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

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

Author Nakahata, Adriana M. Google Scholar
Bueno, Norlene R. Google Scholar
Rocha, Hugo A. O. Google Scholar
Franco, Celia R. C. Google Scholar
Chammas, Roger Google Scholar
Nakaie, Clovis R. Google Scholar
Jasiulionis, Miriam G. Google Scholar
Nader, Helena B. Google Scholar
Santana, Lucimeire A. Google Scholar
Sampaio, Misako U. Google Scholar
Oliva, Maria Luiza V. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Univ Fed Rio Grande Norte
Univ Fed Parana
Universidade de São Paulo (USP)
Abstract 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.
Keywords Bauhinia
cell adhesion
trypsin inhibitor
Language English
Date 2006-12-15
Published in International Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 40, n. 1, p. 22-29, 2006.
ISSN 0141-8130 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 22-29
Access rights Closed access
Type Article
Web of Science ID WOS:000243052100004

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