Structural and inhibitory properties of a plant proteinase inhibitor containing the RGD motif
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Data
2006-12-15
Autores
Nakahata, Adriana Miti [UNIFESP]
Bueno, Norlene Regina [UNIFESP]
Rocha, Hugo Alexandre de Oliveira
Franco, Celia Regina Cavichiolo
Chammas, Roger
Nakaie, Clovis Ryuichi [UNIFESP]
Jasiulionis, Miriam Galvonas [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Santana, Lucimeire Aparecida de [UNIFESP]
Sampaio, Misako Uemura [UNIFESP]
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Resumo
Purified from Bauhinia rufa seeds, BrTI is a Kunitz proteinase inhibitor that contains the RGD sequence. BrTI inhibits trypsin (K-iapp 2.9 nM) and human plasma kallikrein (K-iapp 14.0 nM) but not other related enzymes. the synthetic peptide YLEPVARGDGGLA-NH2 (70 mu M) 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-NH2 in which Asp(9) was 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-NH2 in which Glu(3) was changed into Ile does not interfere with B16F10 and was less effective on Tm5 cell line adhesion. Neither YLEPVARGDGGLA-NH2, YLIPVARGDGGLA-NH2 or YLEPVARGEGGLA-NH2 inhibit the interaction of RAEC (endothelial cell line from rabbit aorta) with fibronectin. (c) 2006 Elsevier B.V. All rights reserved.
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International Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 40, n. 1, p. 22-29, 2006.