Molecular characterization and gene expression of ferritin in red abalone (Haliotis rufescens)



Salinas-Clarot K, Gutiérrez AP, Núñez-Acuña G & Gallardo-Escárate C (2011) Molecular characterization and gene expression of ferritin in red abalone (Haliotis rufescens). Fish and Shellfish Immunology, 30 (1), pp. 430-433.

Ferritin is the principal iron storage protein in the majority of living organisms. Its capacity to capture the toxic cellular iron in excess in a compact and safe manner, gives to this protein a key role in detoxification and iron storage. It has a main role in cellular homeostasis and in cellular defense against oxidative stress produced by the reactive oxygen species (ROS). In this research, the cDNA coding sequence of ferritin for Red abalone (Haliotis rufescens) was obtained, which had an open reading frame (ORF) of 516 bp. The deduced amino acid sequence was consisted of 171 residues with a calculated molecular weight of 19.77 kDa. In addition, tissue expression profiles of ferritin in Red abalone were induced by thermal stress showed an expression peak from 16 °C to 22 °C. The transcriptional level of ferritin was mainly achieved in muscle, digestive gland, gills, foot, mantle and gonad respectively. This research providing more information to better understands the structural and functional properties of this protein in Haliotis.

Haliotis rufescens; Ferritin; Temperature challenge; RT-PCR; Gene expression

Fish and Shellfish Immunology: Volume 30, Issue 1

Publication date31/01/2011
Publication date online01/10/2010
Date accepted by journal19/09/2010
PublisherElsevier BV

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Dr Alejandro Gutierrez
Dr Alejandro Gutierrez

Lecturer in Genetic Improvement, Institute of Aquaculture