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      Glycosylation in the Tumor Microenvironment: Implications for Tumor Angiogenesis and Metastasis

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          Abstract

          Just as oncogene activation and tumor suppressor loss are hallmarks of tumor development, emerging evidence indicates that tumor microenvironment-mediated changes in glycosylation play a crucial functional role in tumor progression and metastasis. Hypoxia and inflammatory events regulate protein glycosylation in tumor cells and associated stromal cells in the tumor microenvironment, which facilitates tumor progression and also modulates a patient’s response to anti-cancer therapeutics. In this review, we highlight the impact of altered glycosylation on angiogenic signaling and endothelial cell adhesion, and the critical consequences of these changes in tumor behavior.

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          The endothelial glycocalyx: composition, functions, and visualization

          Sietze Reitsma, Dick Slaaf, Hans Vink … (2007)
          This review aims at presenting state-of-the-art knowledge on the composition and functions of the endothelial glycocalyx. The endothelial glycocalyx is a network of membrane-bound proteoglycans and glycoproteins, covering the endothelium luminally. Both endothelium- and plasma-derived soluble molecules integrate into this mesh. Over the past decade, insight has been gained into the role of the glycocalyx in vascular physiology and pathology, including mechanotransduction, hemostasis, signaling, and blood cell–vessel wall interactions. The contribution of the glycocalyx to diabetes, ischemia/reperfusion, and atherosclerosis is also reviewed. Experimental data from the micro- and macrocirculation alludes at a vasculoprotective role for the glycocalyx. Assessing this possible role of the endothelial glycocalyx requires reliable visualization of this delicate layer, which is a great challenge. An overview is given of the various ways in which the endothelial glycocalyx has been visualized up to now, including first data from two-photon microscopic imaging.
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            Heparan sulphate proteoglycans fine-tune mammalian physiology.

            Jeffrey Esko, Manuela Schuksz, Joseph R. Bishop … (2007)
            Heparan sulphate proteoglycans reside on the plasma membrane of all animal cells studied so far and are a major component of extracellular matrices. Studies of model organisms and human diseases have demonstrated their importance in development and normal physiology. A recurrent theme is the electrostatic interaction of the heparan sulphate chains with protein ligands, which affects metabolism, transport, information transfer, support and regulation in all organ systems. The importance of these interactions is exemplified by phenotypic studies of mice and humans bearing mutations in the core proteins or the biosynthetic enzymes responsible for assembling the heparan sulphate chains.
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              Inhibition of the Glycolytic Activator PFKFB3 in Endothelium Induces Tumor Vessel Normalization, Impairs Metastasis, and Improves Chemotherapy.

              Anna Cantelmo, Lena-Christin Conradi, Aleksandra Brajic … (2017)
              Abnormal tumor vessels promote metastasis and impair chemotherapy. Hence, tumor vessel normalization (TVN) is emerging as an anti-cancer treatment. Here, we show that tumor endothelial cells (ECs) have a hyper-glycolytic metabolism, shunting intermediates to nucleotide synthesis. EC haplo-deficiency or blockade of the glycolytic activator PFKFB3 did not affect tumor growth, but reduced cancer cell invasion, intravasation, and metastasis by normalizing tumor vessels, which improved vessel maturation and perfusion. Mechanistically, PFKFB3 inhibition tightened the vascular barrier by reducing VE-cadherin endocytosis in ECs, and rendering pericytes more quiescent and adhesive (via upregulation of N-cadherin) through glycolysis reduction; it also lowered the expression of cancer cell adhesion molecules in ECs by decreasing NF-κB signaling. PFKFB3-blockade treatment also improved chemotherapy of primary and metastatic tumors.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Cells
                Journal ID (iso-abbrev): Cells
                Journal ID (publisher-id): cells
                Title: Cells
                Publisher: MDPI
                ISSN (Electronic): 2073-4409
                Publication date (Electronic): 05 June 2019
                Publication date Collection: June 2019
                Volume: 8
                Issue: 6
                Electronic Location Identifier: 544
                Affiliations
                [1 ]Center for Biomedical Mass Spectrometry, Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA; cecmsms@ 123456bu.edu
                [2 ]Department of Pathology and Laboratory Medicine, Boston University School of Medicine, Boston, MA 02118, USA
                Author notes
                [* ]Correspondence: kbc36@ 123456bu.edu (K.B.C.); nrahmi@ 123456bu.edu (N.R.); Tel.: +1-617-358-1330 (K.B.C.); +1-617-358-2432 (N.R.)
                Author information
                https://orcid.org/0000-0001-5514-9652
                Article
                Publisher ID: cells-08-00544
                DOI: 10.3390/cells8060544
                PMC ID: 6627046
                PubMed ID: 31195728
                SO-VID: 89df5f78-ddb0-48c8-8b09-346509760a70
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 14 May 2019
                Date accepted : 01 June 2019
                Categories
                Subject: Review

                Keywords: glycosylation,tumor microenvironment,angiogenesis,metastasis,n-glycosylation,o-glycosylation,glycosaminoglycans,endothelial,hypoxia,inflammation
                Data availability:
                Keywords: glycosylation, tumor microenvironment, angiogenesis, metastasis, n-glycosylation, o-glycosylation, glycosaminoglycans, endothelial, hypoxia, inflammation

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