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Cancer glycobiology

Antônio F Silva-Filho, Wanessa L B Sena, Luiza R A Lima, Lidiane V N Carvalho, Michelly C Pereira, Lucas G S Santos, Renata V C Santos, Lucas B Tavares, Maira G R Pitta, Moacyr J B M Rêgo
Post-translational and co-translational enzymatic addition of glycans (glycosylation) to proteins, lipids, and other carbohydrates, is a powerful regulator of the molecular machinery involved in cell cycle, adhesion, invasion, and signal transduction, and is usually seen in both in vivo and in vitro cancer models. Glycosyltransferases can alter the glycosylation pattern of normal cells, subsequently leading to the establishment and progression of several diseases, including cancer. Furthermore, a growing amount of research has shown that different oxygen tensions, mainly hypoxia, leads to a markedly altered glycosylation, resulting in altered glycan-receptor interactions...
April 3, 2017: Cellular Physiology and Biochemistry
Shinichiro Shinzaki, Hideki Iijima, Hironobu Fujii, Yoshihiro Kamada, Tetsuji Naka, Tetsuo Takehara, Eiji Miyoshi
Oligosaccharide modifications play an essential role in various inflammatory diseases and cancers, but their pathophysiologic roles, especially in inflammation, are not clear. Inflammatory bowel disease (IBD) is an intractable chronic inflammatory disorder with an unknown aetiology, and the number of patients with IBD is increasing throughout the world. Certain types of immunosuppressant drugs, such as corticosteroids, are effective for IBD, suggesting that immune function is closely associated with the pathophysiology of IBD...
March 7, 2017: Journal of Biochemistry
R R Drake, T W Powers, E E Jones, E Bruner, A S Mehta, P M Angel
Glycosylated proteins account for a majority of the posttranslation modifications of cell surface, secreted, and circulating proteins. Within the tumor microenvironment, the presence of immune cells, extracellular matrix proteins, cell surface receptors, and interactions between stroma and tumor cells are all processes mediated by glycan binding and recognition reactions. Changes in glycosylation during tumorigenesis are well documented to occur and affect all of these associated adhesion and regulatory functions...
2017: Advances in Cancer Research
Leonardo Freire-de-Lima, Jose Osvaldo Previato, Lucia Mendonça-Previato
No abstract text is available yet for this article.
2016: Frontiers in Oncology
Jerrard M Hayes, Mark R Wormald, Pauline M Rudd, Gavin P Davey
Therapeutic antibodies hold great promise for the treatment of cancer and autoimmune diseases, and developments in antibody-drug conjugates and bispecific antibodies continue to enhance treatment options for patients. Immunoglobulin (Ig) G antibodies are proteins with complex modifications, which have a significant impact on their function. The most important of these modifications is glycosylation, the addition of conserved glycans to the antibody Fc region, which is critical for its interaction with the immune system and induction of effector activities such as antibody-dependent cell cytotoxicity, complement activation and phagocytosis...
2016: Journal of Inflammation Research
Chao Li, Lai-Xi Wang
Recent advances in glycobiology have implicated essential roles of oligosaccharides and glycoconjugates in many important biological recognition processes, including intracellular signaling, cell adhesion, cell differentiation, cancer progression, host-pathogen interactions, and immune responses. A detailed understanding of the biological functions, as well as the development of carbohydrate-based therapeutics, often requires structurally well-defined oligosaccharides and glycoconjugates, which are usually difficult to isolate in pure form from natural sources...
2016: Advances in Carbohydrate Chemistry and Biochemistry
Wan-Ling Ho, Wen-Ming Hsu, Min-Chuan Huang, Kenji Kadomatsu, Akira Nakagawara
Glycosylation is the most complex post-translational modification of proteins. Altered glycans on the tumor- and host-cell surface and in the tumor microenvironment have been identified to mediate critical events in cancer pathogenesis and progression. Tumor-associated glycan changes comprise increased branching of N-glycans, higher density of O-glycans, generation of truncated versions of normal counterparts, and generation of unusual forms of terminal structures arising from sialylation and fucosylation. The functional role of tumor-associated glycans (Tn, sTn, T, and sLe(a/x)) is dependent on the interaction with lectins...
September 29, 2016: Journal of Hematology & Oncology
Yasuhiko Kizuka, Sho Funayama, Hidehiko Shogomori, Miyako Nakano, Kazuki Nakajima, Ritsuko Oka, Shinobu Kitazume, Yoshiki Yamaguchi, Masahiro Sano, Hiroaki Korekane, Tsui-Ling Hsu, Hsiu-Yu Lee, Chi-Huey Wong, Naoyuki Taniguchi
Fucose, a terminal sugar in glycoconjugates, critically regulates various physiological and pathological phenomena, including cancer development and inflammation. However, there are currently no probes for efficient labeling and detection of this sugar. We chemically synthesized a novel series of alkynyl-fucose analogs as probe candidates and found that 7-alkynyl-fucose gave the highest labeling efficiency and low cytotoxicity. Among the fucose analogs, 7-alkynyl-fucose was the best substrate against all five fucosyltransferases examined...
July 21, 2016: Cell Chemical Biology
Andreas Geissner, Peter H Seeberger
A major branch of glycobiology and glycan-focused biomedicine studies the interaction between carbohydrates and other biopolymers, most importantly, glycan-binding proteins. Today, this research into glycan-biopolymer interaction is unthinkable without glycan arrays, tools that enable high-throughput analysis of carbohydrate interaction partners. Glycan arrays offer many applications in basic biochemical research, for example, defining the specificity of glycosyltransferases and lectins such as immune receptors...
June 12, 2016: Annual Review of Analytical Chemistry
Lise Boon, Estefania Ugarte-Berzal, Jennifer Vandooren, Ghislain Opdenakker
Matrix metalloproteases (MMPs) are crucial components of a complex and dynamic network of proteases. With a wide range of potential substrates, their production and activity are tightly controlled by a combination of signalling events, zymogen activation, post-translational modifications and extracellular inhibition. Slight imbalances may result in the initiation or progression of specific disease states, such as cancer and pathological inflammation. As glycosylation modifies the structures and functions of glycoproteins and many MMPs contain N- or O-linked oligosaccharides, we examine, compare and evaluate the evidence for whether glycosylation affects MMP catalytic activity and other functions...
June 1, 2016: Biochemical Journal
Sharmeen Nishat, Peter R Andreana
Carbohydrates are regarded as promising targets for vaccine development against infectious disease because cell surface glycans on many infectious agents are attributed to playing an important role in pathogenesis. In addition, oncogenic transformation of normal cells, in many cases, is associated with aberrant glycosylation of the cell surface glycan generating tumor associated carbohydrate antigens (TACAs). Technological advances in glycobiology have added a new dimension to immunotherapy when considering carbohydrates as key targets in developing safe and effective vaccines to combat cancer, bacterial infections, viral infections, etc...
2016: Vaccines
Kekoa Taparra, Phuoc T Tran, Natasha E Zachara
The epithelial-mesenchymal transition (EMT) is a highly conserved program necessary for orchestrating distant cell migration during embryonic development. Multiple studies in cancer have demonstrated a critical role for EMT during the initial stages of tumorigenesis and later during tumor invasion. Transcription factors (TFs) such as SNAIL, TWIST, and ZEB are master EMT regulators that are aberrantly overexpressed in many malignancies. Recent evidence correlates EMT-related transcriptomic alterations with metabolic reprograming in cancer...
2016: Frontiers in Oncology
Yasuhiko Kizuka, Naoyuki Taniguchi
N-glycan, a fundamental and versatile protein modification in mammals, plays critical roles in various physiological and pathological events including cancer progression. The formation of N-glycan branches catalyzed by specific N-acetylglucosaminyltransferases [GnT-III, GnT-IVs, GnT-V, GnT-IX (Vb)] and a fucosyltransferase, Fut8, provides functionally diverse N-glycosylated proteins. Aberrations of these branches are often found in cancer cells and are profoundly involved in cancer growth, invasion and metastasis...
April 28, 2016: Biomolecules
Naoyuki Taniguchi, Yasuhiko Kizuka, Shinji Takamatsu, Eiji Miyoshi, Congxiao Gao, Keiichiro Suzuki, Shinobu Kitazume, Kazuaki Ohtsubo
Reduction-oxidation (redox) response is one of the most important biological phenomena. The concept introduced by Helmut Sies encouraged many researchers to examine oxidative stress under pathophysiological conditions. Our group has been interested in redox regulation under oxidative stress as well as glycobiology in relation to disease. Current studies by our group and other groups indicate that functional and structural changes of glycans are regulated by redox responses resulting from the generation of reactive oxygen species (ROS) or reactive nitrogen species (RNS) in various diseases including cancer, diabetes, neurodegenerative disease such as Parkinson disease, Alzheimer's disease and amyotrophic lateral sclerosis (ALS), and chronic obstructive pulmonary disease (COPD), even though very few investigators appear to be aware of these facts...
April 1, 2016: Archives of Biochemistry and Biophysics
Matthew P Campbell, Nicolle H Packer
BACKGROUND: UniCarbKB aims to provide a resource for the representation of mammalian glycobiology knowledge by providing a curated database of structural and experimental data, supported by a web application that allows users to easily find and view richly annotated information. The database comprises two levels of annotation (i) global-specific data of oligosaccharides released and characterised from single purified glycoproteins and (ii) information pertaining to site-specific glycan heterogeneity...
August 2016: Biochimica et Biophysica Acta
Yuqin Shang, Yun Zeng, Yong Zeng
Protein glycosylation is one of the key processes that play essential roles in biological functions and dysfunctions. However, progress in glycomics has considerably lagged behind genomics and proteomics, due in part to the enormous challenges in analysis of glycans. Here we present a new integrated and automated microfluidic lectin barcode platform to substantially improve the performance of lectin array for focused glycomic profiling. The chip design and flow control were optimized to promote the lectin-glycan binding kinetics and speed of lectin microarray...
February 2, 2016: Scientific Reports
A V Timoshenko, J Lanteigne, K Kozak
Galectins, a family of soluble β-galactoside-binding proteins, are involved in the regulation of various cellular functions, which are essential for adaptive cellular stress responses (CSRs). Although expression patterns of galectins and galectin-binding glycans change during tissue development and cancer, the requirement and role of galectin networks in the CSRs are not completely understood. In this study, we report that the treatment of human promyelocytic HL-60 cells with stimuli mimicking hypoxia (CoCl2), inducing the endoplasmic reticulum stress (tunicamycin), and stimulating cell differentiation, result in stress-specific differential expression of galectin transcripts...
February 2016: Molecular and Cellular Biochemistry
Elliot C Woods, Nathan A Yee, Jeff Shen, Carolyn R Bertozzi
Synthetic glycopolymers that emulate cell-surface mucins have been used to elucidate the role of mucin overexpression in cancer. However, because they are internalized within hours, these glycopolymers could not be employed to probe processes that occur on longer time scales. In this work, we tested a panel of glycopolymers bearing a variety of lipids to identify those that persist on cell membranes. Strikingly, we found that cholesterylamine (CholA) anchored glycopolymers are internalized into vesicles that serve as depots for delivery back to the cell surface, allowing for the display of cell-surface glycopolymers for at least ten days, even while the cells are dividing...
December 21, 2015: Angewandte Chemie
Lili Tian, Dachuan Shen, Xiaodong Li, Xiu Shan, Xiaoqi Wang, Qiu Yan, Jiwei Liu
The epithelial-mesenchymal transition (EMT) is an important factor in lung cancer metastasis, and targeting EMT is a potential therapeutic strategy. Fucosyltransferase IV (FUT4) and its synthetic cancer sugar antigen Lewis Y (LeY) was abnormally elevated in many cancers. In this study, a traditional Chinese medicine ginsenoside Rg3 was used to investigate whether its inhibition to EMT and invasion of lung cancer is by the glycobiology mechanism. We found that Rg3 treatment (25, 50, 100 μg/ml) inhibited cell migration and invasion by wound-healing and transwell assays...
January 12, 2016: Oncotarget
Stephanie Holst, Anna J M Deuss, Gabi W van Pelt, Sandra J van Vliet, Juan J Garcia-Vallejo, Carolien A M Koeleman, André M Deelder, Wilma E Mesker, Rob A Tollenaar, Yoann Rombouts, Manfred Wuhrer
Various cancers such as colorectal cancer (CRC) are associated with alterations in protein glycosylation. CRC cell lines are frequently used to study these (glyco)biological changes and their mechanisms. However, differences between CRC cell lines with regard to their glycosylation have hitherto been largely neglected. Here, we comprehensively characterized the N-glycan profiles of 25 different CRC cell lines, derived from primary tumors and metastatic sites, in order to investigate their potential as glycobiological tumor model systems and to reveal glycans associated with cell line phenotypes...
January 2016: Molecular & Cellular Proteomics: MCP
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