Academic literature on the topic 'Β-O-linked glycosylation'
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Journal articles on the topic "Β-O-linked glycosylation"
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Claude, Patrick, Christian Lehmann, and Thomas Ziegler. "Dependency of the regio- and stereoselectivity of intramolecular, ring-closing glycosylations upon the ring size." Beilstein Journal of Organic Chemistry 7 (December 1, 2011): 1609–19. http://dx.doi.org/10.3762/bjoc.7.189.
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Phenyl 3,4,6-tri-O-benzyl-2-O-(3-carboxypropionyl)-1-thio-β-D-galactopyranoside (1) was condensed via its pentafluorophenyl ester 2 with 5-aminopentyl (4a), 4-aminobutyl (4b), 3-aminopropyl (4c) and 2-aminoethyl 4,6-O-benzylidene-β-D-glucopyranoside (4d), prepared from the corresponding N-Cbz protected glucosides 3a–d, to give the corresponding 2-[3-(alkylcarbamoyl)propionyl] tethered saccharides 5a–d. Intramolecular, ring closing glycosylation of the saccharides with NIS and TMSOTf afforded the tethered β(1→3) linked disaccharides 6a–c, the α(1→3) linked disaccharides 7a–d and the α(1→2) linked disaccharide 8d in ratios depending upon the ring size formed during glycosylation. No β(1→2) linked disaccharides were formed. Molecular modeling of saccharides 6–8 revealed that a strong aromatic stacking interaction between the aromatic parts of the benzyl and benzylidene protecting groups in the galactosyl and glucosyl moieties was mainly responsible for the observed regioselectivity and anomeric selectivity of the ring-closing glycosylation step.
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Fradin, Chantal, Marie Christine Slomianny, Céline Mille, Annick Masset, Raymond Robert, Boualem Sendid, Joachim F. Ernst, Jean Claude Michalski, and Daniel Poulain. "β-1,2 Oligomannose Adhesin Epitopes Are Widely Distributed over the Different Families of Candida albicans Cell Wall Mannoproteins and Are Associated through both N- and O-Glycosylation Processes." Infection and Immunity 76, no. 10 (July 21, 2008): 4509–17. http://dx.doi.org/10.1128/iai.00368-08.
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ABSTRACT β-1,2-Linked mannosides (β-Mans) are believed to contribute to Candida albicans virulence. The presence of β-Mans has been chemically established for two molecules (phosphopeptidomannan [PPM] and phospholipomannan) that are noncovalently linked to the cell wall, where they correspond to specific epitopes. However, a large number of cell wall mannoproteins (CWMPs) also express β-Man epitopes, although their nature and mode of β-mannosylation are unknown. We therefore used Western blotting to map β-Man epitopes for the different families of mannoproteins gradually released from the cell wall according to their mode of anchorage (soluble, released by dithiothreitol, β-1,3 glucan linked, and β-1,6 glucan linked). Reduction of β-Man epitope expression occurred after chemical and enzymatic deglycosylation of the different cell wall fractions, as well as in a secreted form of Hwp1, a representative of the CWMPs linked by glycosylphosphatidylinositol remnants. Enzyme-linked immunosorbent assay inhibition tests were performed to assess the presence of β-Man epitopes in released oligomannosides. A comparison of the results obtained with CWMPs to the results obtained with PPM and the use of mutants with mutations affecting O and N glycosylation demonstrated that both O glycosylation and N glycosylation participate in the association of β-Mans with the protein moieties of CWMPs. This process, which can alter the function of cell wall molecules and their recognition by the host, is therefore more important and more complex than originally thought, since it differs from the model established previously with PPM.
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Ryan, Philip, Andy Hsien Wei Koh, Anna Elizabeth Lohning, and Santosh Rudrawar. "Solid-Phase O-Glycosylation with a Glucosamine Derivative for the Synthesis of a Glycopeptide." Australian Journal of Chemistry 70, no. 10 (2017): 1151. http://dx.doi.org/10.1071/ch17201.
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An efficient synthesis of the O-linked glycosylamino acid Fmoc–l-Ser((Ac)3–β-d-GlcNAc)-OH building block is described. The utility of the method was demonstrated with direct solid-phase O-glycosylation of the hydroxyl group on the amino acid (Ser) side chain of a human α-A crystallin-derived peptide (AIPVSREEK) in nearly quantitative glycosylation yield.
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Schirm, M., M. Kalmokoff, A. Aubry, P. Thibault, M. Sandoz, and S. M. Logan. "Flagellin from Listeria monocytogenes Is Glycosylated with β-O-Linked N-Acetylglucosamine." Journal of Bacteriology 186, no. 20 (October 15, 2004): 6721–27. http://dx.doi.org/10.1128/jb.186.20.6721-6727.2004.
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ABSTRACT Glycan staining of purified flagellin from Listeria monocytogenes serotypes 1/2a, 1/2b, 1/2c, and 4b suggested that the flagellin protein from this organism is glycosylated. Mass spectrometry analysis demonstrated that the flagellin protein of L. monocytogenes is posttranslationally modified with O-linked N-acetylglucosamine (GlcNAc) at up to six sites/monomer. The sites of glycosylation are all located in the central, surface-exposed region of the protein monomer. Immunoblotting with a monoclonal antibody specific for β-O-linked GlcNAc confirmed that the linkage was in the β configuration, this residue being a posttranslational modification commonly observed in eukaryote nuclear and cytoplasmic proteins.
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KONRAD, Robert J., Irina MIKOLAENKO, Joseph F. TOLAR, Kan LIU, and Jeffrey E. KUDLOW. "The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic β-cell O-GlcNAc-selective N-acetyl-β-d-glucosaminidase." Biochemical Journal 356, no. 1 (May 8, 2001): 31–41. http://dx.doi.org/10.1042/bj3560031.
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Streptozotocin (STZ), an analogue of GlcNAc, inhibits purified rat spleen O-GlcNAc-selective N-acetyl-β-d-glucosaminidase (O-GlcNAcase), the enzyme that removes O-GlcNAc from protein. We have shown previously that STZ increases pancreatic islet O-linked protein glycosylation. In light of these data, we investigated the possibility further that STZ causes β-cell death by inhibiting O-GlcNAcase. In isolated islets, the time course and dose curve of STZ-induced O-glycosylation correlated with β-cell toxicity. STZ inhibition of rat islet O-GlcNAcase activity also paralleled that of its β-cell toxicity, with significant inhibition occurring at a concentration of 1mM. In contrast, STZ inhibition of rat brain O-GlcNAcase and β-TC3 insulinoma cell O-GlcNAcase was significantly right-shifted compared with islets, with STZ only significantly inhibiting activity at a concentration of 5mM, the same concentration required for β-TC3 cell toxicity. In comparison, N-methyl-N-nitrosourea, the nitric oxide-donating portion of STZ, did not cause increased islet O-glycosylation, β-cell toxicity or inhibition of β-cell O-GlcNAcase. Enhanced STZ sensitivity of islet O-GlcNAcase compared with O-GlcNAcase from other tissues or an insulinoma cell line suggests why actual islet β-cells are particularly sensitive to STZ. Confirming this idea, STZ-induced islet β-cell toxicity was completely blocked by GlcNAc, which also prevented STZ-induced O-GlcNAcase inhibition, but was not even partially blocked by glucose, glucosamine or GalNAc. Together, these data demonstrate that STZ's inhibition of β-cell O-GlcNAcase is the mechanism that accounts for its diabetogenic toxicity.
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Larsen, Ida Signe Bohse, Yoshiki Narimatsu, Hiren Jitendra Joshi, Lina Siukstaite, Oliver J. Harrison, Julia Brasch, Kerry M. Goodman, et al. "Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins." Proceedings of the National Academy of Sciences 114, no. 42 (October 2, 2017): 11163–68. http://dx.doi.org/10.1073/pnas.1708319114.
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The cadherin (cdh) superfamily of adhesion molecules carry O-linked mannose (O-Man) glycans at highly conserved sites localized to specific β-strands of their extracellular cdh (EC) domains. These O-Man glycans do not appear to be elongated like O-Man glycans found on α-dystroglycan (α-DG), and we recently demonstrated that initiation of cdh/protocadherin (pcdh) O-Man glycosylation is not dependent on the evolutionary conserved POMT1/POMT2 enzymes that initiate O-Man glycosylation on α-DG. Here, we used a CRISPR/Cas9 genetic dissection strategy combined with sensitive and quantitative O-Man glycoproteomics to identify a homologous family of four putative protein O-mannosyltransferases encoded by the TMTC1–4 genes, which were found to be imperative for cdh and pcdh O-Man glycosylation. KO of all four TMTC genes in HEK293 cells resulted in specific loss of cdh and pcdh O-Man glycosylation, whereas combined KO of TMTC1 and TMTC3 resulted in selective loss of O-Man glycans on specific β-strands of EC domains, suggesting that each isoenzyme serves a different function. In addition, O-Man glycosylation of IPT/TIG domains of plexins and hepatocyte growth factor receptor was not affected in TMTC KO cells, suggesting the existence of yet another O-Man glycosylation machinery. Our study demonstrates that regulation of O-mannosylation in higher eukaryotes is more complex than envisioned, and the discovery of the functions of TMTCs provide insight into cobblestone lissencephaly caused by deficiency in TMTC3.
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Pantaleon, M., H. Tan, and P. L. Kaye. "253. Toxic effects of hyperglycaemia arise from induced O-linked glycosylation in early mouse embryos." Reproduction, Fertility and Development 20, no. 9 (2008): 53. http://dx.doi.org/10.1071/srb08abs253.
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Glucose flux through the hexosamine biosynthetic pathway (HBP) which is essential for preimplantation development (1) produces uridine 5′-diphospho-N-acetylglucosamine, a donor substrate for multiple glycosylation reactions including O-linked glycosylation. This novel signalling arm of the HBP, known as the hexosamine signalling pathway (HSP) operates via reversible addition of an O-linked β-N-acetylglucosamine (O-GlcNAc) unit to serine and threonine residues of proteins including transcription factors, cytoskeletal components, metabolic enzymes and cellular signalling components. O-linked glycosylation is functionally reciprocal to phosphorylation at the same residues, altering the activity and/or stability of targeted proteins, thus providing a mechanism for modulating cellular physiology in response to glucose availability. The enzymes regulating this O-GlcNAcylation are the β-linked-O-GlcNAc transferase (OGT) and an O-GlcNAc-selective β-N-acetylglucosaminidase (O-GlcNAcase). We hypothesised that the toxicity of hyperglycemia on early embryos arises from increased flux through HBP and increased O-GlcNAcylation of key proteins. Mouse zygotes (18 h post hCG) were cultured under conditions of modified flux through the HSP including hypoglycemia, hyperglycemia or supplemented with glucosamine which feeds exclusively into the HBP to increase downstream O-GlcNAcylation. BADGP was used to inhibit OGT and O-GlcNAcylation. Blastocyst formation, cell proliferation and apoptosis were assessed. Treatments that perturb levels of intracellular protein O-GlcNAcylation inhibited embryo development. Whilst some flux through HBP is required to activate embryonic differentiation (1), excess flux arising from a hyperglycemic environment or glucosamine supplementation reduced cell proliferation and blastocyst formation, confirming the criticality of this novel post-translational signalling pathway. Inhibition of OGT using 2 mM BADGP blocked the negative impact of hyperglycemia on blastocyst formation, cell number and apoptosis supporting our hypothesis that O-GlcNAcylation is a key mechanism used by the embryo to sense and respond to perturbations of glucose in its environment. (1) Pantaleon M, Scott J and Kaye PL (2008) Biol Reprod, 78(4):595–600
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Staudt, Konrad, Friederike Petra Maria Saxe, Heiko Schmied, Raphael Soeur, Wolfgang Böhme, and Werner Baumgartner. "Comparative Investigations of the Sandfish’s β-Keratin (Reptilia: Scincidae: Scincus scincus). Part 1: Surface and Molecular Examinations." Journal of Biomimetics, Biomaterials and Tissue Engineering 15 (October 2012): 1–16. http://dx.doi.org/10.4028/www.scientific.net/jbbte.15.1.
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The Sandfish (Scincidae: Scincus Scincus) Is a Lizard Capable of Moving through Desert Sand in a Swimming-Like Fashion. the Epidermis of this Lizard Shows a High Resistance against Abrasion Together with a Low Friction to Sand as an Adaption to a Subterranean Life below the Desert’s Surface, Outperforming even Steel. the Low Friction Is Mainly Caused by Chemical Composition of the Scales, which Consist of Glycosylated β-Keratins. in this Study, the Friction, the Micro-Structure, the Glycosylation of the β-Keratin Proteins and β-Keratin Coding DNA of the Sandfish in Comparison to other Reptilian Species Was Investigated, Mainly with the Closely Related Berber Skink (Scincidae: Eumeces Schneideri) and another Sand Swimming Species, the Not Closer Related Shovel-Snouted Lizard (Lacertidae: Meroles Anchietae). Glycosylated β-Keratins of the Sandfish, Visualized with Different Lectins Resulted in O-Linked Glycans through PNA Employed as Carbohydrate Marker. Furthermore, the Glycosylation of β-Keratins in Various Squamatean Species Was Investigated and All Species Tested Were Found Positive; however, it Seems Like both Sand Swimming Species Examined Have a much Stronger Glycosylation of their β-Keratins. in Order to Prove this Finding through a Genetic Foundation, DNA of a β-Keratin Coding Gene of the Sandfish Was Sequenced and Compared with a Homologue Gene of Eumeces Schneideri. by Comparison of the Protein Sequence, a Higher Abundance of O-Glycosylation Sites Was Found in the Sandfish (enabled through the Amino Acids Serine and Threonine), Giving Molecular Support for a Higher Glycosylation of the β-Keratins in this Species.
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Bimboese, Patricia, Craig J. Gibson, Stefan Schmidt, Wanqing Xiang, and Barbara E. Ehrlich. "Isoform-specific Regulation of the Inositol 1,4,5-Trisphosphate Receptor by O-Linked Glycosylation." Journal of Biological Chemistry 286, no. 18 (March 7, 2011): 15688–97. http://dx.doi.org/10.1074/jbc.m110.206482.
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The inositol 1,4,5-trisphosphate receptor (InsP3R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications. We showed previously that InsP3R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci. 27, 13813–13821). We now report the effect of O-GlcNAcylation on InsP3R-2 and InsP3R-3. Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP3R-2, showed no detectable O-GlcNAcylation of InsP3R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide. In contrast, InsP3R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP3R-3, was functionally modified by O-GlcNAcylation. Interestingly, the functional impact of O-GlcNAcylation on the InsP3R-3 channel was opposite the effect measured with InsP3R-1. Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP3R-3 single channel open probability. Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP3-dependent calcium release from the endoplasmic reticulum. The dynamic and inducible nature of O-GlcNAcylation and the InsP3R isoform specificity suggest that this form of modification of InsP3R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
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Greer, Wenda L., Elizabeth Higgins, D. Robert Sutherland, Abraham Novogrodsky, Inka Brockhausen, Monica Peacocke, Laurence A. Rubin, Michael Baker, James W. Dennis, and Katherine A. Siminovitch. "Altered expression of leucocyte sialoglycoprotein in Wiskott-Aldrich syndrome is associated with a specific defect in O-glycosylation." Biochemistry and Cell Biology 67, no. 9 (September 1, 1989): 503–9. http://dx.doi.org/10.1139/o89-081.
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The Wiskott-Aldrich syndrome (WAS) is an X-linked immune deficiency disorder characterized clinically by both lymphocyte and platelet dysfunction. Studies of WAS T lymphocytes have revealed deficient or defective cell surface expression of the highly O-glycosylated leucocyte sialoglycoprotein CD43. To further elucidate the basis for, and functional relevance of, CD43 modifications on WAS lymphocytes, we have studied lymphocytes from two WAS patients with regard to membrane glycoprotein profile and mitogen-induced proliferative responses. CD43 was found to be either absent or altered in size on peripheral blood lymphocytes and lectin-stimulated T cells from both patients. Compared with control cells, the WAS lymphocytes displayed reduced, but measurable proliferative responses to lectins and neuraminidase/galactose oxidase, and virtually no response to periodate, a mitogenic agent which targets sialic acid residues on membrane glycoproteins such as CD43. Analysis of activities of three glycosyltransferases involved in O-glycosylation revealed marked reduction in the level of activity of UDP-N-acetylglucosamine: Galβ1-3GalNAc-R β-1,6-N-acetylglucosamine (β-1,6-GlcNAc) transferase in one WAS patient and no detectable activity of this enzyme in a second. β-1,6-GlcNAc transferase activity has recently been shown to increase during T cell activation coincident with changes in the O-linked glycans on CD43. A selective reduction of this glycosyltransferase in WAS lymphocytes suggests that O-linked oligosaccharides may be important to the structure of membrane glycoproteins involved in lymphocyte activation.Key words: Wiskott-Aldrich syndrome, immune deficiency, O-glycosylation, glycosyltransferase, lymphocyte activation.
Dissertations / Theses on the topic "Β-O-linked glycosylation"
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Frank, Laura Alice. "The role of the hexosamine biosynthesis pathway and β-O-linked glycosylation in determining oocyte developmental competence." Thesis, 2012. http://hdl.handle.net/2440/96463.
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Maternal diabetes and conditions such as obesity in which blood glucose levels are elevated are associated with reduced fertility and poor pregnancy outcomes. Many studies have examined the effects of hyperglycaemia on the early embryo and fetus; however, it is becoming increasingly evident that the peri-conceptual environment surrounding the oocyte has a significant impact on developmental competence and the long-term health of offspring. In this thesis, I aimed to investigate the role of the hexosamine biosynthesis pathway (HBP) in oocyte developmental competence. The HBP is a glucose-metabolising pathway which can also be upregulated by glucosamine, a potent hyperglycaemic mimetic which enters the HBP downstream of the rate-limiting enzyme. The HBP produces uridine diphosphate-N acetylglucosamine, which can be used for the β-O-linked glycosylation (O-GlcNAcylation) of proteins, regulating their function in a similar manner to phosphorylation. Firstly I established the effect of hyper- and hypo-glycaemic conditions during in vitro maturation (IVM) of mouse cumulus-oocyte complexes (COCs) on a range of measures associated with oocyte developmental competence, including cumulus expansion, meiotic maturation, cleavage and blastocyst development rates. A low (1 mM) glucose concentration achieved optimal oocyte competence, and glucose supplementation during only the first hour of IVM was necessary and sufficient to support oocyte maturation and embryo development to the blastocyst stage. Glucosamine was able to substitute for glucose during this first hour. In the absence of glucose throughout IVM, glucosamine was not able to increase developmental competence, and at higher concentrations (2.5 and 5 mM) had a detrimental effect on these outcomes. These experiments underscored the importance of the other glucose metabolic pathways, during COC maturation, and supported the concept that excess flux through the HBP has detrimental consequences. Using Western blots and immunohistochemistry, it was shown that both glucosamine and high glucose levels induced an increase in total O-GlcNAcylation in COCs, which was reduced in the presence of an inhibitor of the β-O-linked glycosyltransferase enzyme. Several specific proteins were identified using mass spectrometry as potential targets of O-GlcNAcylation in COCs, including heat-shock protein 90 (HSP90, both α and β isoforms). While glucosamine treatment of COCs significantly decreased blastocyst development rate, inhibiting HSP90 with 17-allylamino-17-demethoxygeldanamycin during IVM in the presence of glucosamine recovered blastocyst rates to control levels. This effect was not due to an increase in overall HSP90 levels, since inhibiting HSP90 in control COCs did not affect blastocyst rate. These results suggest O-GlcNacylated HSP90 has an aberrant function in the COC. This study is the first to examine in detail O-GlcNAcylation levels in the COC, and their correlation to oocyte developmental competence. HSP90 was identified as a potential target of O-GlcNAcylation in the COC, and subsequently shown to mediate oocyte developmental competence. This research is significant because of the increasing numbers of women wishing to become pregnant who have high blood glucose levels due to diabetes, obesity or poor diet. I have generated critically needed knowledge towards understanding how these lifestyle factors affect fertility and identifying possible avenues for new therapies.Thesis (Ph.D.) -- University of Adelaide, School of Paediatrics and Reproductive Health, 2012
Book chapters on the topic "Β-O-linked glycosylation"
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Kihlberg, Jan. "Glycopeptide synthesis." In Fmoc Solid Phase Peptide Synthesis. Oxford University Press, 1999. http://dx.doi.org/10.1093/oso/9780199637256.003.0012.
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Most eukaryotic proteins, some bacterial and many viral proteins carry structurally diverse carbohydrates that are covalently attached through N- or O-glycosidic bonds to the side chains of asparagine, serine, threonine, hydroxylysine, tyrosine, and hydroxyproline. In nature, N-linked glycoproteins are assembled by post-translational, enzymatic attachment of a common oligosaccharide having the composition Glc3Man9GlcNAc2 to the side chain of asparagine. This saccharide is then modified enzymatically, thereby giving structural variation to the part remote from the protein. However, N-linked glycoproteins have a common pentasaccharide core (Manα3(Manα6)Manβ4GlcNAcβ4GlcNAc) in which the chitobiose moiety (GlcNAcβ4GlcNAc) is bound to asparagine. By contrast, O-linked glycoproteins are built up by sequential attachment of monosaccharides by different enzymes to hydroxylated amino acids in the protein, and therefore no common core is formed. Thus, N-acetyl-α-D-galactosamine attached to serine and threonine is found in mucin secreted from epithelial cells. β-D-Xylosyl serine is found in many proteoglycans, whereas β-D-galactosyl hydroxylysine is common in collagen found in connective tissue. α-L-Fucosyl residues linked to serine and threonine are found in fibrinolytic and coagulation proteins. N-Acetyl-β-D-glucosamine attached to serine and threonine occurs frequently in glycoproteins located in the nucleus and cytoplasm, whereas glycoproteins produced by yeast have α-D-mannosyl residues linked to serine and threonine. Larger structures are usually formed by attachment of additional saccharides to the O-linked 2-4 when found in glycoproteins. Structures 5,10, and 11 can also carry additional monosaccharides. In recent years numerous glycoproteins have been isolated and characterized, but the roles for the protein-bound carbohydrates have only just begun to be unravelled. It is now well established that glycosylation affects both the physiochemical properties and the biological functions of a glycoprotein. For instance, glycosylation has been found to influence uptake, distribution, excretion, and proteolytic stability. It is also known to have important roles in communication between cells and in attachment of bacteria and viruses to the host. Efforts to understand the role of glycosylation of proteins, or to develop glycopeptides as tools in drug discovery and drug design, have led to substantial progress in development of methodology for the synthesis of glycopeptides during the last decades.