A novel lectin from Sarcophaga. Its purification, characterization, and cDNA cloning.

The Journal of Biological Chemistry
Y FujitaS Natori

Abstract

A novel C-type lectin that agglutinates rabbit red cells was purified from NIH-Sape-4 cells derived from the flesh fly (Sarcophaga peregrina), and its cDNA was isolated. This lectin, named granulocytin, appeared to be a trimer of a 20-kDa subunit consisting of 151 amino acid residues. The gene for granulocytin was activated in third instar larvae, and its expression was enhanced when the larval body wall was injured. In third instar larvae, granulocytin was found to be synthesized by hemocytes and secreted into the hemolymph. The molecular mass and gene expression patterns of granulocytin were very similar to those of Drosophila lectin that we reported previously (Haq, S., Kubo, T., Kurata, S., Kobayashi, A., and Natori, S. (1996) J. Biol. Chem. 271, 20213-20218). However, these two lectins showed amino acid identities of 20% at most, and no significant hapten sugar for granulocytin was identified.

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Citations

Sep 7, 2000·Biochemical and Biophysical Research Communications·Y FujitaS Natori
Aug 11, 2005·International Journal of Colorectal Disease·Kazue NakataGen-Ichiro Soma
Jul 30, 1999·Developmental and Comparative Immunology·S NatoriA Kobayashi
Jun 18, 2004·Immunological Reviews·George K ChristophidesFotis C Kafatos
Dec 13, 2005·The FEBS Journal·Alex N Zelensky, Jill E Gready
Aug 27, 2002·Fish & Shellfish Immunology·So Young Lee, Kenneth Söderhäll
Feb 16, 2006·The Biochemical Journal·Takahiro TanjiShunji Natori
May 12, 2021·International Journal of Biological Macromolecules·Kamalanathan TamilarasanSundaram Janarthanan

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