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Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
Published on: June 28, 2024
Distribution, polymorphism, and function of the cellular-aggregation-promoting protein, Apostichopus japonicus
Shunsuke Sugawara1, Sara Kuwata1, Miyabi Sato1
1School of Marine Biosciences, Kitasato University, 1-15-1, Kitasato, Minami-ku, Sagamihara, Kanagawa, 252-0373, Japan.
None:
Coelomocytes of echinoderms aggregate rapidly in response to various stimuli. In a previous study, we identified an endogenous aggregation-promoting factor in the Japanese sea cucumber Apostichopus japonicus and designated it as AjGBCL, a galactose-binding C-type lectin. In the present study, we produced recombinant AjGBCL (rAjGBCL) together with anti-rAjGBCL mouse serum. We confirmed that rAjGBCL indeed promotes coelomocyte aggregation. Western blotting using the antibody revealed that AjGBCL exists as a monomer, dimer, or tetramer under non-reducing conditions. Immunohistochemistry showed that AjGBCL is mainly localized within the granules of several coelomocyte types, which correspond to basophilic granulocytes described previously. Immunopositive cells in the intestine also exhibited granulocyte-like morphology, suggesting that AjGBCL is produced by resident coelomocytes in various tissues. We further discovered extraordinary sequence polymorphism in AjGBCL mRNA. From 28 clones derived from five individuals, we identified 23 distinct cDNA sequences that encoded 23 different deduced amino acid sequences. Amino-acid substitutions occurred at 40 positions in the 144-residue sequence. The possible origins and significance of this remarkable polymorphism are discussed.
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