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Blood, Vol. 96 No. 3 (August 1), 2000:
pp. 840-845
LEC induces chemotaxis and adhesion by interacting with CCR1 and
CCR8
O. M. Zack Howard,
Hui Fang Dong,
Aiko-Konno Shirakawa, and
Joost J. Oppenheim
From the Intramural Research Support Program, Laboratory of
Molecular Immunoregulation, Division of Basic Science, National Cancer
Institute-Frederick Cancer Research and Development Center, Frederick,
MD.
Liver-expressed chemokine (LEC) is an unusually large CC chemokine,
which is also known as LMC, HCC-4, NCC-4, and CCL16. Previously, LEC
was shown to induce leukocyte migration but the responsible signaling
receptors were not characterized. We report chemotaxis and competitive
binding studies that show LEC binds to and activates CCR1 and CCR8
transfected HEK-293 cells. LEC induced maximal migration of CCR1 and
CCR8 transfected cells at 89.3 nmol/L and cell adhesion at 5.6 nmol/L.
The molar concentration of LEC required to induce maximum cell
migration is 20- to 200-fold greater than that required for RANTES or
I309, respectively. All 3 chemokines induced maximal static adhesion at
5 to 7 nmol/L. A neutralizing polyclonal antibody to LEC was developed
to demonstrate that the unusually high concentration of LEC required to
induce chemotaxis was a property of LEC and not as a result of an
irrelevant protein contamination. This study suggests that LEC may be a
more effective inducer of cell adhesion than cell migration.
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