Inhibitory activity of the peptides derived from buffalo prolactin on angiogenesis

Lee, Jaeok ; Majumder, Symantak ; Chaterjee, Suvro ; Muralidhar, Kambadur (2011) Inhibitory activity of the peptides derived from buffalo prolactin on angiogenesis Journal of Bioscience, 36 (2). pp. 341-354. ISSN 0250-5991

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Official URL: http://www.ias.ac.in/jbiosci/jun2011/341.pdf

Related URL: http://dx.doi.org/10.1007/s12038-011-9073-6

Abstract

The peptide fragments obtained by cathepsin digestion of purified buffalo prolactin (buPRL) monomer have been characterized using SDS-PAGE and FPLC with regard to size and pI. Their antiangiogenic activity was tested in chick embryo chorioallantoic membrane (CAM) assay and the human endothelial cells wound healing assay. Antiangiogenic activity was observed in cathepsin-cleaved fragments from buPRL. Further, a peptide sequence 45A- 46Q-47G-48K-49G-50F-51I-52T-53M-54A-55L-56N-57S-58C, which matched with human somatostatin (hSST), a known antiangiogenic factor, was located in the second loop between the first and second a-helices in the threedimensional structure of buPRL, obtained by homology modelling. The synthetic peptide matching with SST sequence was found to exhibit antiangiogenic activity in both in vitro and ex vivo assays. It was also observed that all the peptides related to buPRL could antagonize the vascular endothelial growth factor (VEGF) and bradykinin (BK)- dependent production of endothelial nitric oxide (NO), which is a pre-requisite for endothelial tube formation. It is concluded therefore that an internal sequence in buPRL and peptide fragments derived from cathepsin-digested buPRL exhibit antiangiogenic activities.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
Keywords:Antiangiogenesis; Buffalo Prolactin; Prolactin-derived Peptide
ID Code:64827
Deposited On:17 Oct 2011 03:50
Last Modified:18 May 2016 13:06

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