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Glycosylation in Cancer
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Glycosylation in Cancer

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Applied Biosciences and Bioengineering".

Deadline for manuscript submissions: closed (31 October 2020) | Viewed by 5460

Special Issue Editors

Dr. Jennifer Munkley

E-Mail Website
Guest Editor
Institute of Genetic Medicine, Newcastle University, International Centre for Life, Newcastle Upon Tyne NE1 3BZ, UK
Interests: glycosylation; glycans; prostate cancer; metastasis; biomarkers; therapeutics
Special Issues, Collections and Topics in MDPI journals
Dr. Emma Scott

E-Mail Website
Guest Editor
Institute of Genetic Medicine, Newcastle University, International Centre for Life, Newcastle Upon Tyne NE1 3BZ, UK
Interests: glycans in prostate cancer; cancer immunology; biomarkers; therapeutics

Special Issue Information

Dear Colleagues,

This Special Issue is devoted to Glycosylation in Cancer. Cell surface carbohydrates, known as glycans, are often aberrantly expressed or found at atypical levels in cancer. Aberrant glycosylation has roles in all of the cancer hallmarks and can impact all steps in tumour progression. New advances in the technologies to study glycans have spurred a renewed interest in this exciting area. Glycan based targeting strategies are currently being tested in clinical trials and are a rich and untapped frontier for development. Glycans have also shown huge promise as cancer biomarkers to improve patient stratification and guide personalized therapy. We invite submissions exploring the role of glycans in all aspects of cancer biology.

Dr. Jennifer Munkley
Dr. Emma Scott
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2400 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Glycans in cancer
  • Biomarkers
  • Therapeutics

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Published Papers (2 papers)

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Research

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12 pages, 4374 KiB  
Article
Glycan-Dependent and -Independent Dual Recognition between DC-SIGN and Type II Serine Protease MSPL/TMPRSS13 in Colorectal Cancer Cells
by Motohiro Nonaka, Shogo Matsumoto, Bruce Yong Ma, Hiroshi Kido, Nana Kawasaki, Nobuko Kawasaki and Toshisuke Kawasaki
Appl. Sci. 2020, 10(8), 2687; https://doi.org/10.3390/app10082687 - 13 Apr 2020
Cited by 1 | Viewed by 2729
Abstract
A class of glycoproteins such as carcinoembryonic antigen (CEA)/CEA-related cell adhesion molecule 1(CEACAM1), CD26 (DPPIV), and mac-2 binding protein (Mac-2BP) harbor tumor-associated glycans in colorectal cancer. In this study, we identified type II transmembrane mosaic serine protease large-form (MSPL) and its splice variant [...] Read more.
A class of glycoproteins such as carcinoembryonic antigen (CEA)/CEA-related cell adhesion molecule 1(CEACAM1), CD26 (DPPIV), and mac-2 binding protein (Mac-2BP) harbor tumor-associated glycans in colorectal cancer. In this study, we identified type II transmembrane mosaic serine protease large-form (MSPL) and its splice variant transmembrane protease serine 13 (TMPRSS13) as ligands of Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) on the colorectal cancer cells. DC-SIGN is a C-type lectin expressed on dendritic cells, serves as a pattern recognition receptor for numerous pathogens such as human immunodeficiency virus (HIV) and M. tuberculosis. DC-SIGN recognizes these glycoproteins in a Ca2+ dependent manner. Meanwhile, we found that MSPL proteolytically cleaves DC-SIGN in addition to the above glycan-mediated recognition. DC-SIGN was degraded more efficiently by MSPL when treated with ethylenediaminetetraacetic acid (EDTA), suggesting that glycan-dependent interaction of the two molecules partially blocked DC-SIGN degradation. Our findings uncovered a dual recognition system between DC-SIGN and MSPL/TMPRSS13, providing new insight into the mechanism underlying colorectal tumor microenvironment. Full article
(This article belongs to the Special Issue Glycosylation in Cancer)
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Review

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16 pages, 914 KiB  
Review
Status Quo of Glycosylation in Cancer: What Is, What Is Not and What Is to Be
by Manikandan Muthu, Judy Gopal, Sechul Chun, Anna Jacintha Prameela Devadoss and Jae-Wook Oh
Appl. Sci. 2020, 10(23), 8401; https://doi.org/10.3390/app10238401 - 25 Nov 2020
Viewed by 2283
Abstract
Glycobiology is gaining paramount importance for its influence on diseases as a consequence of a fundamental understanding of the underlying processes involved in them. Cancer is still posing threats to human health and welfare and therapies are perpetually being sought. Glycans are selectively [...] Read more.
Glycobiology is gaining paramount importance for its influence on diseases as a consequence of a fundamental understanding of the underlying processes involved in them. Cancer is still posing threats to human health and welfare and therapies are perpetually being sought. Glycans are selectively attached to proteins and lipids during glycosylation, and these hold anchorage positions in many important biological processes involved in cancer through their altered expression or activity upon malignant transformation. Aberrant glycosylation is well established as a hallmark of cancer, linked to tumor development and metastasis. The analytical inputs and milestones achieved and the characterization and detection of glycosylation in cancer have been summarized in this review. The milestones achieved in cancer research through inputs from glycosylation have been highlighted. With almost 70% of biopharmaceuticals being glycoproteins and almost 80% of cancer biomarkers being glycan in origin, glycosylation has a lot of say in cancer prognosis and diagnosis. The future of glycosylation in cancer and the lacunae in the smooth channelization of state-of-the-art technologies for taking this research knowledge from bench top to bedside (actual clinical settings) is speculated upon. The incorporation of cross-disciplinary integrated approaches and nano-instrumentation sophistications are proposed for achieving scaling up. Full article
(This article belongs to the Special Issue Glycosylation in Cancer)
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