Chinese, and other Orientals. We report here the genotyping of ALDH I locus in blood samples of 218 South Korean individuals by means of hybridization analysis with allele-specific oligonucleotide probes and enzymatically amplified human genomic DNA. The results of genotyping are compared with the phenotype analysis in hair roots of the same individuals. Among 62 apparently deficient phenotypes, 58 heterozygote and 4 homozygote deficient genotypes were observed.

Aldehyde Dehydrogenase↗
PubMed1989

Inheritance of mitochondrial aldehyde dehydrogenase: genotyping in Chinese, Japanese and South Korean families reveals dominance of the mutant allele.

Genotyping of mitochondrial aldehyde dehydrogenase (ALDH I) was performed in enzymatically amplified DNA of 20 Chinese, Japanese and South Korean families (85 individuals) and in 113 unrelated persons by employing allele-specific oligonucleotide probes and dot blot hybridization. Genotyping individuals with phenotypic deficiency of ALDH I activity always showed the presence of at least one mutant allele. The data are compatible with a model assuming dominant inheritance of the mutant allele, which we have previously suggested on the basis of a population study.

Aldehyde Dehydrogenase↗
PubMed1989

Red cell enzyme and serum protein polymorphisms in South Korea.

Two population groups in South Korea, one from Kwangju and one from Kangreung, were studied in regard to the erythrocyte enzyme polymorphisms GPT, ACP, GLO, ESD, 6PGD, ADA, AK, PGP and subtypes of PGM1 as well as regarding the serum protein variants of C3, HP, BF, PLG, AMY and the subtypes of GC, TF and PI. The results were compared with data of the population groups from the area of Cheju Island, Taejon and Seoul. The Korean population showed a rather high degree of genetic homogeneity.

Adolescent↗
PubMed1989

Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme.

Human red cell aldehyde dehydrogenase (ALDH) resembles the liver cytosolic isozyme in numerous physicochemical properties. This study was undertaken to establish the structural relationship between the erythrocyte and liver ALDH isozymes. The purified red cell ALDH was S-(14C)-carboxymethylated, and cleaved with trypsin. The tryptic digest was fractionated using Sephadex and reversed-phase chromatography. All peptides analyzed were identified within the liver cytosolic enzyme structure. In each case the sequence obtained corresponds exactly to a segment from the human liver cytosolic ALDH. Thus, the erythrocyte enzyme, by virtue of its chemical and structural identity with the liver cytosolic enzyme, may serve as a suitable peripheral enzyme model to understand the cause and mechanism of alcohol abuse-related changes in liver cytosolic ALDH that has been found to be reduced in alcoholics.

Aldehyde Dehydrogenase↗