8.A.37 The Hepcidin (Hepcidin) Family

Hepcidin is known to increase intracellular iron through binding to and degrading ferroportin, which is a transmembrane protein that transports iron from the cytoplasm to the outside. Hepcidin (<100 nM/L) increases intracellular calcium when cells are exposed to high environmental iron concentrations (Li et al., 2012). L-type calcium channel, and ryanodine receptors are not involved. Antagonists of these channels inhibit abnormal calcium release from the sarco-endoplasmic reticulum. The increase of intracellular calcium induced by hepcidin is probably due to calcium release from the endoplasmic reticulum.



This family belongs to the .

 

References:

Le Gac G., Ka C., Joubrel R., Gourlaouen I., Lehn P., Mornon JP., Ferec C. and Callebaut I. (2013). Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues. Hum Mutat. 34(10):1371-80.

Li GF., Xu YJ., He YF., Du BC., Zhang P., Zhao DY., Yu C., Qin CH. and Li K. (2012). Effect of hepcidin on intracellular calcium in human osteoblasts. Mol Cell Biochem. 366(1-2):169-74.

Rice, A.E., M.J. Mendez, C.A. Hokanson, D.C. Rees, and P.J. Björkman. (2009). Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter. J. Mol. Biol. 386: 717-732.

Examples:

TC#NameOrganismal TypeExample
8.A.37.1.1

Hepcidin

Animal

Hepcidin of Mus musculus (Q9EQ21)

 
8.A.37.1.2

Human hepcidin (84 aas).  Binds to and inhibits ferroportin (TC#2.A.100.1.4) (Le Gac et al. 2013).  Causes ferroportin internalization and degradation (Rice et al. 2009).

Animals

Hepcidin of Homo sapiens

 
8.A.37.1.3

Hepcidin antimicrobial peptide 4 of 95 aas.

Hepcidin peptide of Pagrus auriga

 
8.A.37.1.4

Hepcidin-like protein of 81 aas

Hepcidin-like protein of Python bivittatus

 
8.A.37.1.6

Uncharacterized protein of 111 aas.

UP of Quercus suber