Review
BibTex RIS Cite

Kanser Metabolizmasında ve Metastazında Glikanların Önemi

Year 2021, Volume: 6 Issue: 2, 112 - 119, 30.08.2021

Nebiye Pelin Türker , Elvan Bakar

https://doi.org/10.51754/cusbed.867416
Cited By: 1

Abstract

Glikobiyolojinin kanser mekanizmalarının anlaşılmasındaki rolü, teşhis uygulamaları ve terapötik stratejiler için bir dizi hedef sağlaması, bu bilim alanının kanser araştırmalarındaki önemini her geçen gün arttırmaktadır. Glikozilasyonun, çeşitli fizyopatolojik süreçleri kontrol eden önemli düzenleyici bir mekanizma olarak işlev görebileceği ön görülmektedir. Hücrelerdeki glikozilasyon değişimleri ve bu değişimlerin hastalıklarla olan bağlantıları, glikomun önemli ölçüde biyolojik bilgi içerdiğini göstermektedir. Glikan zincirlerinin dallanma ve uzunluklarındaki değişiklikler, yapılarında yer alan karbohidratların çeşidi, bu moleküllerin biyolojik fonksiyonlarının değişmesine neden olmaktadır. Bununla birlikte glikan bağlayıcı proteinlerin biyolojik fonksiyonlarının karakterize edilmesi, kanser araştırmalarına önemli katkılar sağlamaktadır. Farklı glikokonjugat tipleri, anahtar kanser hücresi süreçlerine ve aynı zamanda tümör mikro-ortamına müdahale ederek, kanserin ilerlemesine yol açmaktadır.

Keywords

Kanser Metastaz Glikan Glikolizasyon

References

  • Arnold JN, Saldova R, Hamid UM, Rudd PM (2008) Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics, 8: 3284-93. https://doi.org/10.1002/pmic.200800163
  • Aryal RP, Ju T, Cummings RD (2010) The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase. J Biol Chem, 285: 2456-62. https://doi.org/10.1074/jbc.M109.065169
  • Baldus SE, Zirbes TK, Monig SP, Engel S, Monaca E, Rafiqpoor K, Hanisch FG, Hanski C, Thiele J, Pichlmaier H, Dienes HP (1998) Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: Sialosyl-Lewis(a), Sialosyl-Lewis(x) and sialosyl-Tn. Tumour Biol, 19: 445-53. https://doi.org/10.1159/000030036
  • Bharadwaj AG, Kovar JL, Loughman E, Elowsky C, Oakley GG, Simpson MA (2009) Spontaneous Metastasis of Prostate Cancer Is Promoted by Excess Hyaluronan Synthesis and Processing. American Journal of Pathology, 174: 1027-1036. https://doi.org/10.2353/ajpath.2009.080501
  • Borsig L, Wong R, Feramisco J, Nadeau DR, Varki NM, Varki A (2001) Heparin and cancer revisited: Mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis (vol 98, pg 3352, 2001).
  • Proceedings of the National Academy of Sciences of the United States of America, 98: 5369-5369.
  • Carvalho AS, Harduin-Lepers A, Magalhaes A, Machado E, Mendes N, Costa LT, Matthiesen R, Almeida R, Costa J, Reis CA (2010) Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells. Int J Biochem Cell Biol, 42: 80-9. https://doi.org/10.1016/j.biocel.2009.09.010
  • Croci DO, Cerliani JP, Dalotto-Moreno T, Mendez-Huergo SP, Mascanfroni ID, Dergan-Dylon S, Toscano MA, Caramelo JJ, Garcia-Vallejo JJ, Ouyang J, Mesri EA, Junttila MR, Bais C, Shipp MA, Salatino M, Rabinovich GA (2014) Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors. Cell, 156: 744-58. https://doi.org/10.1016/j.cell.2014.01.043
  • da Cunha CB, Oliveira C, Wen X, Gomes B, Sousa S, Suriano G, Grellier M, Huntsman DG, Carneiro F, Granja PL, Seruca R (2010) De novo expression of CD44 variants in sporadic and hereditary gastric cancer. Lab Invest, 90: 1604-14. https://doi.org/10.1038/labinvest.2010.155
  • Dall'Olio F, Malagolini N, Trinchera M, Chiricolo M (2012) Mechanisms of cancer-associated glycosylation changes. Front Biosci (Landmark Ed), 17: 670-99. https://doi.org/10.2741/3951
  • Dalziel M, Whitehouse C, McFarlane I, Brockhausen I, Gschmeissner S, Schwientek T, Clausen H, Burchell JM, Taylor-Papadimitriou J (2001) The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. J Biol Chem, 276: 11007-15. https://doi.org/10.1074/jbc.M006523200
  • Dennis J, Waller C, Timpl R, Schirrmacher V (1982) Surface sialic acid reduces attachment of metastatic tumour cells to collagen type IV and fibronectin. Nature, 300: 274-6. https://doi.org/10.1038/300274a0
  • Dennis JW, Laferte S, Waghorne C, Breitman ML, Kerbel RS (1987) Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science, 236: 582-5. https://doi.org/10.1126/science.2953071
  • Dennis JW, Nabi IR, Demetriou M (2009) Metabolism, cell surface organization, and disease. Cell, 139: 1229-41. https://doi.org/10.1016/j.cell.2009.12.008
  • Di Lella S, Sundblad V, Cerliani JP, Guardia CM, Estrin DA, Vasta GR, Rabinovich GA (2011) When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again. Biochemistry, 50: 7842-7857. https://doi.org/10.1021/bi201121m
  • Falconer RA, Errington RJ, Shnyder SD, Smith PJ, Patterson LH (2012) Polysialyltransferase: a new target in metastatic cancer. Curr Cancer Drug Targets, 12: 925-39. https://doi.org/10.2174/156800912803251225
  • Feizi T (1985) Carbohydrate antigens in human cancer. Cancer Surv, 4: 245-69.
  • Gill DJ, Chia J, Senewiratne J, Bard F (2010) Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. Journal of Cell Biology, 189: 843-858. https://doi.org/10.1083/jcb.201003055
  • Gill DJ, Tham KM, Chia J, Wang SC, Steentoft C, Clausen H, Bard-Chapeau EA, Bard FA (2013) Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness. Proceedings of the National Academy of Sciences of the United States of America, 110: E3152-E3161. https://doi.org/10.1073/pnas.1305269110
  • Gu J, Sato Y, Kariya Y, Isaji T, Taniguchi N, Fukuda T (2009) A Mutual Regulation between Cell-Cell Adhesion and N-Glycosylation: Implication of the Bisecting GlcNAc for Biological Functions. Journal of Proteome Research, 8: 431-435. https://doi.org/10.1021/pr800674g
  • Guo H, Nagy T, Pierce M (2014) Post-translational glycoprotein modifications regulate colon cancer stem cells and colon adenoma progression in Apc(min/+) mice through altered Wnt receptor signaling. J Biol Chem, 289: 31534-49. https://doi.org/10.1074/jbc.M114.602680
  • Hakomori S, Kannagi R (1983) Glycosphingolipids as Tumor-Associated and Differentiation Markers. Jnci-Journal of the National Cancer Institute, 71: 231-251.
  • Hakomori S, Murakami WT (1968) Glycolipids of Hamster Fibroblasts and Derived Malignant-Transformed Cell Lines. Proceedings of the National Academy of Sciences of the United States of America, 59: 254-&. https://doi.org/DOI 10.1073/pnas.59.1.254
  • Helenius A, Aebi M (2001) Intracellular functions of N-linked glycans. Science, 291: 2364-2369. https://doi.org/DOI 10.1126/science.291.5512.2364
  • Hiraiwa N, Yabuta T, Yoritomi K, Hiraiwa M, Tanaka Y, Suzuki T, Yoshida M, Kannagi R (2003) Transactivation of the fucosyltransferase VII gene by human T-cell leukemia virus type 1 Tax through a variant cAMP-responsive element. Blood, 101: 3615-3621. https://doi.org/10.1182/blood-2002-07-2301
  • Jian YL, Xu ZY, Xu CY, Zhang L, Sun XX, Yang DY, Wang SJ (2020) The Roles of Glycans in Bladder Cancer. Frontiers in Oncology, 10. https://doi.org/ARTN 957 10.3389/fonc.2020.00957
  • Ju T, Cummings RD (2002) A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase. Proc Natl Acad Sci U S A, 99: 16613-8. https://doi.org/10.1073/pnas.262438199
  • Julien S, Bobowski M, Steenackers A, Le Bourhis X, Delannoy P (2013) How Do Gangliosides Regulate RTKs Signaling? Cells, 2: 751-67. https://doi.org/10.3390/cells2040751
  • Julien S, Picco G, Sewell R, Vercoutter-Edouart AS, Tarp M, Miles D, Clausen H, Taylor-Papadimitriou J, Burchell JM (2009) Sialyl-Tn vaccine induces antibody-mediated tumour protection in a relevant murine model. Br J Cancer, 100: 1746-54. https://doi.org/10.1038/sj.bjc.6605083
  • Kannagi R, Yin J, Miyazaki K, Izawa M (2008) Current relevance of incomplete synthesis and neo-synthesis for cancer-associated alteration of carbohydrate determinants--Hakomori's concepts revisited. Biochim Biophys Acta, 1780: 525-31. https://doi.org/10.1016/j.bbagen.2007.10.007
  • Katoh S, Zheng Z, Oritani K, Shimozato T, Kincade PW (1995) Glycosylation of CD44 negatively regulates its recognition of hyaluronan. J Exp Med, 182: 419-29. https://doi.org/10.1084/jem.182.2.419
  • Kim SH, Turnbull J, Guimond S (2011) Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. J Endocrinol, 209: 139-51. https://doi.org/10.1530/JOE-10-0377
  • Kitada T, Miyoshi E, Noda K, Higashiyama S, Ihara H, Matsuura N, Hayashi N, Kawata S, Matsuzawa Y, Taniguchi N (2001) The addition of bisecting N-acetylglucosamine residues to E-cadherin down-regulates the tyrosine phosphorylation of beta-catenin. J Biol Chem, 276: 475-80. https://doi.org/10.1074/jbc.M006689200
  • Kudelka MR, Ju T, Heimburg-Molinaro J, Cummings RD (2015) Simple sugars to complex disease--mucin-type O-glycans in cancer. Adv Cancer Res, 126: 53-135. https://doi.org/10.1016/bs.acr.2014.11.002
  • Kumamoto K, Goto Y, Sekikawa K, Takenoshita S, Ishida N, Kawakita M, Kannagi R (2001) Increased expression of UDP-galactose transporter messenger RNA in human colon cancer tissues and its implication in synthesis of Thomsen-Friedenreich antigen and sialyl Lewis A/X determinants. Cancer Res, 61: 4620-7.
  • Ladenson RP, Schwartz SO, Ivy AC (1949) Incidence of the blood groups and the secretor factor in patients with pernicious anemia and stomach carcinoma. Am J Med Sci, 217: 194-7. https://doi.org/10.1097/00000441-194902000-00011
  • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, Demetriou M, Dennis JW (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell, 129: 123-34. https://doi.org/10.1016/j.cell.2007.01.049
  • Lin S, Kemmner W, Grigull S, Schlag PM (2002) Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells. Exp Cell Res, 276: 101-10. https://doi.org/10.1006/excr.2002.5521
  • Lise M, Belluco C, Perera SP, Patel R, Thomas P, Ganguly A (2000) Clinical correlations of alpha2,6-sialyltransferase expression in colorectal cancer patients. Hybridoma, 19: 281-6. https://doi.org/10.1089/027245700429828
  • Liu YC, Yen HY, Chen CY, Chen CH, Cheng PF, Juan YH, Chen CH, Khoo KH, Yu CJ, Yang PC, Hsu TL, Wong CH (2011) Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells. Proc Natl Acad Sci U S A, 108: 11332-7. https://doi.org/10.1073/pnas.1107385108
  • Magalhaes A, Marcos-Pinto R, Nairn AV, Dela Rosa M, Ferreira RM, Junqueira-Neto S, Freitas D, Gomes J, Oliveira P, Santos MR, Marcos NT, Xiaogang W, Figueiredo C, Oliveira C, Dinis-Ribeiro M, Carneiro F, Moremen KW, David L, Reis CA (2015) Helicobacter pylori chronic infection and mucosal inflammation switches the human gastric glycosylation pathways. Biochim Biophys Acta, 1852: 1928-39. https://doi.org/10.1016/j.bbadis.2015.07.001
  • Marcos NT, Bennett EP, Gomes J, Magalhaes A, Gomes C, David L, Dar I, Jeanneau C, DeFrees S, Krustrup D, Vogel LK, Kure EH, Burchell J, Taylor-Papadimitriou J, Clausen H, Mandel U, Reis CA (2011) ST6GalNAc-I controls expression of sialyl-Tn antigen in gastrointestinal tissues. Front Biosci (Elite Ed), 3: 1443-55. https://doi.org/10.2741/e345
  • Marcos NT, Pinho S, Grandela C, Cruz A, Samyn-Petit B, Harduin-Lepers A, Almeida R, Silva F, Morais V, Costa J, Kihlberg J, Clausen H, Reis CA (2004) Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen. Cancer Res, 64: 7050-7. https://doi.org/10.1158/0008-5472.CAN-04-1921
  • Marshall S, Bacote V, Traxinger RR (1991) Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J Biol Chem, 266: 4706-12.
  • Mechref Y, Hu Y, Garcia A, Hussein A (2012) Identifying cancer biomarkers by mass spectrometry-based glycomics. Electrophoresis, 33: 1755-67. https://doi.org/10.1002/elps.201100715
  • Paredes J, Figueiredo J, Albergaria A, Oliveira P, Carvalho J, Ribeiro AS, Caldeira J, Costa AM, Simoes-Correia J, Oliveira MJ, Pinheiro H, Pinho SS, Mateus R, Reis CA, Leite M, Fernandes MS, Schmitt F, Carneiro F, Figueiredo C, Oliveira C, Seruca R (2012) Epithelial E- and P-cadherins: role and clinical significance in cancer. Biochim Biophys Acta, 1826: 297-311. https://doi.org/10.1016/j.bbcan.2012.05.002
  • Paszek MJ, DuFort CC, Rossier O, Bainer R, Mouw JK, Godula K, Hudak JE, Lakins JN, Wijekoon AC, Cassereau L, Rubashkin MG, Magbanua MJ, Thorn KS, Davidson MW, Rugo HS, Park JW, Hammer DA, Giannone G, Bertozzi CR, Weaver VM (2014) The cancer glycocalyx mechanically primes integrin-mediated growth and survival. Nature, 511: 319-25. https://doi.org/10.1038/nature13535
  • Peng W, Goli M, Mirzaei P, Mechref Y (2019) Revealing the Biological Attributes of N-Glycan Isomers in Breast Cancer Brain Metastasis Using Porous Graphitic Carbon (PGC) Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS). J Proteome Res, 18: 3731-3740. https://doi.org/10.1021/acs.jproteome.9b00429
  • Pinho S, Marcos NT, Ferreira B, Carvalho AS, Oliveira MJ, Santos-Silva F, Harduin-Lepers A, Reis CA (2007) Biological significance of cancer-associated sialyl-Tn antigen: modulation of malignant phenotype in gastric carcinoma cells. Cancer Lett, 249: 157-70. https://doi.org/10.1016/j.canlet.2006.08.010
  • Pinho SS, Oliveira P, Cabral J, Carvalho S, Huntsman D, Gartner F, Seruca R, Reis CA, Oliveira C (2012) Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions. PLoS One, 7: e33191. https://doi.org/10.1371/journal.pone.0033191
  • Potapenko IO, Haakensen VD, Luders T, Helland A, Bukholm I, Sorlie T, Kristensen VN, Lingjaerde OC, Borresen-Dale AL (2010) Glycan gene expression signatures in normal and malignant breast tissue; possible role in diagnosis and progression. Mol Oncol, 4: 98-118. https://doi.org/10.1016/j.molonc.2009.12.001
  • Rabinovich GA, Toscano MA (2009) Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat Rev Immunol, 9: 338-52. https://doi.org/10.1038/nri2536
  • Roth J, Wang Y, Eckhardt AE, Hill RL (1994) Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc Natl Acad Sci U S A, 91: 8935-9. https://doi.org/10.1073/pnas.91.19.8935
  • Saeland E, van Vliet SJ, Backstrom M, van den Berg VC, Geijtenbeek TB, Meijer GA, van Kooyk Y (2007) The C-type lectin MGL expressed by dendritic cells detects glycan changes on MUC1 in colon carcinoma. Cancer Immunol Immunother, 56: 1225-36. https://doi.org/10.1007/s00262-006-0274-z
  • Saoncella S, Echtermeyer F, Denhez F, Nowlen JK, Mosher DF, Robinson SD, Hynes RO, Goetinck PF (1999) Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers. Proc Natl Acad Sci U S A, 96: 2805-10. https://doi.org/10.1073/pnas.96.6.2805
  • Sarrazin S, Lamanna WC, Esko JD (2011) Heparan sulfate proteoglycans. Cold Spring Harb Perspect Biol, 3. https://doi.org/10.1101/cshperspect.a004952
  • Sato Y, Nakata K, Kato Y, Shima M, Ishii N, Koji T, Taketa K, Endo Y, Nagataki S (1993) Early Recognition of Hepatocellular-Carcinoma Based on Altered Profiles of Alpha-Fetoprotein. New England Journal of Medicine, 328: 1802-1806. https://doi.org/Doi 10.1056/Nejm199306243282502
  • Seberger PJ, Chaney WG (1999) Control of metastasis by Asn-linked, beta 1-6 branched oligosaccharides in mouse mammary cancer cells. Glycobiology, 9: 235-241. https://doi.org/DOI 10.1093/glycob/9.3.235
  • Seidenfaden R, Krauter A, Schertzinger F, Gerardy-Schahn R, Hildebrandt H (2003) Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions. Molecular and Cellular Biology, 23: 5908-5918. https://doi.org/10.1128/Mcb.23.16.5908-5918.2003
  • Sewell R, Backstrom M, Dalziel M, Gschmeissner S, Karlsson H, Noll T, Gatgens J, Clausen H, Hansson GC, Burchell J, Taylor-Papadimitriou J (2006) The ST6GalNAc-I sialyltransferase localizes throughout the golgi and is responsible for the synthesis of the tumor-associated Sialyl-Tn O-glycan in human breast cancer. Journal of Biological Chemistry, 281: 3586-3594. https://doi.org/10.1074/jbc.M511826200
  • Slawson C, Copeland RJ, Hart GW (2010) O-GIcNAc signaling: a metabolic link between diabetes and cancer? Trends in Biochemical Sciences, 35: 547-555. https://doi.org/10.1016/j.tibs.2010.04.005
  • Takahashi M, Kuroki Y, Ohtsubo K, Taniguchi N (2009) Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydrate Research, 344: 1387-1390. https://doi.org/10.1016/j.carres.2009.04.031
  • Thomas D, Rathinavel AK, Radhakrishnan P (2021) Altered glycosylation in cancer: A promising target for biomarkers and therapeutics. Biochim Biophys Acta Rev Cancer, 1875: 188464. https://doi.org/10.1016/j.bbcan.2020.188464
  • Todeschini AR, Dos Santos JN, Handa K, Hakomori S (2007) Ganglioside GM2-tetraspanin CD82 complex inhibits met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse. Journal of Biological Chemistry, 282: 8123-8133. https://doi.org/10.1074/jbc.M611407200
  • Tsai CH, Tzeng SF, Chao TK, Tsai CY, Yang YC, Lee MT, Hwang JJ, Chou YC, Tsai MH, Cha TL, Hsiao PW (2016) Metastatic Progression of Prostate Cancer Is Mediated by Autonomous Binding of Galectin-4-O-Glycan to Cancer Cells. Cancer Research, 76: 5756-5767. https://doi.org/10.1158/0008-5472.Can-16-0641
  • Tsuboi S (2019) Two Opposite Roles of Core 2 O-Glycans in Evasion Mechanisms of Tumor Immunity. Trends in Glycoscience and Glycotechnology, 31: E113-E119. https://doi.org/10.4052/tigg.1832.1E
  • Vlodavsky I, Friedmann Y (2001) Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. Journal of Clinical Investigation, 108: 341-347. https://doi.org/Doi 10.1172/Jci13662
  • Wolff EA, Greenfield B, Taub DD, Murphy WJ, Bennett KL, Aruffo A (1999) Generation of artificial proteoglycans containing glycosaminoglycan-modified CD44 - Demonstration of the interaction between RANTES and chondroitin sulfate. Journal of Biological Chemistry, 274: 2518-2524. https://doi.org/DOI 10.1074/jbc.274.4.2518
  • Yuecheng Zhang, Kushtrim Llapashtica, Sudhirkumar Shinde, Börje Sellergren, Zahra El-Schich, Wingren AG (2019) Determination of cytokine regulated glycan expression by using molecularly imprinted polymers targeting sialic acid. Journal of Cancer Metastasis and Treatment, 5:56. https://doi.org/10.20517/2394-4722.2018.112
  • Zachara NE, Hart GW (2006) Cell signaling, the essential role of O-GlcNAc! Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids, 1761: 599-617. https://doi.org/10.1016/j.bbalip.2006.04.007

The Importance of Glycans in Cancer Metabolism and Metastasis

Year 2021, Volume: 6 Issue: 2, 112 - 119, 30.08.2021

Nebiye Pelin Türker , Elvan Bakar

https://doi.org/10.51754/cusbed.867416
Cited By: 1

Abstract

The role of glycobiology in understanding cancer mechanisms, providing a set of targets for diagnostic applications and therapeutic strategies increases the importance of this field of science in cancer research day by day. It is predicted that glycosylation may function as an important regulatory mechanism controlling a variety of physiopathological processes. Glycosylation changes in cells and their links with disease show that the glycome contains significant biological information. Changes in the branching and length of the glycan chains, the variety of carbohydrates in their structure cause the biological functions of these molecules to change. However, characterization of the biological functions of glycan binding proteins makes important contributions to cancer research. Different types of glycoconjugates lead to cancer progression by interfering with key cancer cell processes as well as the tumor microenvironment.

Keywords

Cancer Metastasis Glycan Glycosylation

References

  • Arnold JN, Saldova R, Hamid UM, Rudd PM (2008) Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics, 8: 3284-93. https://doi.org/10.1002/pmic.200800163
  • Aryal RP, Ju T, Cummings RD (2010) The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase. J Biol Chem, 285: 2456-62. https://doi.org/10.1074/jbc.M109.065169
  • Baldus SE, Zirbes TK, Monig SP, Engel S, Monaca E, Rafiqpoor K, Hanisch FG, Hanski C, Thiele J, Pichlmaier H, Dienes HP (1998) Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: Sialosyl-Lewis(a), Sialosyl-Lewis(x) and sialosyl-Tn. Tumour Biol, 19: 445-53. https://doi.org/10.1159/000030036
  • Bharadwaj AG, Kovar JL, Loughman E, Elowsky C, Oakley GG, Simpson MA (2009) Spontaneous Metastasis of Prostate Cancer Is Promoted by Excess Hyaluronan Synthesis and Processing. American Journal of Pathology, 174: 1027-1036. https://doi.org/10.2353/ajpath.2009.080501
  • Borsig L, Wong R, Feramisco J, Nadeau DR, Varki NM, Varki A (2001) Heparin and cancer revisited: Mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis (vol 98, pg 3352, 2001).
  • Proceedings of the National Academy of Sciences of the United States of America, 98: 5369-5369.
  • Carvalho AS, Harduin-Lepers A, Magalhaes A, Machado E, Mendes N, Costa LT, Matthiesen R, Almeida R, Costa J, Reis CA (2010) Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells. Int J Biochem Cell Biol, 42: 80-9. https://doi.org/10.1016/j.biocel.2009.09.010
  • Croci DO, Cerliani JP, Dalotto-Moreno T, Mendez-Huergo SP, Mascanfroni ID, Dergan-Dylon S, Toscano MA, Caramelo JJ, Garcia-Vallejo JJ, Ouyang J, Mesri EA, Junttila MR, Bais C, Shipp MA, Salatino M, Rabinovich GA (2014) Glycosylation-dependent lectin-receptor interactions preserve angiogenesis in anti-VEGF refractory tumors. Cell, 156: 744-58. https://doi.org/10.1016/j.cell.2014.01.043
  • da Cunha CB, Oliveira C, Wen X, Gomes B, Sousa S, Suriano G, Grellier M, Huntsman DG, Carneiro F, Granja PL, Seruca R (2010) De novo expression of CD44 variants in sporadic and hereditary gastric cancer. Lab Invest, 90: 1604-14. https://doi.org/10.1038/labinvest.2010.155
  • Dall'Olio F, Malagolini N, Trinchera M, Chiricolo M (2012) Mechanisms of cancer-associated glycosylation changes. Front Biosci (Landmark Ed), 17: 670-99. https://doi.org/10.2741/3951
  • Dalziel M, Whitehouse C, McFarlane I, Brockhausen I, Gschmeissner S, Schwientek T, Clausen H, Burchell JM, Taylor-Papadimitriou J (2001) The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. J Biol Chem, 276: 11007-15. https://doi.org/10.1074/jbc.M006523200
  • Dennis J, Waller C, Timpl R, Schirrmacher V (1982) Surface sialic acid reduces attachment of metastatic tumour cells to collagen type IV and fibronectin. Nature, 300: 274-6. https://doi.org/10.1038/300274a0
  • Dennis JW, Laferte S, Waghorne C, Breitman ML, Kerbel RS (1987) Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science, 236: 582-5. https://doi.org/10.1126/science.2953071
  • Dennis JW, Nabi IR, Demetriou M (2009) Metabolism, cell surface organization, and disease. Cell, 139: 1229-41. https://doi.org/10.1016/j.cell.2009.12.008
  • Di Lella S, Sundblad V, Cerliani JP, Guardia CM, Estrin DA, Vasta GR, Rabinovich GA (2011) When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again. Biochemistry, 50: 7842-7857. https://doi.org/10.1021/bi201121m
  • Falconer RA, Errington RJ, Shnyder SD, Smith PJ, Patterson LH (2012) Polysialyltransferase: a new target in metastatic cancer. Curr Cancer Drug Targets, 12: 925-39. https://doi.org/10.2174/156800912803251225
  • Feizi T (1985) Carbohydrate antigens in human cancer. Cancer Surv, 4: 245-69.
  • Gill DJ, Chia J, Senewiratne J, Bard F (2010) Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. Journal of Cell Biology, 189: 843-858. https://doi.org/10.1083/jcb.201003055
  • Gill DJ, Tham KM, Chia J, Wang SC, Steentoft C, Clausen H, Bard-Chapeau EA, Bard FA (2013) Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness. Proceedings of the National Academy of Sciences of the United States of America, 110: E3152-E3161. https://doi.org/10.1073/pnas.1305269110
  • Gu J, Sato Y, Kariya Y, Isaji T, Taniguchi N, Fukuda T (2009) A Mutual Regulation between Cell-Cell Adhesion and N-Glycosylation: Implication of the Bisecting GlcNAc for Biological Functions. Journal of Proteome Research, 8: 431-435. https://doi.org/10.1021/pr800674g
  • Guo H, Nagy T, Pierce M (2014) Post-translational glycoprotein modifications regulate colon cancer stem cells and colon adenoma progression in Apc(min/+) mice through altered Wnt receptor signaling. J Biol Chem, 289: 31534-49. https://doi.org/10.1074/jbc.M114.602680
  • Hakomori S, Kannagi R (1983) Glycosphingolipids as Tumor-Associated and Differentiation Markers. Jnci-Journal of the National Cancer Institute, 71: 231-251.
  • Hakomori S, Murakami WT (1968) Glycolipids of Hamster Fibroblasts and Derived Malignant-Transformed Cell Lines. Proceedings of the National Academy of Sciences of the United States of America, 59: 254-&. https://doi.org/DOI 10.1073/pnas.59.1.254
  • Helenius A, Aebi M (2001) Intracellular functions of N-linked glycans. Science, 291: 2364-2369. https://doi.org/DOI 10.1126/science.291.5512.2364
  • Hiraiwa N, Yabuta T, Yoritomi K, Hiraiwa M, Tanaka Y, Suzuki T, Yoshida M, Kannagi R (2003) Transactivation of the fucosyltransferase VII gene by human T-cell leukemia virus type 1 Tax through a variant cAMP-responsive element. Blood, 101: 3615-3621. https://doi.org/10.1182/blood-2002-07-2301
  • Jian YL, Xu ZY, Xu CY, Zhang L, Sun XX, Yang DY, Wang SJ (2020) The Roles of Glycans in Bladder Cancer. Frontiers in Oncology, 10. https://doi.org/ARTN 957 10.3389/fonc.2020.00957
  • Ju T, Cummings RD (2002) A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase. Proc Natl Acad Sci U S A, 99: 16613-8. https://doi.org/10.1073/pnas.262438199
  • Julien S, Bobowski M, Steenackers A, Le Bourhis X, Delannoy P (2013) How Do Gangliosides Regulate RTKs Signaling? Cells, 2: 751-67. https://doi.org/10.3390/cells2040751
  • Julien S, Picco G, Sewell R, Vercoutter-Edouart AS, Tarp M, Miles D, Clausen H, Taylor-Papadimitriou J, Burchell JM (2009) Sialyl-Tn vaccine induces antibody-mediated tumour protection in a relevant murine model. Br J Cancer, 100: 1746-54. https://doi.org/10.1038/sj.bjc.6605083
  • Kannagi R, Yin J, Miyazaki K, Izawa M (2008) Current relevance of incomplete synthesis and neo-synthesis for cancer-associated alteration of carbohydrate determinants--Hakomori's concepts revisited. Biochim Biophys Acta, 1780: 525-31. https://doi.org/10.1016/j.bbagen.2007.10.007
  • Katoh S, Zheng Z, Oritani K, Shimozato T, Kincade PW (1995) Glycosylation of CD44 negatively regulates its recognition of hyaluronan. J Exp Med, 182: 419-29. https://doi.org/10.1084/jem.182.2.419
  • Kim SH, Turnbull J, Guimond S (2011) Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. J Endocrinol, 209: 139-51. https://doi.org/10.1530/JOE-10-0377
  • Kitada T, Miyoshi E, Noda K, Higashiyama S, Ihara H, Matsuura N, Hayashi N, Kawata S, Matsuzawa Y, Taniguchi N (2001) The addition of bisecting N-acetylglucosamine residues to E-cadherin down-regulates the tyrosine phosphorylation of beta-catenin. J Biol Chem, 276: 475-80. https://doi.org/10.1074/jbc.M006689200
  • Kudelka MR, Ju T, Heimburg-Molinaro J, Cummings RD (2015) Simple sugars to complex disease--mucin-type O-glycans in cancer. Adv Cancer Res, 126: 53-135. https://doi.org/10.1016/bs.acr.2014.11.002
  • Kumamoto K, Goto Y, Sekikawa K, Takenoshita S, Ishida N, Kawakita M, Kannagi R (2001) Increased expression of UDP-galactose transporter messenger RNA in human colon cancer tissues and its implication in synthesis of Thomsen-Friedenreich antigen and sialyl Lewis A/X determinants. Cancer Res, 61: 4620-7.
  • Ladenson RP, Schwartz SO, Ivy AC (1949) Incidence of the blood groups and the secretor factor in patients with pernicious anemia and stomach carcinoma. Am J Med Sci, 217: 194-7. https://doi.org/10.1097/00000441-194902000-00011
  • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, Demetriou M, Dennis JW (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell, 129: 123-34. https://doi.org/10.1016/j.cell.2007.01.049
  • Lin S, Kemmner W, Grigull S, Schlag PM (2002) Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells. Exp Cell Res, 276: 101-10. https://doi.org/10.1006/excr.2002.5521
  • Lise M, Belluco C, Perera SP, Patel R, Thomas P, Ganguly A (2000) Clinical correlations of alpha2,6-sialyltransferase expression in colorectal cancer patients. Hybridoma, 19: 281-6. https://doi.org/10.1089/027245700429828
  • Liu YC, Yen HY, Chen CY, Chen CH, Cheng PF, Juan YH, Chen CH, Khoo KH, Yu CJ, Yang PC, Hsu TL, Wong CH (2011) Sialylation and fucosylation of epidermal growth factor receptor suppress its dimerization and activation in lung cancer cells. Proc Natl Acad Sci U S A, 108: 11332-7. https://doi.org/10.1073/pnas.1107385108
  • Magalhaes A, Marcos-Pinto R, Nairn AV, Dela Rosa M, Ferreira RM, Junqueira-Neto S, Freitas D, Gomes J, Oliveira P, Santos MR, Marcos NT, Xiaogang W, Figueiredo C, Oliveira C, Dinis-Ribeiro M, Carneiro F, Moremen KW, David L, Reis CA (2015) Helicobacter pylori chronic infection and mucosal inflammation switches the human gastric glycosylation pathways. Biochim Biophys Acta, 1852: 1928-39. https://doi.org/10.1016/j.bbadis.2015.07.001
  • Marcos NT, Bennett EP, Gomes J, Magalhaes A, Gomes C, David L, Dar I, Jeanneau C, DeFrees S, Krustrup D, Vogel LK, Kure EH, Burchell J, Taylor-Papadimitriou J, Clausen H, Mandel U, Reis CA (2011) ST6GalNAc-I controls expression of sialyl-Tn antigen in gastrointestinal tissues. Front Biosci (Elite Ed), 3: 1443-55. https://doi.org/10.2741/e345
  • Marcos NT, Pinho S, Grandela C, Cruz A, Samyn-Petit B, Harduin-Lepers A, Almeida R, Silva F, Morais V, Costa J, Kihlberg J, Clausen H, Reis CA (2004) Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the cancer-associated sialyl-Tn antigen. Cancer Res, 64: 7050-7. https://doi.org/10.1158/0008-5472.CAN-04-1921
  • Marshall S, Bacote V, Traxinger RR (1991) Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J Biol Chem, 266: 4706-12.
  • Mechref Y, Hu Y, Garcia A, Hussein A (2012) Identifying cancer biomarkers by mass spectrometry-based glycomics. Electrophoresis, 33: 1755-67. https://doi.org/10.1002/elps.201100715
  • Paredes J, Figueiredo J, Albergaria A, Oliveira P, Carvalho J, Ribeiro AS, Caldeira J, Costa AM, Simoes-Correia J, Oliveira MJ, Pinheiro H, Pinho SS, Mateus R, Reis CA, Leite M, Fernandes MS, Schmitt F, Carneiro F, Figueiredo C, Oliveira C, Seruca R (2012) Epithelial E- and P-cadherins: role and clinical significance in cancer. Biochim Biophys Acta, 1826: 297-311. https://doi.org/10.1016/j.bbcan.2012.05.002
  • Paszek MJ, DuFort CC, Rossier O, Bainer R, Mouw JK, Godula K, Hudak JE, Lakins JN, Wijekoon AC, Cassereau L, Rubashkin MG, Magbanua MJ, Thorn KS, Davidson MW, Rugo HS, Park JW, Hammer DA, Giannone G, Bertozzi CR, Weaver VM (2014) The cancer glycocalyx mechanically primes integrin-mediated growth and survival. Nature, 511: 319-25. https://doi.org/10.1038/nature13535
  • Peng W, Goli M, Mirzaei P, Mechref Y (2019) Revealing the Biological Attributes of N-Glycan Isomers in Breast Cancer Brain Metastasis Using Porous Graphitic Carbon (PGC) Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS). J Proteome Res, 18: 3731-3740. https://doi.org/10.1021/acs.jproteome.9b00429
  • Pinho S, Marcos NT, Ferreira B, Carvalho AS, Oliveira MJ, Santos-Silva F, Harduin-Lepers A, Reis CA (2007) Biological significance of cancer-associated sialyl-Tn antigen: modulation of malignant phenotype in gastric carcinoma cells. Cancer Lett, 249: 157-70. https://doi.org/10.1016/j.canlet.2006.08.010
  • Pinho SS, Oliveira P, Cabral J, Carvalho S, Huntsman D, Gartner F, Seruca R, Reis CA, Oliveira C (2012) Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions. PLoS One, 7: e33191. https://doi.org/10.1371/journal.pone.0033191
  • Potapenko IO, Haakensen VD, Luders T, Helland A, Bukholm I, Sorlie T, Kristensen VN, Lingjaerde OC, Borresen-Dale AL (2010) Glycan gene expression signatures in normal and malignant breast tissue; possible role in diagnosis and progression. Mol Oncol, 4: 98-118. https://doi.org/10.1016/j.molonc.2009.12.001
  • Rabinovich GA, Toscano MA (2009) Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat Rev Immunol, 9: 338-52. https://doi.org/10.1038/nri2536
  • Roth J, Wang Y, Eckhardt AE, Hill RL (1994) Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc Natl Acad Sci U S A, 91: 8935-9. https://doi.org/10.1073/pnas.91.19.8935
  • Saeland E, van Vliet SJ, Backstrom M, van den Berg VC, Geijtenbeek TB, Meijer GA, van Kooyk Y (2007) The C-type lectin MGL expressed by dendritic cells detects glycan changes on MUC1 in colon carcinoma. Cancer Immunol Immunother, 56: 1225-36. https://doi.org/10.1007/s00262-006-0274-z
  • Saoncella S, Echtermeyer F, Denhez F, Nowlen JK, Mosher DF, Robinson SD, Hynes RO, Goetinck PF (1999) Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers. Proc Natl Acad Sci U S A, 96: 2805-10. https://doi.org/10.1073/pnas.96.6.2805
  • Sarrazin S, Lamanna WC, Esko JD (2011) Heparan sulfate proteoglycans. Cold Spring Harb Perspect Biol, 3. https://doi.org/10.1101/cshperspect.a004952
  • Sato Y, Nakata K, Kato Y, Shima M, Ishii N, Koji T, Taketa K, Endo Y, Nagataki S (1993) Early Recognition of Hepatocellular-Carcinoma Based on Altered Profiles of Alpha-Fetoprotein. New England Journal of Medicine, 328: 1802-1806. https://doi.org/Doi 10.1056/Nejm199306243282502
  • Seberger PJ, Chaney WG (1999) Control of metastasis by Asn-linked, beta 1-6 branched oligosaccharides in mouse mammary cancer cells. Glycobiology, 9: 235-241. https://doi.org/DOI 10.1093/glycob/9.3.235
  • Seidenfaden R, Krauter A, Schertzinger F, Gerardy-Schahn R, Hildebrandt H (2003) Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions. Molecular and Cellular Biology, 23: 5908-5918. https://doi.org/10.1128/Mcb.23.16.5908-5918.2003
  • Sewell R, Backstrom M, Dalziel M, Gschmeissner S, Karlsson H, Noll T, Gatgens J, Clausen H, Hansson GC, Burchell J, Taylor-Papadimitriou J (2006) The ST6GalNAc-I sialyltransferase localizes throughout the golgi and is responsible for the synthesis of the tumor-associated Sialyl-Tn O-glycan in human breast cancer. Journal of Biological Chemistry, 281: 3586-3594. https://doi.org/10.1074/jbc.M511826200
  • Slawson C, Copeland RJ, Hart GW (2010) O-GIcNAc signaling: a metabolic link between diabetes and cancer? Trends in Biochemical Sciences, 35: 547-555. https://doi.org/10.1016/j.tibs.2010.04.005
  • Takahashi M, Kuroki Y, Ohtsubo K, Taniguchi N (2009) Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydrate Research, 344: 1387-1390. https://doi.org/10.1016/j.carres.2009.04.031
  • Thomas D, Rathinavel AK, Radhakrishnan P (2021) Altered glycosylation in cancer: A promising target for biomarkers and therapeutics. Biochim Biophys Acta Rev Cancer, 1875: 188464. https://doi.org/10.1016/j.bbcan.2020.188464
  • Todeschini AR, Dos Santos JN, Handa K, Hakomori S (2007) Ganglioside GM2-tetraspanin CD82 complex inhibits met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse. Journal of Biological Chemistry, 282: 8123-8133. https://doi.org/10.1074/jbc.M611407200
  • Tsai CH, Tzeng SF, Chao TK, Tsai CY, Yang YC, Lee MT, Hwang JJ, Chou YC, Tsai MH, Cha TL, Hsiao PW (2016) Metastatic Progression of Prostate Cancer Is Mediated by Autonomous Binding of Galectin-4-O-Glycan to Cancer Cells. Cancer Research, 76: 5756-5767. https://doi.org/10.1158/0008-5472.Can-16-0641
  • Tsuboi S (2019) Two Opposite Roles of Core 2 O-Glycans in Evasion Mechanisms of Tumor Immunity. Trends in Glycoscience and Glycotechnology, 31: E113-E119. https://doi.org/10.4052/tigg.1832.1E
  • Vlodavsky I, Friedmann Y (2001) Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. Journal of Clinical Investigation, 108: 341-347. https://doi.org/Doi 10.1172/Jci13662
  • Wolff EA, Greenfield B, Taub DD, Murphy WJ, Bennett KL, Aruffo A (1999) Generation of artificial proteoglycans containing glycosaminoglycan-modified CD44 - Demonstration of the interaction between RANTES and chondroitin sulfate. Journal of Biological Chemistry, 274: 2518-2524. https://doi.org/DOI 10.1074/jbc.274.4.2518
  • Yuecheng Zhang, Kushtrim Llapashtica, Sudhirkumar Shinde, Börje Sellergren, Zahra El-Schich, Wingren AG (2019) Determination of cytokine regulated glycan expression by using molecularly imprinted polymers targeting sialic acid. Journal of Cancer Metastasis and Treatment, 5:56. https://doi.org/10.20517/2394-4722.2018.112
  • Zachara NE, Hart GW (2006) Cell signaling, the essential role of O-GlcNAc! Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids, 1761: 599-617. https://doi.org/10.1016/j.bbalip.2006.04.007
There are 70 citations in total.

Details

Primary Language Turkish
Subjects Health Care Administration
Journal Section Review
Authors

Nebiye Pelin Türker 0000-0001-6060-3557

Elvan Bakar 0000-0001-5703-3469

Publication Date August 30, 2021
Published in Issue Year 2021Volume: 6 Issue: 2

Cite

APA Türker, N. P., & Bakar, E. (2021). Kanser Metabolizmasında ve Metastazında Glikanların Önemi. Instıtute of Health Sciences Journal, 6(2), 112-119. https://doi.org/10.51754/cusbed.867416

Cited By

https://doi.org/
 Download Cover Image

   ici2.png    logo.png        asos-index.png       crossref-logo-landscape-200.png     logo.png       search-result-logo-horizontal-TEST.jpg 

     

logo.png    scilit.jpg     goole_scholar.jpg       logo.png    logo.png


f9ab67f.png                    download