Catfish hepcidin gene is expressed in a wide range of tissues and exhibits tissue-specific upregulation after bacterial infection

Bao, Baolong; Peatman, Eric; Li, Ping; He, Chongbo; Liu, Zhanjiang

doi:10.1016/j.dci.2005.03.006

Cited by 163 publications

(94 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These data are in agreement with the hepcidin tissue distribution in human (Krause et al 2000, Park et al 2001, mouse (Pigeon et al 2001, Ilyin et al 2003, dog (Fry et al 2004), 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. Similarly to previous studies , we were able to detect hepcidin mRNA and peptide in extrahepatic organs of guinea pig including kidney, heart, and pancreas, albeit at different levels, showing that hepcidin may play a role in extrahepatic organs, too.…”

Section: Discussionsupporting

confidence: 81%

“…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.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Schwarz

Strnad²,

Singer³

et al. 2009

Journal of Endocrinology

View full text Add to dashboard Cite

Hepcidin, a cysteine-rich peptide hormone with antimicrobial and iron-regulatory activity, plays a central role in regulating iron metabolism during inflammation, hypoxia, iron deficiency, and iron overload. The aim of this study was to isolate and sequence the guinea pig hepcidin gene and show peptide's tissue distribution to identify the guinea pig as good animal model to study the regulation and function of hepcidin. The guinea pig hepcidin cDNA contains a 252 bp open reading frame encoding for an 83 amino acid protein with eight highly conserved cysteine residues. Phylogenetic analyses showed that guinea pig hepcidin was more related to human and chimpanzee than to rodents like mouse or rat. RT-PCR studies revealed that hepcidin mRNA was most abundant in liver, less ample in pancreas, heart, and kidney and not detectable in lung and biliary system. Western blot analyses showed a distinct immunoreactive band of w8 kDa, consistent with the predicted size of prohepcidin, and revealed that guinea pig hepcidin protein is synthesized predominantly in the liver, and with lower expression in kidney, heart, and pancreas. Immunohistochemical studies showed hepcidin predominantly at the basolateral membrane domain of hepatocytes in periportal regions. In pancreas, hepcidin immunoreactivity was confined to endocrine islets of Langerhans, while hepcidin was seen in tubules, but not in the glomeruli in the kidney. Our data identify guinea pig as a convenient model organism to study the role of hepcidin, given the remarkable sequence similarity and tissue distribution pattern largely identical to human.

show abstract

Section: Discussionsupporting

confidence: 81%

Section: Introductionmentioning

confidence: 99%

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

Schwarz

Strnad²,

Singer³

et al. 2009

Journal of Endocrinology

View full text Add to dashboard Cite

show abstract

“…Sequences of the overgo primers are shown in Table 1. Overgo hybridization was conducted as described [22,24]. Positive clones were identified according to the clone distribution instructions from CHORI, and one clone was picked out for sequencing analysis.…”

Section: Cmentioning

confidence: 99%

Characterization of a NK-lysin antimicrobial peptide gene from channel catfish

Wang

Bao

Wang

et al. 2006

Fish & Shellfish Immunology

Self Cite

View full text Add to dashboard Cite

“…Aside from its antimicrobial activity, a much more important role was quickly attributed to hepcidin, as the long-sought key regulator of iron metabolism, through the inhibition of the iron exporter ferroportin (5,6). A hepcidin homolog was soon after found in a teleost fish, the hybrid striped bass (Morone saxatilis 3 Morone chrysops) (7), and several others followed (8)(9)(10). However, contrary to mammals, in which a single hepcidin gene exists [with the mouse being the only known exception (11)], the studies performed with other fish species have shown that many teleosts could possess a large number of hepcidin genes (1,12), especially in Perciformes and Pleuronectiformes.…”

mentioning

confidence: 99%

Multiple Hepcidins in a Teleost Fish, Dicentrarchus labrax: Different Hepcidins for Different Roles

Neves

Caldas

Vieira

et al. 2015

The Journal of Immunology

View full text Add to dashboard Cite

Teleost fish rely heavily on their innate immunity for an adequate response against pathogens and environmental challenges, with the production of antimicrobial peptides being one of their first lines of defense. Among those is hepcidin, a small cysteine-rich antimicrobial peptide that is also the key regulator of iron metabolism. Although most mammals possess a single hepcidin gene, with a dual role in both iron metabolism regulation and antimicrobial response, many teleost fish present multiple copies of hepcidin, most likely because of genome duplications and positive Darwinian selection, suggesting that different hepcidins may perform different functions. To study the roles of hepcidin in teleost fish, we have isolated and characterized several genes in the European sea bass (Dicentrarchus labrax) and evaluated variations in their expression levels in response to different experimental conditions. Although several hepcidin genes were found, after phylogenetic analysis they could be clustered in two groups: hamp1-like, with a single isoform similar to mammalian hepcidins, and hamp2-like, with several isoforms. Under experimental conditions, hamp1 was upregulated in response to iron overload and infection and downregulated during anemia and hypoxic conditions. Hamp2 did not respond to either iron overload or anemia but was highly upregulated during infection and hypoxia. In addition, Hamp2 synthetic peptides exhibited a clear antimicrobial activity against several bacterial strains in vitro. In conclusion, teleost fish that present two hepcidin types show a degree of subfunctionalization of its functions, with hamp1 more involved in the regulation of iron metabolism and hamp2 mostly performing an antimicrobial role.

show abstract

Catfish hepcidin gene is expressed in a wide range of tissues and exhibits tissue-specific upregulation after bacterial infection

Cited by 163 publications

References 44 publications

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

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

Characterization of a NK-lysin antimicrobial peptide gene from channel catfish

Multiple Hepcidins in a Teleost Fish, Dicentrarchus labrax: Different Hepcidins for Different Roles

Contact Info

Product

Resources

About