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Volume 272, Number 26, Issue of June 27, 1997 pp. 16329-16334
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Analysis of Small Latent Transforming Growth Factor- Complex Formation and Dissociation by Surface Plasmon Resonance
ABSENCE OF DIRECT INTERACTION WITH THROMBOSPONDINS

(Received for publication, December 20, 1996, and in revised form, April 11, 1997)

From the INSERM U244, DBMS/BRCE, Commissariat à l'Energie Atomique Grenoble, 17 rue des martyrs, 38054 Grenoble Cedex 9, France

Transforming growth factor- (TGF) is a pluripotent regulator of cell growth and differentiation. The growth factor is expressed as a latent complex that must be converted to an active form before interacting with its ubiquitous high affinity receptors. This conversion involves the release of the mature TGF through disruption of the noncovalent interactions with its propeptide or latency associated protein (LAP). Complex formation or dissociation between LAP and TGF plays a very important role in TGF biological activity at different steps. To further characterize the kinetic parameters of this interaction, we have employed surface plasmon resonance biosensor methodology. Using this technique, we observed real time association of LAP with mature TGF1. The complex formation showed an equilibrium K_d around 3-7 nM. Furthermore, we observed dissociation of the complex in the presence of extreme pH, chaotropic agents, or plasmin, confirming their effects on TGF activation. The same approach was used to examine whether latent TGF1 could interact with thrombospondins, previously described as activators of latent TGF. Using this method, we could not detect any direct interaction of thrombospondins with either LAP alone, TGF1 alone, or the small latent TGF1 complex. This suggests that activation of latent TGF1 complex by thrombospondins is through an indirect mechanism.

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