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Secretion of Endothelial-Leukocyte Adhesion Molecule (ELAM-1) Upon Deletion of Portions of Its Carboxyl Terminus

  • T. J. Ahern
  • M. A. Shaffer
  • D. S. Sako
  • Glenn R. Larsen
Part of the NATO ASI Series book series (NSSA, volume 208)

Abstract

The carboxyl terminus of endothelial-leukocyte adhesion molecule (ELAM-1) consists of a 22-amino acid, hydrophobic domain followed by a 32-amino acid, hydrophilic domain. In an effort to identify the portions of the carboxyl terminus necessary for efficient subcellular transport and anchoring of ELAM-1 in the endothelial cell membrane, we have altered these domains by site-directed mutagenesis of the molecularly cloned sequence of ELAM-1. Expression of mature ELAM-1 in mammalian cells produced no detectable ELAM-1 in the conditioned media, as determined by pulse-chase labeling with 35S-methionine. Modifications within the carboxyl terminus of ELAM-1 resulted in expression and secretion of the variant forms. Unlike cells expressing full-length ELAM-1, none of the cells expressing secreted mutant forms bound either neutrophils or HL-60 cells (a promyelocytic precursor of neutrophils), indicating that functional ELAM-1 was not associated with the cell. We conclude that the carboxyl terminal region is required for anchoring ELAM-1 into the cell membrane.

Keywords

Public Health Cell Membrane Mammalian Cell Conditioned Medium Variant Form 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • T. J. Ahern
    • 1
  • M. A. Shaffer
    • 1
  • D. S. Sako
    • 1
  • Glenn R. Larsen
    • 1
  1. 1.Genetics InstituteCambridgeUSA

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