4.5 Article

Stabilin-2 mediates homophilic cell-cell interactions via its FAS1 domains

Journal

FEBS LETTERS
Volume 583, Issue 8, Pages 1375-1380

Publisher

WILEY
DOI: 10.1016/j.febslet.2009.03.046

Keywords

Stabilin-2; Homophilic; Cell-cell interaction; FAS1 domain

Funding

  1. National R&D Program for Cancer Control, Ministry of Health & Welfare, Republic of Korea [0720550-2]
  2. Korea government (MEST) [R11-2008-044-03001-0]
  3. Brain Korea 21 Project
  4. National Research Foundation of Korea [R11-2008-044-03001-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Stabilin-2 was recently shown to mediate a heterophilic interaction with integrin alphaMbeta2 via its FAS1 domain. Here, we demonstrate that stabilin-2 also mediates homophilic cell-cell interactions. L cells expressing stabilin-2 mediate a significant level of cell aggregation, and this aggregation is significantly inhibited by anti-stabilin-2 antibody. Stabilin-2-mediated aggregation is mediated by homophilic interactions and enhanced in the presence of Ca2+ and Mg2+. Interestingly, exogenous addition of FAS1 domains but not EGF-like domains enhances stabilin-2-mediated cell aggregation, suggesting that exogenous FAS1 domains may form polymeric structure with FAS1 domains of stabilin-2. Together, these data show the participation of stabilin-2 in homophilic cell adhesion and role of FAS1 domains. (C) 2009 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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