Structural and inhibitory properties of a plant proteinase inhibitor containing the RGD motif

  • Nakahata A
  • Bueno N
  • Rocha H
 et al. 
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Abstract

Purified from Bauhinia rufa seeds, BrTI is a Kunitz proteinase inhibitor that contains the RGD sequence. BrTI inhibits trypsin (Kiapp2.9 nM) and human plasma kallikrein (Kiapp14.0 nM) but not other related enzymes. The synthetic peptide YLEPVARGDGGLA-NH2(70 μM) inhibited the adhesion to fibronectin of B16F10 (high-metastatic B16 murine mouse melanoma cell line) and of Tm5 (murine melanoma cell lines derived from a non-tumorigenic lineage of pigmented murine melanocytes, melan-a). YLEPVARGEGGLA-NH2in which Asp9was changed into Glu does not affect the cell attachment. Moreover, this peptide was functional only when the sequence present in the native protein was preserved, since YLIPVARGDGGLA-NH2in which Glu3was changed into Ile does not interfere with B16F10 and was less effective on Tm5 cell line adhesion. Neither YLEPVARGDGGLA-NH2, YLIPVARGDGGLA-NH2or YLEPVARGEGGLA-NH2inhibit the interaction of RAEC (endothelial cell line from rabbit aorta) with fibronectin. © 2006 Elsevier B.V. All rights reserved.

Author-supplied keywords

  • Bauhinia
  • Cell adhesion
  • Elastase
  • Melanoma
  • RGD
  • Trypsin inhibitor
  • Tumor

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