Immunohistochemical localization of alcohol dehydrogenase in human kidney, endocrine organs and brain

Bühler, Rolf E.; Pestalozzi, D; Hess, M. W.; Wartburg, J. P. von

doi:10.1016/0091-3057(83)90147-8

Cited by 55 publications

(30 citation statements)

References 16 publications

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“…Also in line with expectations was the high expression of myoglobin in heart and alcohol dehydrogenase-1 in liver and kidney (Fig. 6A) consistent with the known expression pattern of this metabolic enzyme (34,35). Fig.…”

Section: Figsupporting

confidence: 72%

Quantitative Profile of Five Murine Core Proteomes Using Label-free Functional Proteomics

Cutillas

Vanhaesebroeck

2007

Molecular & Cellular Proteomics

106

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Analysis of primary animal and human tissues is key in biological and biomedical research. Comparative proteomics analysis of primary biological material would benefit from uncomplicated experimental work flows capable of evaluating an unlimited number of samples. In this report we describe the application of label-free proteomics to the quantitative analysis of five mouse core proteomes. We developed a computer program and normalization procedures that allow exploitation of the quantitative data inherent in LC-MS/MS experiments for relative and absolute quantification of proteins in complex mixtures. Important features of this approach include (i) its ability to compare an unlimited number of samples, (ii) its applicability to primary tissues and cultured cells, (iii) its straightforward work flow without chemical reaction steps, and (iv) its usefulness not only for relative quantification but also for estimation of absolute protein abundance. We applied this approach to quantitatively characterize the most abundant proteins in murine brain, heart, kidney, liver, and lung. We matched 8,800 MS/MS peptide spectra to 1,500 proteins and generated 44,000 independent data points to profile the ϳ1,000 most abundant proteins in mouse tissues. This dataset provides a quantitative profile of the fundamental proteome of a mouse, identifies the major similarities and differences between organ-specific proteomes, and serves as a paradigm of how label-free quantitative MS can be used to characterize the phenotype of mammalian primary tissues at the molecular level. Molecular & Cellular Proteomics 6: 1560 -1573, 2007.Experiments on immortalized cell lines have resulted in the generation of a vast amount of information on the biological and biochemical processes that govern the function of cultured cells. However, discerning the mechanisms by which genes control mammalian physiology in vivo may only be achieved by investigations that involve the use of animal models of which the laboratory mouse (Mus musculus) offers many advantages (1). There is a wealth of resources related to the molecular biology of mouse cells that have benefited from genomics, transcriptomics, and, more recently, proteomics projects aimed at profiling the molecular composition of murine tissues (2-4). The generation of gene-targeted mice is particularly useful in advancing our understanding of how genes control fundamental processes of mammalian physiology (e.g. Refs. 5-9).Once created, finding the phenotype of a gene-targeted strain of mice is not a trivial task (1, 10). Several years are needed to fully characterize phenotypic alterations, and subtle phenotypes often go unnoticed. Robust and high throughput methods for profiling the proteomes of primary tissues in a quantitative fashion may expedite the search for phenotypic changes in gene-targeted and other animal models. Insights gained by powerful methods for the molecular characterization of primary tissues could also direct classical physiological experiments, reduce the number of experimental an...

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Section: Figsupporting

confidence: 72%

Quantitative Profile of Five Murine Core Proteomes Using Label-free Functional Proteomics

Cutillas

Vanhaesebroeck

2007

Molecular & Cellular Proteomics

106

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“…Recently, in our review we suggested indirect mechanisms by which alcohol disrupts the EMPS . However, based on increasing evidences (Deitrich et al, 2006;Wick et al, 1998;Quertemont 2004;Buhler et al, 1983), a direct disruption might also be possible, especially, if we consider the possibility that receptors of neuromediators might have "alcohol pockets-receptors". It is reported that glycine and GABAA receptors may harbor specific pockets for alcohol .…”

Section: Pathways Of Alcohol's Action On the Error Monitoring And Promentioning

confidence: 99%

“…Indirect effect of alcohol on the processing capacity of the basal ganglia by affecting other brain areas connected to the basal ganglia; c. Direct effect on neuromediators that modulate the processing of information in the basal ganglia and/or associated brain pathways; d. Action of alcohol metabolites (acetaldehyde; acetate; protein, lipid, enzyme & DNA adducts of alcohol) on the processing of information in the basal ganglia and/or associated brain pathways. The brain might contain alcohol metabolizing enzymes such as ADH-1, ADH-2, ADH-3 (might play little or no role), CYP P4502E1 (Quertemont 2004;Buhler et al, 1983), although there might be a huge genetic variance. It important to note that injection of acetate into the brain causes significant decrease in motor function (Deitrich et al, 2006).…”

Section: Pathways Of Alcohol's Action On the Error Monitoring And Promentioning

confidence: 99%

“…Alcohol is one of the psychotic substances that affect the functions of the basal ganglia (Goldstein et al, 2007;Goodlett & Horn 2001). Many substances that cross the blood brain barrier can affect the normal functioning of the basal ganglia either indirectly or directly (Buhler et al, 1983). The direct effect occurs, if the substances reach the basal nuclei.…”

Section: Introductionmentioning

confidence: 99%

“…The indirect effect happens when pathways linking other brain regions (sub-cortical pathways) are affected. In addition, the metabolic products of these substances can exert their effect on the neurons of the basal ganglia or on the pathways linking the basal ganglia (Buhler et al, 1983;Deitrich et al 2006;Salvador & Alfredo 2010).…”

Section: Introductionmentioning

confidence: 99%

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Drug‐metabolizing enzymes (DMEs) are primarily expressed in the liver but their role in the extrahepatic tissues such as gastrointestinal tract (GIT), pulmonary, excretory, nervous, cardiovascular system, and skin cannot be neglected. Generally, the expression of DMEs in extrahepatic tissues is quantitatively lower than that in the liver, but there are a few enzymes such as CYP1A1, CYP1B1, CYP2F1, and CYP2U1 that are more abundant in extrahepatic organs. As many extrahepatic organs are portals for administered drugs, DMEs expressed in these organs can be responsible for significant metabolism, leading to first‐pass effects and lower bioavailability. Extrahepatic DMEs are also involved in bioactivation of prodrugs and formation of reactive metabolites that may interact with cellular components, resulting in organ‐specific toxicity. Activity and expression of extrahepatic DMEs is often altered by coadministered drugs, leading to drug–drug interactions. Expression of DMEs in living beings affected by a host of environmental and genetic factors such as genetic polymorphism, age, gender, pathophysiological conditions, inborn errors in metabolism, food habits, and environmental pollutants, contributing to varied drug effects and idiosyncratic toxicities.

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Immunohistochemical localization of alcohol dehydrogenase in human kidney, endocrine organs and brain

Cited by 55 publications

References 16 publications

Quantitative Profile of Five Murine Core Proteomes Using Label-free Functional Proteomics

Quantitative Profile of Five Murine Core Proteomes Using Label-free Functional Proteomics

Basal Ganglia and the Error Monitoring and Processing System: How Alcohol Modulates the Error Monitoring and Processing Capacity of the Basal Ganglia

Extrahepatic Drug‐Metabolizing Enzymes and Their Significance

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