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Heme metabolism enzymes are dynamically expressed during Xenopus embryonic development

JIANLI SHI, WENYAN MEI, JING YANG

Center for Cell & Developmental Biology, the Research Institute at Nationwide Children’s Hospital, Department of Pediatrics, The Ohio State University, 700 Children’s Drive, Columbus, OH 43205, USA.
Address correspondence to: Jing Yang. WA2013/CRI, 700 Children’s Dr. Columbus, Oh 43205, USA. E-mail: jing.yang@nationwidechildrens.org

BIOCELL 2008, 32(3), 259-263. https://doi.org/10.32604/biocell.2008.32.259

Abstract

As the key component of many hemoproteins (heme-containing proteins), heme is involved in a broad range of biological processes. Enzymes required for heme biosynthesis and degradation pathways are evolutionarily conserved. While heme metabolism has been studied extensively, the expression of heme metabolism enzymes during development has not been described. Here, we report that all heme biosynthases and two heme oxygenases, which initiate heme degradation, are dynamically expressed during Xenopus embryonic development. All heme synthases, with the exception of aminolevulinic acid synthase 2, are maternally expressed. At neurula stage, heme synthases are expressed in the developing neural tissue and in migrating neural crest cells. At the swimming tadpole stage, expression of heme synthases can be detected in multiple lineages, including eyes, neural crest cells, developing central nervous system, ventral blood island, pronephron, and pronephric tubule. Similar to heme synthases, heme oxygenases are expressed maternally. Zygotic expression of heme oxygenases is mainly restricted to the developing neural and neural crest lineages. Unlike heme synthases, heme oxygenases are not expressed in the ventral blood island and are expressed at a very low level in the pronephron and pronephric tubule. This indicates that heme metabolism may play important roles during development.

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SHI,, J. (2008). Heme metabolism enzymes are dynamically expressed during Xenopus embryonic development. BIOCELL, 32(3), 259–263. https://doi.org/10.32604/biocell.2008.32.259

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