|aldehyde dehydrogenase 3 family, member B1||OKDB#: 4306|
|Synonyms:||ALDH4, ALDH7, FLJ26433, FLJ34710,||Locus:||11q13 in Homo sapiens|
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|General Comment||NCBI Summary: The aldehyde dehydrogenases are a family of isozymes that may play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. This particular gene spans about 20 kb of genomic DNA and is composed of 9 coding exons. The gene is highly expressed in kidney and lung. The functional significance of this gene as well as the cellular localization of its product are presently unknown. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq]|
|Expression regulated by|
|Comment||Aldehyde Dehydrogenase 3B1 (ALDH3B1): Immunohistochemical Tissue Distribution and Cellular-specific Localization in Normal and Cancerous Human Tissues. Marchitti SA et al. Aldehyde dehydrogenase (ALDH) enzymes are critical in the detoxification of endogenous and exogenous aldehydes. Our previous findings indicate that the ALDH3B1 enzyme is expressed in several mouse tissues and is catalytically active towards aldehydes derived from lipid peroxidation, suggesting a potential role against oxidative stress. The aim of this study was to elucidate by immunohistochemistry the tissue, cellular and subcellular distribution of ALDH3B1 in normal human tissues and in tumors of human lung, colon, breast, and ovary. Our results indicate that ALDH3B1 is expressed in a tissue-specific manner and in a limited number of cell types, including hepatocytes, proximal convoluted tubule cells, cerebellar astrocytes, bronchiole ciliated cells, testis efferent ductule ciliated cells, and histiocytes. ALDH3B1 expression was up-regulated in a high percentage of human tumors (lung > breast = ovarian > colon). Increased ALDH3B1 expression in tumor cells may confer a growth advantage or be the result of an induction mechanism mediated by increased oxidative stress. Subcellular localization of ALDH3B1 was predominantly cytosolic with the exception of normal human lung and testis in which localization appeared membrane-bound or membrane-associated. The specificity of ALDH3B1 distribution may prove to be directly related to the functional role of this enzyme in human tissues.|
|Genomic Region||show genomic region|
|Phenotypes and GWAS||show phenotypes and GWAS|
|created:||June 2, 2010, 6:41 a.m.||by:||
|last update:||June 2, 2010, 6:42 a.m.||by:||hsueh email:|
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