Retinoic acid biosynthetic enzyme ALDH1 localizes in a subset of retinoid-dependent tissues during xenopus development.
Control of retinoic acid synthesis in vertebrate organisms is undoubtedly important for regulating the numerous retinoid signaling events which occur during development. The mechanisms which accomplish this task involve enzymes such as class I aldehyde dehydrogenase (ALDH1), which has recently been found to be conserved from amphibians to mammals and which functions as a retinoic acid biosynthetic enzyme in vivo. Here we have found that Xenopus ALDH1 mRNA and protein is expressed in a subset of retinoid-dependent tissues which develop shortly after neurulation during the tail bud stages. ALDH1 mRNA was first clearly detectable by in situ hybridization in stage 28 tail bud embryos localized in the olfactory placode and pronephros, and at stage 35 mRNA was also detected in the pronephric duct. Antibodies were generated against Xenopus ALDH1, and immunohistochemistry was used to demonstrate that ALDH1 protein accumulates in the olfactory placode, pronephros, and dorsal retina at stage 28, and additionally in the lens placode and pronephric duct at stage 35. Neither ALDH1 mRNA nor protein was detected in the posterior region of Xenopus embryos during the tail bud stages. In contrast to neurula stage embryos in which retinoic acid is distributed in an anteroposterior gradient with the high end posteriorly, we found that tail bud stage embryos have retinoic acid present in significant levels in both the head and trunk regions, but with no detection in the posterior region. These findings are consistent with ALDH1 contributing to retinoic acid synthesis needed for development of certain head structures (olfactory placodes, dorsal retina, lens placode) and certain trunk structures (pronephros and pronephric duct). Dev Dyn 1999;215:264-272.
Gene Regulation Program, Burnham Institute, La Jolla, California 92037, USA.
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D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000080924:Aldehyde Dehydrogenase 1 Family; D000818:Animals; D004625:Embryo, Nonmammalian / Q000033:anatomy & histology / Q000201:enzymology; D005136:Eye Proteins / Q000378:metabolism; D005260:Female; D018507:Gene Expression Regulation, Developmental; D017403:In Situ Hybridization; D007527:Isoenzymes / Q000378:metabolism*; D007668:Kidney / Q000196:embryology / Q000201:enzymology; D008297:Male; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009833:Olfactory Pathways / Q000196:embryology / Q000201:enzymology; D009928:Organ Specificity; D012333:RNA, Messenger / Q000096:biosynthesis; D012160:Retina / Q000196:embryology / Q000201:enzymology; D050697:Retinal Dehydrogenase; D014212:Tretinoin / Q000378:metabolism*; D014982:Xenopus laevis / Q000196:embryology* / Q000235:genetics / Q000378:metabolism
D005136:Eye Proteins; D007527:Isoenzymes; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D014212:Tretinoin; D000080924:Aldehyde Dehydrogenase 1 Family; D000444:Aldehyde Dehydrogenase; D050697:Retinal Dehydrogenase