Peptides 23 (2002) 999–1010 Role of SA–Le a and E-selectin in metastasis assessed with peptide antagonist Insug O. a , Laszlo Otvos, Jr. a , Thomas Kieber-Emmons b , Magdalena Blaszczyk-Thurin a, a The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA b Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA Received 10 August 2001; accepted 10 December 2001 Abstract E-selectin ligand Sialyl–Lewis a (SA–Le a ) carbohydrate is expressed on many carcinomas. Peptide mimicking SA–Le a (DLWD- WVVGKPAG) was previously selected from a recombinant library by screening with monoclonal antibody (MAb) NS19-9. In this study, the residues critical for interaction with the NS19-9 were mapped using peptide array generated by substitution of various amino acid residues. The replacement of Trp 5 with Phe resulted in a change of peptide’s secondary structure and increased binding with MAb and E-selectin, suggesting improved carbohydrate mimicry. Colonization of tumor cells expressing SA–Le a was blocked by the peptide and was completely abolished in E-selectin knock out mice. The data suggest the critical role of carbohydrate antigens and E-selectin in metastasis and that peptides mimicking carbohydrate antigens can function as antagonists of this process. © 2002 Published by Elsevier Science Inc. Keywords: Carbohydrate structure; Sialyl–Lewis a; Peptide mimics; E-selectin; Tumor metastasis 1. Introduction Tumor metastasis is a multistep process requiring detachment of malignant cells from the primary tumor, penetration of blood or lymph vessels and attachment to en- dothelium of distant organs and formation of a new tumor [44]. E-selectin is a tumor necrosis factor-(TNF-) and interleukin-1(IL-1)-inducible, calcium-dependent adhe- sion molecule, that is expressed on vascular endothelium and it is postulated to mediate the initial interaction with tumor cells [9,27,34,60]. E-selectin was also demonstrated to mediate leukocytes rolling along the vessel wall in the leukocyte endothelial cascade involved in the inflammatory response [55]. E-selectin binds to glycoconjugates carrying the terminal tetrasaccharide sialyl–LeX (SA–LeX), NeuAc2,3Gal1, 4(Fuc1,3)GlcNAc1,3Gal1,4Glc1-R [2] and its po- sitional isomer, SA–Le a , NeuAc2,3Gal1,3(Fuc1,4) GlcNAc1,3Gal1,4Glc1-R [1] that are expressed on most of carcinoma cells (SA–LeX and/or SA–Le a ) and leukocytes (SA–LeX). Although adhesion pathways utilized by different tumors show considerable diversity, recent re- ports suggest that E-selectin and SA–Le a and/or SA–LeX Corresponding author. Tel.: +1-215-898-3855; fax: +1-215-898-3868. E-mail address: mthurin@wistar.upenn.edu (M. Blaszczyk-Thurin). carbohydrate ligands, might be involved in tumor metas- tasis [60,65]. Cancer cells that express both SA–Le a and SA–LeX undergo SA–Le a -mediated adhesion almost ex- clusively, possibly due to the higher affinity of E-selectin for the SA–Le a structure [1]. The expression of ligands for E-selectin by both neu- trophils and cancer cells raises the possibility that the basic mechanism that underlie initial step of metastases formation, i.e. interaction of endothelial selectins with the tumor-associated carbohydrate ligands SA–LeX and/or SA–Le a is equivalent to that mediating rolling step in the in- flammatory process. The crucial role of selectin-dependent neutrophil adhesion and carcinoma cell adhesion implies that in vivo blockage of selectin-dependent interactions can decrease leukocyte mobilization and the incidence of metastases, respectively. Various selectin inhibitors of selectin-dependent interaction including peptidic inhibitors have been considered as an anti-inflammatory approach by many laboratories [6,18,36,38,39,41,47,51,56]. Although there is no direct evidence of involvement of E-selectin in naturally occurring tumor metastases in hu- mans, several studies demonstrate the selectin mediated ad- hesion of tumor cells is a key event in metastasis process in vivo. The administration of E-selectin specific antibody and soluble E-selectin was shown to abrogate the formation of hepatic metastasis and lung colony formation in vivo in 0196-9781/02/$ – see front matter © 2002 Published by Elsevier Science Inc. PII:S0196-9781(02)00024-4