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      Common skate (Raja kenojei) secretes pentraxin into the cutaneous secretion: The first skin mucus lectin in cartilaginous fish.

      Journal of Biochemistry
      Agglutination, Amino Acid Sequence, Animals, Base Sequence, C-Reactive Protein, chemistry, isolation & purification, metabolism, Computational Biology, Gene Expression Regulation, Humans, Lectins, Liver, cytology, Molecular Sequence Data, Mucus, Phylogeny, Reverse Transcriptase Polymerase Chain Reaction, Sequence Alignment, Skates (Fish), Skin, Swine

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          Abstract

          A lactose-specific lectin with a molecular mass of about 25 kDa was purified from the skin mucus of a cartilaginous fish-the common skate (Raja kenojei). The complementary DNA sequence of the lectin was 1540 bp long and contained a reading frame encoding 226 amino acids, which showed approximately 38% identity to pentraxins of mammals and teleosts. Gene expression was observed in the skin, gill, stomach and intestine in the healthy skate. We also identified an isotype gene from the liver whose deduced amino-acid sequence shared 69.0% identity with the skin type gene. The antiserum detected protein in the skin, where the lectin is localized in the epidermal cells, and in the blood plasma. The lectin genes are multicopied in the common skate genome. Although pentraxins are acute phase proteins, mRNAs of both the isotypes were not upregulated after the in vivo challenge with formalin-killed Escherichia coli, which suggests that they are constantly present in the skin mucus and blood plasma to protect against pathogenic invasion. This lectin is the fifth type of lectin found in the cutaneous secretions of fish, demonstrating that skin mucus lectins have evolved with marked molecular diversity in fish.

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