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J. Biol. Chem., Vol. 281, Issue 48, 36985-36992, December 1, 2006

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Lysophospholipids Control Integrin-dependent Adhesion in Splenic B Cells through G_i and G₁₂/G₁₃ Family G-proteins but Not through G_q/G₁₁^*

Stefan Rieken, Susanne Herroeder, Antonia Sassmann, Barbara Wallenwein, Alexandra Moers, Stefan Offermanns, and Nina Wettschureck¹

From the Institute of Pharmacology, University of Heidelberg, Im Neuenheimer Feld 366, and the Institute of Anesthesiology, University of Heidelberg, Im Neuenheimer Feld 110, 69120 Heidelberg, Germany

Integrin-mediated adhesion is a crucial step in lymphocyte extravasation and homing. We show here that not only the chemokines CXCL12 and CXCL13 but also the lysophospholipids sphingosine 1-phosphate (S1P) and lysophosphatidic acid (LPA) enhance adhesion of murine follicular and marginal zone B cells to ICAM-1 in vitro. This process involves clustering of integrin LFA-1 and is blocked by pertussis toxin, suggesting that G_i family G-proteins are involved. In addition, lysophospholipid-induced adhesion on ICAM-1 depends on Rho and Rhokinase, indicative of an involvement of G₁₂/G₁₃, possibly also G_q/G₁₁ family G-proteins. We used G₁₂/G₁₃- or G_q/G₁₁-deficient B cells to study the role of these G-protein families in lysophospholipid-induced adhesion and found that the pro-adhesive effects of LPA and S1P are completely abrogated in G₁₂/G₁₃-deficient marginal zone B cells, reduced in G₁₂/G₁₃-deficient follicular B cells, and normal in G_q/G₁₁-deficient B cells. We also show that loss of lysophospholipid-induced adhesion results in disinhibition of migration in response to the follicular chemokine CXCL13, which might contribute to the abnormal localization of splenic B cell populations observed in B cell-specific G₁₂/G₁₃-deficient mice in vivo. Taken together, this study shows that lysophospholipids regulate integrin-mediated adhesion of splenic B cells to ICAM-1 through G_i and G₁₂/G₁₃ family G-proteins but not through G_q/G₁₁.

Received for publication, June 2, 2006 , and in revised form, October 4, 2006.

^* This work was supported by the Collaborative Research Center 405 of the Deutsche Forschungsgemeinschaft. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 49-6221-548255; Fax: 49-6221-548549; E-mail: Nina.Wettschureck{at}urz.uni-heidelberg.de.

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