Hartman Institute for Therapeutic Organ Regeneration

Cloning and expression pattern of the Xenopus erythropoietin receptor.

TitleCloning and expression pattern of the Xenopus erythropoietin receptor.
Publication TypeJournal Article
Year of Publication2006
AuthorsYergeau DA, Schmerer M, Kuliyev E, Evans T, Mead PE
JournalGene Expr Patterns
Volume6
Issue4
Pagination420-5
Date Published2006 Apr
ISSN1567-133X
KeywordsAmino Acid Motifs, Amino Acid Sequence, Animals, Blotting, Northern, Cloning, Molecular, Codon, Initiator, Cysteine, Databases, Factual, Embryo, Nonmammalian, Exons, Expressed Sequence Tags, Gene Expression Regulation, Developmental, In Situ Hybridization, Introns, Molecular Sequence Data, Protein Structure, Tertiary, Receptors, Erythropoietin, Reverse Transcriptase Polymerase Chain Reaction, RNA, Messenger, Sequence Homology, Amino Acid, Tyrosine, Xenopus
Abstract

Cytokine signaling plays an important role in the survival and differentiation of vertebrate hematopoietic cells. In red blood cells, erythropoietin is a key component of the differentiation program and maintains the homeostasis of the erythroid compartment. In the adult, anemia stimulates high levels of circulating erythropoietin that drives erythropoiesis to restore normal levels of red blood cells in circulation. Erythropoietin activates the erythropoietin receptor on immature red blood cell precursors to promote their survival and differentiation. Although extensively studied in mammalian systems, a complete understanding of the function of the erythropoietin receptor during primitive erythropoiesis has been lacking. To address this problem, we have cloned the Xenopus laevis erythropoietin receptor in order to further understand the development of primitive erythropoiesis. The amphibian erythropoietin receptor shares 33% amino acid sequence identity with the mammalian erythropoietin receptors and contains the conserved extracellular ligand binding and fibronectin domains, the WSXWS motif common to cytokine receptors, and several tyrosine phosphorylation sites located on the intracellular domain of the receptor. Expression of the erythropoietin receptor is first detected by in situ hybridization in the ventral blood island during tailbud stages.

DOI10.1016/j.modgep.2005.09.004
Alternate JournalGene Expr Patterns
PubMed ID16378761

Weill Cornell Medicine
Hartman Institute for Therapeutic Organ Regeneration
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