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Rapid modulation of N-formyl chemotactic peptide receptors on the surface of human granulocytes: formation of high-affinity ligand-receptor complexes in transient association with cytoskeleton

Academic Article
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Overview

authors

  • Jesaitis, A. J.
  • Naemura, J. R.
  • Sklar, L. A.
  • Cochrane, Charles
  • Painter, R. G.

publication date

  • 1984

journal

  • Journal of Cell Biology  Journal

abstract

  • When human granulocytes were exposed to 50 nM N-formyl-Met-Leu-[3H]Phe at 37 degrees C they rapidly formed ligand-receptor complexes that dissociated 50-100 times more slowly than those on cells initially exposed to the peptide at 4 degrees C. These complexes of apparent higher affinity were stable after detergent solubilization of the cells with Triton X-100. The complexes co-isolated with the detergent insoluble cytoskeletal residues and were free of the cytosolic and Golgi markers, lactate dehydrogenase and galactosyl transferase, respectively. After 5 s of exposure to f-Met-Leu-Phe, 2,000-3,000 molecules of ligand per cell were trapped in such complexes. Continued exposure resulted in capture of a maximum of 14,000 molecules per cell by 5 min. Exposure at 15 degrees C, a temperature at which endocytosis of the receptor is prevented, resulted in complex formation at a linear rate for at least 20 min to levels twice those measured at 37 degrees C. At 4 degrees C, complex formation was approximately 10% of the maximum amount formed at 37 degrees C. Pulse-chase experiments revealed that the complex was in transient association with the cytoskeleton with a half life ranging between 30 s to 4 min depending on the length of the original incubation. Electron microscopic autoradiography indicated that after 1 min of incubation at 37 degrees C, the majority of the specific autoradiographic grains were localized to the outer circumference of the cellular cytoskeleton. After 4 min of incubation, the grains were less frequent at the cytoskeleton periphery but still threefold enriched over a random cellular distribution. We conclude that a metabolically controlled modulation of the state of the N-formyl chemotactic peptide receptor occurs in the plasma membrane which may be the result of transient association of ligand-receptor complex and the cell cytoskeleton.

subject areas

  • Cell Membrane
  • Electrophoresis, Polyacrylamide Gel
  • Granulocytes
  • Humans
  • Kinetics
  • Ligands
  • Microscopy, Electron
  • N-Formylmethionine Leucyl-Phenylalanine
  • Receptors, Cell Surface
  • Receptors, Formyl Peptide
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Identity

PubMed Central ID

  • PMC2113208

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.98.4.1378

PubMed ID

  • 6325470
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Additional Document Info

start page

  • 1378

end page

  • 1387

volume

  • 98

issue

  • 4

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