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The Journal of Immunology, Vol 153, Issue 8 3574-3583, Copyright © 1994 by American Association of Immunologists
ARTICLES |
CR Maliszewski, GJ Delespesse, MA Schoenborn, RJ Armitage, WC Fanslow, T Nakajima, E Baker, GR Sutherland, K Poindexter and C Birks
Immunex Research and Development Corporation, Seattle, WA 98101.
CD39, a 70- to 100-kDa molecule expressed primarily on activated lymphoid cells, was previously shown to mediate B cell homotypic adhesion when ligated with a subset of anti-CD39 mAbs. In the present study, we describe the cloning and molecular characterization of human and murine CD39. The nucleotide sequence of human CD39 includes an open reading frame encoding a putative 510 amino acid protein with six potential N-linked glycosylation sites, 11 Cys residues, and two potential transmembrane regions. Murine CD39 shares 75% amino acid sequence identity with human CD39 but fails to cross-react with anti- human CD39 mAbs. Although there were no significant similarities with other mammalian genes, considerable homology was found between CD39 and a guanosine diphosphatase from yeast. A series of mouse-human hybrid molecules was constructed to determine the general topology of CD39 and the location of a biologically functional epitope. These findings and supporting evidence from an anti-CD39 mAb-selected phage peptide display library indicate a likely model wherein a short intracellular N- terminus is followed by a large extracellular loop containing the epitope recognized by stimulatory anti-CD39 mAbs, and a short intracellular C terminus. The results demonstrate that CD39 is a novel cell surface glycoprotein with unusual structural characteristics.
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X. Zhong, R. Malhotra, R. Woodruff, and G. Guidotti Mammalian Plasma Membrane Ecto-nucleoside Triphosphate Diphosphohydrolase 1, CD39, Is Not Active Intracellularly. THE N-GLYCOSYLATION STATE OF CD39 CORRELATES WITH SURFACE ACTIVITY AND LOCALIZATION J. Biol. Chem., October 26, 2001; 276(44): 41518 - 41525. [Abstract] [Full Text] [PDF]
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