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Int. J. Mol. Sci. 2017, 18(10), 2126; https://doi.org/10.3390/ijms18102126

Molecular Characterization and Functional Analysis of a Ferritin Heavy Chain Subunit from the Eri-Silkworm, Samia cynthia ricini

School of Life Sciences, Anhui Agricultural University, Hefei 230036, China
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Received: 6 September 2017 / Revised: 5 October 2017 / Accepted: 6 October 2017 / Published: 14 October 2017
(This article belongs to the Section Biochemistry)
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Abstract

Ferritins are conserved iron-binding proteins that are primarily involved in iron storage, detoxification and the immune response. Despite the importance of ferritin in organisms, little is known about their roles in the eri-silkworm (Samia cynthia ricini). We previously identified a ferritin heavy chain subunit named ScFerHCH in the S. c. ricini transcriptome database. The full-length S. c. ricini ferritin heavy chain subunit (ScFerHCH) was 1863 bp and encoded a protein of 231 amino acids with a deduced molecular weight of 25.89 kDa. Phylogenetic analysis revealed that ScFerHCH shared a high amino acid identity with the Bombyx mori and Danaus plexippus heavy chain subunits. Higher ScFerHCH expression levels were found in the silk gland, fat body and midgut of S. c. ricini by reverse transcription quantitative polymerase chain reaction (RT-qPCR) and Western blotting. Injection of Staphylococcus aureus and Pseudomonas aeruginosa was associated with an upregulation of ScFerHCH in the midgut, fat body and hemolymph, indicating that ScFerHCH may contribute to the host’s defense against invading pathogens. In addition, the anti-oxidation activity and iron-binding capacity of recombinant ScFerHCH protein were examined. Taken together, our results suggest that the ferritin heavy chain subunit from eri-silkworm may play critical roles not only in innate immune defense, but also in organismic iron homeostasis. View Full-Text
Keywords: ferritin; Samia cynthia ricini; immune response; iron binding capacity; anti-oxidation activity ferritin; Samia cynthia ricini; immune response; iron binding capacity; anti-oxidation activity
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Yu, H.-Z.; Zhang, S.-Z.; Ma, Y.; Fei, D.-Q.; Li, B.; Yang, L.-A.; Wang, J.; Li, Z.; Muhammad, A.; Xu, J.-P. Molecular Characterization and Functional Analysis of a Ferritin Heavy Chain Subunit from the Eri-Silkworm, Samia cynthia ricini. Int. J. Mol. Sci. 2017, 18, 2126.

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