A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade
2000 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, Vol. 275, no 14, 9996-10001 p.Article in journal (Refereed) Published
A cDNA encoding a protein resembling masquerade, a serine proteinase homologue expressed during embryogenesis, larval, and pupal development in Drosophila melanogaster, was identified in hemocytes of the adult freshwater crayfish, Pacifastacus leniusculus. The crayfish protein is similar to Drosophila masquerade in the following aspects: (a) overall sequence of the serine proteinase domain, such as the position of three putative disulfide bridges, glycine in the place of the catalytic serine residue, and the presence of a substrate-lining pocket typical for trypsins; (b) the presence of several copies of a disulfide-knotted motif in the putative propeptide. This masquerade-like protein is cleaved into a 27-kDa fragment, which could be detected by immunoblot analysis using an affinity-purified antibody against a synthetic peptide in the C-terminal domain of the protein. The 27-kDa protein could be immunoaffinity-purified from hemocyte lysate supernatant and exhibited cell adhesion activity in vitro, indicating that the C-terminal domain of the crayfish masquerade-like protein mediates cell adhesion.
Place, publisher, year, edition, pages
2000. Vol. 275, no 14, 9996-10001 p.
HORSESHOE-CRAB HEMOCYTES, PROPHENOLOXIDASE-ACTIVATING SYSTEM, FRESH-WATER CRAYFISH, BLOOD-CELLS, PROCLOTTING ENZYME, MOLECULAR-BASIS, CDNA CLONING, SEQUENCE, PURIFICATION, COAGULATION
IdentifiersURN: urn:nbn:se:uu:diva-38103OAI: oai:DiVA.org:uu-38103DiVA: diva2:66002
Addresses: Cerenius L, Uppsala Univ, Evolut Biol Ctr, Dept Comparat Physiol, Norbyvagen 18A, SE-75236 Uppsala, Sweden. Uppsala Univ, Evolut Biol Ctr, Dept Comparat Physiol, SE-75236 Uppsala, Sweden.2006-10-162006-10-162009-04-20Bibliographically approved