scholarly journals L1CAM as an E-selectin Ligand in Colon Cancer

2020 ◽  
Vol 21 (21) ◽  
pp. 8286
Author(s):  
Fanny M. Deschepper ◽  
Roberta Zoppi ◽  
Martina Pirro ◽  
Paul J. Hensbergen ◽  
Fabio Dall’Olio ◽  
...  

Metastasis is the main cause of death among colorectal cancer (CRC) patients. E-selectin and its carbohydrate ligands, including sialyl Lewis X (sLeX) antigen, are key players in the binding of circulating tumor cells to the endothelium, which is one of the major events leading to organ invasion. Nevertheless, the identity of the glycoprotein scaffolds presenting these glycans in CRC remains unclear. In this study, we firstly have characterized the glycoengineered cell line SW620 transfected with the fucosyltransferase 6 (FUT6) coding for the α1,3-fucosyltransferase 6 (FUT6), which is the main enzyme responsible for the synthesis of sLeX in CRC. The SW620FUT6 cell line expressed high levels of sLeX antigen and E-selectin ligands. Moreover, it displayed increased migration ability. E-selectin ligand glycoproteins were isolated from the SW620FUT6 cell line, identified by mass spectrometry, and validated by flow cytometry and Western blot (WB). The most prominent E-selectin ligand we identified was the neural cell adhesion molecule L1 (L1CAM). Previous studies have shown association of L1CAM with metastasis in cancer, thus the novel role as E-selectin counter-receptor contributes to understand the molecular mechanism involving L1CAM in metastasis formation.

1997 ◽  
Vol 230 (3) ◽  
pp. 546-551 ◽  
Author(s):  
Chikako Mitsuoka ◽  
Naoko Kawakami-Kimura ◽  
Mikiko Kasugai-Sawada ◽  
Nozomu Hiraiwa ◽  
Ken'ichi Toda ◽  
...  

Biology ◽  
2017 ◽  
Vol 6 (4) ◽  
pp. 16 ◽  
Author(s):  
Marco Trinchera ◽  
Adele Aronica ◽  
Fabio Dall’Olio

1998 ◽  
Vol 273 (18) ◽  
pp. 11225-11233 ◽  
Author(s):  
Chikako Mitsuoka ◽  
Mikiko Sawada-Kasugai ◽  
Keiko Ando-Furui ◽  
Mineko Izawa ◽  
Hayao Nakanishi ◽  
...  

Biochemistry ◽  
2001 ◽  
Vol 40 (18) ◽  
pp. 5382-5391 ◽  
Author(s):  
Kendra G. Bowman ◽  
Brian N. Cook ◽  
Christopher L. de Graffenried ◽  
Carolyn R. Bertozzi

Blood ◽  
2002 ◽  
Vol 99 (7) ◽  
pp. 2609-2611 ◽  
Author(s):  
Tero Satomaa ◽  
Ossi Renkonen ◽  
Jari Helin ◽  
Juha Kirveskari ◽  
Antti Mäkitie ◽  
...  

Leukocyte traffic into lymph nodes and sites of inflammation is guided by L-selectin. Experiments performed in vitro and with gene-deleted mice suggest that CD34 recognizes L-selectin if decorated by 6-sulfo sialyl Lewis x (sLex) saccharides and the MECA-79 epitope. However, very little is known about glycosylation of human L-selectin ligands. We report here on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) profiles of N- and O-linked oligosaccharide fractions from human tonsillar endothelial CD34. All detected O-glycans were sialylated; some were also monosulfated or monosulfated and monofucosylated. If a given CD34-glycan may carry all requirements for L-selectin recognition, that is, both 6-sulfo-sLex and MECA-79 epitopes, only one O-glycan fraction, O-9, SA2Hex3HexNAc3- Fuc1(SO3)1, meets the criteria. A candidate structure is SAα2-3Galβ1-4(Fucα1-3)(6-sulfo)GlcNAcβ1-3Galβ1-3(SAα2-3Galβ1-4GlcNAcβ1-6)GalNAc. However, if sulfo sLex glycans are supplemented with separate sulfated, nonfucosylated O-glycans, saccharides in O-6, O-8, or O-9, putatively carrying MECA-79 epitopes, could form multiglycan binding epitopes for L-selectin.


2012 ◽  
Vol 287 (43) ◽  
pp. 35922-35933 ◽  
Author(s):  
Chunsheng Jin ◽  
Anna-Karin Hultgård Ekwall ◽  
Johan Bylund ◽  
Lena Björkman ◽  
Ruby P. Estrella ◽  
...  

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