Source:http://linkedlifedata.com/resource/pubmed/id/10858567
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rdf:type | |
lifeskim:mentions |
umls-concept:C0008633,
umls-concept:C0017262,
umls-concept:C0017428,
umls-concept:C0025914,
umls-concept:C0026809,
umls-concept:C0029246,
umls-concept:C0030016,
umls-concept:C0035331,
umls-concept:C0185117,
umls-concept:C0332307,
umls-concept:C1332076,
umls-concept:C1516050,
umls-concept:C1707455,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
2000-9-27
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pubmed:abstractText |
Retinaldehyde dehydrogenase (RALDH) isozymes catalyze the formation of an essential developmental modulator, retinoic acid. We determined the structural organization of mouse type-2 Raldh2 by isolation of overlapping genomic DNA clones from a phage library. The gene consists of 14 exons spanning more than 70 kb of genomic DNA. It was localized to mouse chromosome 6. Northern blot analysis revealed testis-specific expression. The RALDH genes belong to the aldehyde dehydrogenase (ALDH) multi-gene family. Three types of RALDH genes (e.g. human ALDH1/mouse Ahd2/rat RalDH(I), human ALDH11/mouse Raldh2/rat RalDH(II) and human ALDH6) are highly conserved during evolution, sharing about 70% identity at the amino acid level between any two gene types and 90% identity between any two mammalian genes of the same type. Different RALDH types show specific tissue and developmental expression patterns, suggesting (i) a regulatory mechanism of retinoic acid synthesis via different promoters of RALDH genes, and (ii) distinctive biological roles of different isozymes in embryogenesis and organogenesis.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
1492
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
289-93
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10858567-Aldehyde Oxidoreductases,
pubmed-meshheading:10858567-Amino Acid Sequence,
pubmed-meshheading:10858567-Animals,
pubmed-meshheading:10858567-Base Sequence,
pubmed-meshheading:10858567-Chromosome Mapping,
pubmed-meshheading:10858567-Chromosomes,
pubmed-meshheading:10858567-DNA,
pubmed-meshheading:10858567-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:10858567-Genome,
pubmed-meshheading:10858567-Humans,
pubmed-meshheading:10858567-Mice,
pubmed-meshheading:10858567-Molecular Sequence Data,
pubmed-meshheading:10858567-Retinal Dehydrogenase,
pubmed-meshheading:10858567-Sequence Homology, Amino Acid,
pubmed-meshheading:10858567-Tissue Distribution
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pubmed:year |
2000
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pubmed:articleTitle |
Mouse type-2 retinaldehyde dehydrogenase (RALDH2): genomic organization, tissue-dependent expression, chromosome assignment and comparison to other types.
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pubmed:affiliation |
Division of Molecular Medicine, Beckman Research Institute of the City of Hope, 1450 E. Duarte Road, Duarte, CA 91010, USA. lhsu@coh.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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