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Fish Shellfish Immunol. 2014 Aug;39(2):136-7. doi: 10.1016/j.fsi.2014.05.007. Epub 2014 May 14.

Molecular cloning of α-2-macroglobulin from hemocytes of common periwinkle Littorina littorea.

Author information

1
Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences (IEPhB RAS), St-Petersburg, Russia.
2
Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences (IEPhB RAS), St-Petersburg, Russia. Electronic address: agorbushin@gmail.com.

Abstract

We report the sequence of the proteinase inhibitor with a wide inhibition spectrum, α-2-macroglobulin (α2M), belonging to the thioester superfamily of proteins. This is the first α2M sequence from coenogastropod prosobranch snails. The full-length cDNA was cloned by RACE method, spans 7897 bp and contains an open reading frame of 5460 bp. The ORF encodes a protein of 1819 amino acids. The deduced mature protein contains 1795 amino acids with a molecular weight of 200 kDa and isoelectric point of 5.00. Littorina littorea α2M bears 4 conserved α2M domains and one internal thioester. Phylogenetic analysis showed that the sequence forms well supported cluster with Mollusca species and other representatives of Lophotrochozoa.

KEYWORDS:

Coenogastropoda; Hemocytes; Innate immunity; Mollusca; Proteinase inhibitors

PMID:
24830774
DOI:
10.1016/j.fsi.2014.05.007
[Indexed for MEDLINE]

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