ABSTRACT
The immense role of glycosylation in protein structure stabilization, as well as proper biological functioning, is well documented. Glycosylation happens to be the most common and crucial post-translational modification that is carried out just after protein synthesis by specific enzymes in the endoplasmic reticulum (ER) and Golgi apparatus (GA). Lectins are host cell surface proteins that identify and bind to their target glycans. Moreover, mammalian cells turning cancerous are reported to be associated with changes in glycosylation profile on their surface, indicating how powerfully glycosylation drives the development and angiogenesis of tumors, culminating in metastasis. Glycosylation regulates antibody functioning in a big way. The presence and quantity of fucose and galactose on the Fc region of immunoglobulins modulate their binding affinity to their own receptors located on immune cells. A few adhesion molecules of tumor cells, such as mucins, selectins, cadherins, integrins, laminins, etc., have been discussed here in terms of their altered glycome. A unique feature associated with metastasis is the development of neo-vasculature from preexisting blood vessels. Aberrations in glycosylation patterns have been identified among 128the causes of angiogenesis of metastatic tumors. Equipped with adequate knowledge of the altered glycome of various types of cancers, their reliable diagnosis, prevention, and therapy is fast becoming a possibility. Glycome remodeling enzymes could be a potential route of preventing as well as treating tumors at large. The present was designed to review the role of glycans in metastasis with the intention of highlighting the possible role of glycans in the therapeutic intervention of cancer. Future insights in this context have also been included in the chapter.
