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Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages

Academic Article
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Overview

authors

  • Crocker, P. R.
  • Kelm, S.
  • Dubois, C.
  • Martin, B.
  • McWilliam, A. S.
  • Shotton, D. M.
  • Paulson, James
  • Gordon, S.

publication date

  • July 1991

journal

  • EMBO Journal  Journal

abstract

  • Macrophage subpopulations in the mouse express a lectin-like receptor, sialoadhesin (originally named sheep erythrocyte receptor, SER), which selectively recognizes sialoglycoconjugates and is likely to be involved in cellular interactions of stromal macrophages in haematopoietic and lymphoid tissues. In this report we describe the purification and ligand specificity of sialoadhesin isolated from mouse spleen. Purified sialoadhesin, a glycoprotein of 185 kd apparent Mr, agglutinated sheep or human erythrocytes at nanomolar concentrations in a sialic acid-dependent manner. Low angle shadowing and electron microscopy showed that sialoadhesin consisted of a globular head region of approximately 9 nm and an extended tail of approximately 35 nm. To investigate the specificity for sialic acid, we studied the interaction of sialoadhesin with derivatized human erythrocytes, glycoproteins, and glycolipids. In conclusion, sialoadhesin specifically recognizes the oligosaccharide sequence Neu5Ac alpha 2----3Gal beta 1----3GalNAc in either sialoglycoproteins or gangliosides. These findings imply that specific sialoglycoconjugates carrying this structure may be involved in cellular interactions between stromal macrophages and subpopulations of haematopoietic cells and lymphocytes.

subject areas

  • Animals
  • Carbohydrate Sequence
  • Chromatography, Thin Layer
  • Erythrocyte Aggregation
  • Macrophages
  • Membrane Glycoproteins
  • Mice
  • Molecular Sequence Data
  • Oligosaccharides
  • Receptors, Immunologic
  • Sialic Acid Binding Ig-like Lectin 1
  • Sialic Acids
  • Spleen
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Research

keywords

  • ADHESION
  • LECTIN
  • MACROPHAGE
  • RECEPTOR
  • SIALIC ACID
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Identity

PubMed Central ID

  • PMC452836

International Standard Serial Number (ISSN)

  • 0261-4189

PubMed ID

  • 2050106
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Additional Document Info

start page

  • 1661

end page

  • 1669

volume

  • 10

issue

  • 7

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