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J Biol Chem, Vol. 275, Issue 14, 9996-10001, April 7, 2000

A Cell Adhesion Protein from the Crayfish Pacifastacus leniusculus, a Serine Proteinase Homologue Similar to Drosophila Masquerade*

Tien-sheng HuangDagger , Haiyao Wang, So Young Lee, Mats W. Johansson§, Kenneth Söderhäll, and Lage Cerenius

From the Department of Comparative Physiology, Evolutionary Biology Centre, Uppsala University, Norbyvägen 18A, SE-752 36 Uppsala, Sweden

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.

* This work was supported by grants from the Swedish Natural Science Research Council, the Swedish Council for Forestry and Agricultural Research and by the European Union Fair PL-97-3660 (to K. S.), and from the Swedish Medical Research Council (to M. W. J.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Medical Biochemistry and Microbiology, BMC, Uppsala University, Box 575, S.E.-751 23 Uppsala, Sweden.

§ Present address: Dept. of Medicine, University of Wisconsin, 4285A Medical Sciences Center, 1300 University Avenue, Madison, WI 53706-1532.

To whom correspondence should be addressed: Dept. of Comparative Physiology, Evolutionary Biology Center, Uppsala University, Norbyvägen 18A, 752 36 Uppsala, Sweden. Tel.: 46-18-4712804; Fax: 46-18-4716425; E-mail: Lage.Cerenius@fysbot.uu.se.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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