LEC induces chemotaxis and adhesion by interacting with CCR1 and CCR8

Citation
Omz. Howard et al., LEC induces chemotaxis and adhesion by interacting with CCR1 and CCR8, BLOOD, 96(3), 2000, pp. 840-845
Citations number
38
Categorie Soggetti
Hematology,"Cardiovascular & Hematology Research
Journal title
BLOOD
ISSN journal
00064971 → ACNP
Volume
96
Issue
3
Year of publication
2000
Pages
840 - 845
Database
ISI
SICI code
0006-4971(20000801)96:3<840:LICAAB>2.0.ZU;2-I
Abstract
Liver-expressed chemokine (LEC) is an unusually large CC chemokine, which i s 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 s how 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 requi red for RANTES or 1309, respectively. All 3 chemokines induced maximal stat ic adhesion at 5 to 7 nmol/L. A neutralizing polyclonal antibody to LEC was developed to demonstrate that the unusually high concentration of LEC requ ired to induce chemotaxis was a property of LEC end not as a result of an i rrelevant protein contamination. This study suggests that LEC may be a more effective inducer of cell adhesion than cell migration. (C) 2000 by The Am erican Society of Hematology.