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      https://www.ias.ac.in/article/fulltext/jbsc/036/02/0341-0354

    • Keywords

       

      Antiangiogenesis; buffalo prolactin; prolactin-derived peptide

    • 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 α-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.

    • Author Affiliations

       

      Jaeok Lee1 Syamantak Majumder2 Suvro Chatterjee2 Kambadur Muralidhar1

      1. Hormone Research Laboratory, Department of Zoology, University of Delhi, Delhi, India
      2. AU-KBC Research Centre, MIT Campus, Anna University, Chennai, India
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    • Supplementary Material

       
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