TI  -   <prot>LEC</prot>   induces chemotaxis and adhesion by interacting with  <prot>CCR1</prot>  and  <prot>CCR8</prot> .
PG  - 840-5
AB  - <prot>Liver-expressed chemokine</prot> (<prot>LEC</prot>) is an unusually large CC chemokine, which
      is also known as <prot>LMC</prot>, <prot>HCC-4</prot>, <prot>NCC-4</prot>, and <prot>CCL16</prot>. Previously, <prot>LEC</prot> was shown
      to induce leukocyte migration but the responsible signaling receptors were
      not characterized. We report chemotaxis and competitive binding studies
      that show    <prot>LEC</prot>   binds to and activates  <prot>CCR1</prot>  and    <prot>CCR8</prot> transfected HEK-293
      cells. <prot>LEC</prot> induced maximal migration of <prot>CCR1</prot> and <prot>CCR8</prot> transfected cells at
      89.3 nmol/L and cell adhesion at 5.6 nmol/L. The molar concentration of
      <prot>LEC</prot> required to induce maximum cell migration is 20- to 200-fold greater
      than that required for <prot>RANTES</prot> or <prot>I309</prot>, respectively. All 3 chemokines
      induced maximal static adhesion at 5 to 7 nmol/L. A neutralizing
      polyclonal antibody to <prot>LEC</prot> was developed to demonstrate that the unusually
      high concentration of <prot>LEC</prot> required to induce chemotaxis was a property of
      <prot>LEC</prot> and not as a result of an irrelevant protein contamination. This study
      suggests that <prot>LEC</prot> may be a more effective inducer of cell adhesion than
      cell migration.
AD  - Intramural Research Support Program, Laboratory of Molecular
