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Compartmentalization of cyclic GMP-dependent protein kinase in formyl-
peptide stimulated neutrophils
KB Pryzwansky, TA Wyatt, H Nichols and TM Lincoln
Department of Pathology, University of North Carolina, Chapel Hill
27599-7525.
The presence and physiologic role of cyclic GMP-dependent protein kinase
(G-kinase) in human neutrophils was investigated by Western blot analysis
and immunocytochemistry. Small quantities of G-kinase were found in the
cytoskeletal-enriched fraction of neutrophil lysates as detected by Western
blots using a polyclonal antibody raised against bovine aorta G-kinase.
Immunofluorescence microscopy demonstrated in adherent neutrophils that
G-kinase was localized diffusely within the cytoplasm, at the microtubule
organizing center, and in the euchromatin of the nucleus. Because cyclic
GMP is implicated as a modulator of neutrophil chemotaxis, G-kinase
localization was investigated in neutrophils activated with
N-formyl-methionyl-leucyl-phenylalanine (fMLP). fMLP stimulated transient
focal changes in G-kinase localization that coincided with transient
changes in cell shape. G- kinase translocated over a period of 5 minutes
from diffuse staining of the cytosol to filaments within the uropod of
polarized cells (1 minute), to bundles of filaments associated with loss of
cell polarity (2.5 minutes), and finally to more intense staining of the
nuclear euchromatin (5 minutes). Optical sectioning of neutrophils by
confocal laser scanning microscopy confirmed that G-kinase was restricted
to specific sub-cellular compartments during cell activation. This
transient localization of G-kinase was disrupted by cytoskeletal inhibitors
and was augmented by 8-Br-cyclic GMP. These data provide evidence for the
first time that G-kinase plays a physiologic role in human neutrophils, and
support the concept of compartmentalization of cyclic nucleotides during
neutrophil activation.
Volume 76,
Issue 3,
pp. 612-618,
08/01/1990
Copyright © 1990 by The American Society of Hematology
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