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Review
. 2006 Mar;117(3):301-9.
doi: 10.1111/j.1365-2567.2005.02316.x.

Dealing with the family: CD147 interactions with cyclophilins

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Review

Dealing with the family: CD147 interactions with cyclophilins

Vyacheslav Yurchenko et al. Immunology. 2006 Mar.

Abstract

CD147 is a widely expressed plasma membrane protein that has been implicated in a variety of physiological and pathological activities. It is best known for its ability to function as extracellular matrix metalloproteinase inducer (hence the other name for this protein, EMMPRIN), but has also been shown to regulate lymphocyte responsiveness, monocarboxylate transporter expression and spermatogenesis. These functions reflect multiple interacting partners of CD147. Recently, interaction of CD147 with proteins of the cyclophilin family has been demonstrated and activity of CD147 as a signalling receptor to extracellular cyclophilins A and B has been shown. Given that extracellular cyclophilins are potent chemotactic agents for various immune cells, further studies of the role of cyclophilin-CD147 interaction in inflammation followed. They demonstrated that agents targeting CD147 or cyclophilin had a significant anti-inflammatory effect in animal models of acute or chronic lung diseases and rheumatoid arthritis. Here, we review the current knowledge about interactions between CD147 and cyclophilins.

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Figures

Figure 1
Figure 1
Proposed interactions between cyclophilins and CD147. CD147 is transported to the cell surface via the Golgi network. Interaction between cyclophilin 60 (CyP60) and Pro211 (the residue at the interface between the transmembrane and extracellular domains of CD147) occurs in the lumen of Golgi vesicle. Cyclophilin A (CyPA) is excluded from Golgi and does not have access to Pro211. Extracellular CyPA interacts with cell surface heparan sulfate proteoglycan (HSPG) and Pro180 in the extracellular domain of CD147. Membrane-proximal Pro211 is not accessible for interaction for sterical reasons. Not drawn to scale.

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