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Human granulocyte colony-stimulating factor: biologic activities and
receptor characterization on hematopoietic cells and small cell lung cancer
cell lines
BR Avalos, JC Gasson, C Hedvat, SG Quan, GC Baldwin, RH Weisbart, RE Williams, DW Golde and JF DiPersio
Department of Internal Medicine, Ohio State University, Columbus 43210.
Human granulocyte colony-stimulating factor (G-CSF) is a regulatory
glycoprotein that stimulates the production of neutrophilic granulocytes
from committed hematopoietic progenitor cells both in vitro and in vivo. In
this report, we show that biosynthetic (recombinant) human G-CSF enhances
colony formation by normal human bone marrow and the human myeloid leukemic
cell lines, HL-60 and KG-1, as well as nonhematopoietic small cell lung
cancer lines, H128 and H69. G-CSF also modulates multiple differentiated
functions of human neutrophils, including enhanced oxidative metabolism in
response to f- Met-Leu-Phe (f-MLP), increased antibody-dependent
cell-mediated cytotoxicity (ADCC), and augmented arachidonic acid release
in response to ionophore and chemotactic agents. These effects are all
maximal at a concentration of 100 to 500 pmol/L. Using 125I-labeled
recombinant human G-CSF, high affinity binding sites were identified on
human neutrophils, the myeloid leukemia cell lines KG-1 and HL-60, and the
small cell carcinoma cell lines, H128 and H69. G-CSF receptor numbers
ranged between 138 and 285 sites per cell with a kd of 77 to 140 pmol/L,
consistent with the concentrations of G-CSF that elicit biologic responses
in vitro. Decreased specific binding of 125l-G-CSF by human neutrophils was
consistently observed in the presence of excess unlabeled human
granulocyte-macrophage colony-stimulating factor (GM-CSF), suggesting
competition or down modulation by GM-CSF of the G- CSF receptor.
Volume 75,
Issue 4,
pp. 851-857,
02/15/1990
Copyright © 1990 by The American Society of Hematology
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