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Blood, Vol. 95 No. 5 (March 1), 2000:
pp. 1551-1559
GCP-2-induced internalization of IL-8 receptors: hierarchical
relationships between GCP-2 and other ELR+-CXC chemokines
and mechanisms regulating CXCR2 internalization and
recycling
Rotem Feniger-Barish,
Dan Belkin,
Alon Zaslaver,
Shira Gal,
Mally Dori,
Maya Ran, and
Adit Ben-Baruch
From the Department of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
The chemotactic potencies of ELR+-CXC chemokines
during acute inflammation are regulated by their binding affinities and
by their ability to activate, desensitize, and internalize their specific receptors, CXCR1 and CXCR2. To gain insight into the fine
mechanisms that control acute inflammatory processes, we have focused
in this study on the highly potent ELR+-CXC chemokine
Granulocyte Chemotactic Protein 2 (GCP-2), and on its ability to
control the cell surface expression of CXCR1 and CXCR2. Although GCP-2
has been considered an effective ligand for both CXCR1 and CXCR2, our
findings demonstrated that it was a potent inducer of CXCR2
internalization only. A functional hierarchy was shown to exist between
GCP-2 and 2 other ELR+-CXC chemokines, IL-8 and NAP-2, in
their abilities to induce CXCR1 and CXCR2 internalization, according to
the following: IL-8 > GCP-2 > NAP-2. By the use of pertussis toxin
(PTx), it was demonstrated that the actual events of
G i-coupling to CXCR2 do not have a major role in the
regulation of its internalization. Rather, CXCR2 internalization was
shown to be negatively controlled by induction of signaling events, as
indicated by the promotion of CXCR2 internalization following exposure
to wortmannin, a potent inhibitor of phosphatidylinositol (PI) 3 kinases and PI4 kinases. Furthermore, our results suggest that
rab11+-endosomes participate in the trafficking of CXCR2
through the endocytic pathway, to eventually allow its recycling back
to the plasma membrane. To conclude, our findings shed light on the
interrelationships between GCP-2 and other ELR+-CXC
chemokines, and determine the mechanisms involved in the regulation
of GCP-2-induced internalization and recycling of CXCR2.
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