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Keywords:

  • laminin-binding;
  • F-actin-binding;
  • glycoprotein

Abstract

Two major EHS-laminin-binding membrane glycoproteins—with apparent molecular masses of 50kD and 18kD—were shown by protein blotting in membrane fractions of porcine neutrophils. These galectin-like glycoproteins (binding probably via the N-acetyllactosamine sequences to laminin) could also be detected by labelled F-actin in protein blots. Following 35min adhesion to the plastic surface, the relative amount of the 18kD protein increased considerably in the light (plasma membrane) and in the dense (intracellular) membrane fractions of the attached cells; the 50kD polypeptide (identified as a CD14-like protein) seemed to accumulate characteristically in the dense membrane fraction. These observations imply that direct connections could be formed between membrane glycoproteins and microfilaments during cell—substrate adhesion which may be preceded by enhanced cell surface targeting of certain adhesion receptors.