Comparative analysis of Xenopus tropicalis hepcidin I and hepcidin II genes

Genomic organization and tissue-specific expression of hepcidin in the pacific mutton hamlet, Alphestes immaculatus (Breder, 1936)

“…The basal hepcidin expression analysis showed liver as the highest relative expression tissue, and since the initial discovery of hepcidin in humans, in almost all vertebrates, liver is the tissue that has the highest hepcidin expression level [1,8,31,32]. One exception was observed in the P. crocea, where liver was the lowest expression tissue and kidney the highest [19].…”

Identification, sequencing, and cellular localization of hepcidin in guinea pig (Cavia porcellus)

“…It was first isolated from human serum and urine (Krause et al 2000, Park et al 2001. Subsequently, a number of hepcidin genes were identified, both from mammals like mouse (Pigeon et al 2001, Ilyin et al 2003, rats, and dogs (Fry et al 2004) and lower-vertebrates like amphibians (Hu et al 2008) and fishes (Shike et al 2002, Douglas et al 2003, Bao et al 2005, Chen et al 2005, Hirono et al 2005, Kim et al 2005, Cuesta et al 2007). All isolated hepcidin sequences share a highly homologous amino acid sequence and evolutionary conserved cysteine residue pattern, which are characteristic for antimicrobial peptides, leading to the formation of three to four disulfide bridges that might be necessary for the antimicrobial function of hepcidin.…”

Anuran adaptations to climatic stress : immune responses and the SMAD family in the wood frog, Rana sylvatica, and the African clawed frog, Xenopus laevis

“…While only one form of hepcidin exists in humans, multiple forms have been identified in various fish species and two forms (hepcidin I and hepcidin II) have been found inX. tropicalis (Hirono et al, 2005;Kim et al, 2005;Huang et al, 2007;Yang et al, 2007;Hu et al, 2008). In the present study, two differentially regulated hepcidin cDNA sequences were amplified from X. laevis liver whereas previously, only one form was thought to exist based on the EST tag CB199190 (Hu et al, 2006).…”

“…The differential regulation of hepcidin I and II in response to dehydration suggests the possibility of a functional divergence between the hepcidin forms inX laevis. This idea has been presented before in light of the multiple copies of hepcidin found in fish species as well as X. tropicalis (Cho et al, 2009;Wang et al, 2009;Hu et al, 2008;Padhi & Verghese, 2007). InX tropicalis, hepcidin II was suggested to be ironregulatory whereas hepcidin I was thought to function as an antimicrobial peptide .…”

“…This gene conservation between frog species is consistent with the high degree of structural conservation previously found between all hepcidin forms. In fact, in contrast to other antimicrobial peptides, hepcidin is highly conserved throughout vertebrate evolution (Shi and Camus, 2006;Padhi and Verghese, 2007;Hu et al, 2008).…”