Open AccessTumor cell N-glycans in metastasis.
Author(s) -
Piotr Laidler,
Anna Lityń́ska
Publication year - 1997
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1997_4431
Subject(s) - fucosylation , glycosylation , selectin , galectin , cell adhesion molecule , cell adhesion , immunoglobulin superfamily , glycan , metastasis , l1 , chemistry , integrin , neural cell adhesion molecule , sialyl lewis x , n acetylneuraminic acid , microbiology and biotechnology , cell , sialic acid , glycoprotein , biochemistry , biology , cancer , gene , genetics
Metastasis accounts for most of deaths caused by cancer. The increasing body of evidence suggests that changes in N-glycosylation of tumor cell proteins such as increased branching, increased sialylation, polysialylation, decreased fucosylation, enhanced formation of Lewis X and sialyl Lewis X antigens are among important factors determining metastatic potential of tumor cell. Most of the adhesion proteins, e.g., integrins, members of immunoglobulin superfamily, and cadherins are heavily N-glycosylated. The other proteins involved in adhesion, like galectins and type-C selectins, recognize N-glycans as a part of their specific ligands. In this review we focus on recent reports concerning the contribution of N-glycosylation of tumor cell adhesion molecules and some selected membrane proteins in the tumor invasion and metastasis.