Ceruloplasmin, a moonlighting protein in fish

Fish & Shellfish Immunology
Sweta Das, Pramoda Kumar Sahoo

Abstract

Ceruloplasmin is an ancient multicopper oxidase evolved to insure a safe handling of oxygen in some metabolic pathways of vertebrates. The current knowledge of its structure provides a glimpse of its plasticity, revealing a multitude of binding sites that point to an elaborate mechanism of multifunctional activity. Ceruloplasmin is highly conserved throughout the vertebrate evolution. Cupredoxin, a multi-cupper blue protein is believed to be the evolutionary precursor of ceruloplasmin with three trinuclear and three mononuclear copper binding sites. There are 20 copper-binding residues in ceruloplasmin gene out of which 16 residues are conserved in fish. This ceruloplasmin gene is being characterized in zebrafish (Danio rerio), rohu (Labeo rohita), Indian medaka (Oryzias melastigama), catfish (Ictalurus punctatus), icefish (Chionodraco rastrospinosus), goldfish (Carassius auratus) and yellow perch (Perca flaviscens). The complete coding sequence of fish ceruloplasmin gene is around 3.2 kb which codes for 1000 to 1100 amino acid residues. The size of ceruloplasmin gene sequence in fish ranges around 13 kb containing 20 exons and 19 introns. Liver is the major site of synthesis in fish. Increased expression of this gene during ba...Continue Reading

Citations

Jan 16, 2020·Biology·Richard A PhillipsSigrun Lange
Aug 21, 2019·Journal of Personalized Medicine·Ekaterina Y IlyechovaSergey A Samsonov
Jun 20, 2019·Nutrients·Ludmila V PuchkovaRoman S Polishchuk
Dec 17, 2019·The Science of the Total Environment·Jana BlahovaZdenka Svobodova
Nov 19, 2020·Vaccines·Irina V KiselevaLudmila V Puchkova
Jun 3, 2021·International Journal of Molecular Sciences·Ludmila V PuchkovaEkaterina Yu Ilyechova

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