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Journal of Chromatography. B,... Oct 2005Liquid chromatography (LC)-mass spectrometry (MS) has developed into an invaluable technology for the analysis of protein glycosylation. This review focuses on the... (Review)
Review
Liquid chromatography (LC)-mass spectrometry (MS) has developed into an invaluable technology for the analysis of protein glycosylation. This review focuses on the recent developments in LC and combinations thereof with MS for this field of research. Recently introduced methods for the structural analysis of released glycans (native or derivatised) as well as glycopeptides, on normal phase, reverse phase and graphitized carbon LC columns with online MS(/MS) will be reviewed. Performed on nano-scale or capillary-scale, these LC-MS methods operate at femtomole sensitivity and support the further integration of glycosylation analysis in proteomics methodology.
Topics: Chromatography, High Pressure Liquid; Chromatography, Liquid; Glycopeptides; Glycoproteins; Glycosylation; Lectins; Mass Spectrometry; Polysaccharides; Proteins; Sensitivity and Specificity
PubMed: 16213446
DOI: 10.1016/j.jchromb.2005.01.030 -
Biochemical Society Transactions Feb 2013Every living cell is covered with a dense and complex array of covalently attached sugars or sugar chains. The majority of these glycans are linked to proteins via the... (Review)
Review
Every living cell is covered with a dense and complex array of covalently attached sugars or sugar chains. The majority of these glycans are linked to proteins via the so-called glycosylation process. Protein glycosylation is found in all three domains of life: Eukarya, Bacteria and Archaea. However, on the basis of the limit in analytic tools for glycobiology and genetics in Archaea, only in the last few years has research on archaeal glycosylation pathways started mainly in the Euryarchaeota Haloferax volcanii, Methanocaldococcus maripaludis and Methanococcus voltae. Recently, major steps of the crenarchaeal glycosylation process of the thermoacidophilic archaeon Sulfolobus acidocaldarius have been described. The present review summarizes the proposed N-glycosylation pathway of S. acidocaldarius, describing the phenotypes of the mutants disrupted in N-glycan biosynthesis as well as giving insights into the archaeal O-linked and glycosylphosphatidylinositol anchor glycosylation process.
Topics: Archaeal Proteins; Genes, Archaeal; Glycosylation; Glycosylphosphatidylinositols; Lipid Metabolism; Polysaccharides; Sulfolobus acidocaldarius
PubMed: 23356316
DOI: 10.1042/BST20120296 -
Biochimica Et Biophysica Acta Aug 2016Complex diseases such as cancer are a consequence of numerous causes. State of the art personalised medicine approaches are mostly based on evaluating patients'... (Review)
Review
BACKGROUND
Complex diseases such as cancer are a consequence of numerous causes. State of the art personalised medicine approaches are mostly based on evaluating patients' individual genetic background. Despite the advances of genomics it fails to take individual dynamic influences into account that contribute to the individual and unique glycomic and glycoproteomic "configurations" of every living being.
SCOPE OF REVIEW
Glycomic and glycoproteomic-based personalised medicine diagnostics are still in their infancies, however some initial success stories indicate that these fields are highly promising to mediate novel early diagnosis and disease stratification markers, subsequently resulting in improved patient well-being and reduced treatment costs. In this review we not only summarise current protein glycosylation based examples that substantially improve or possess great potential for personalised medicine, but also describe current limitations as well as future perspectives and challenges associated with establishing protein glycosylation aspects for this purpose.
MAJOR CONCLUSIONS
Many protein biomarkers currently in clinical use are glycoproteins, however, their glycosylation status is seldom evaluated in a clinical context. To date just few examples have already been successfully translated into clinical practice, making protein glycosylation a highly promising diagnostic target with humongous potential for personalised medicine.
GENERAL SIGNIFICANCE
There is an urgent need for markers that enable the establishment of an individualised and optimised patient treatment at the earliest disease stage possible. The glycosylation status of a patient and/or specific marker proteins can provide important clues that result in improved patient management. This article is part of a Special Issue entitled "Glycans in personalised medicine" Guest Editor: Professor Gordan Lauc.
Topics: Biomarkers; Glycoproteins; Glycosylation; Humans; Precision Medicine
PubMed: 26987810
DOI: 10.1016/j.bbagen.2016.03.012 -
Journal of Proteome Research Oct 2020Glycosylation is one of the most important post-translational modifications of proteins and plays an essential role in spermatogenesis, maturation, extracellular quality... (Review)
Review
Glycosylation is one of the most important post-translational modifications of proteins and plays an essential role in spermatogenesis, maturation, extracellular quality control, capacitation, sperm-egg recognition, and final fertilization. Spermatozoa are synthesized in the testes inactively with a thick glycocalyx and passed through the epididymis for further modification by glycosylation, deglycosylation, and integration to reach maturation. Subsequently, sperm capacitation and further fertilization require redistribution of glycoconjugates and dramatic glycocalyx modification of the spermatozoa surface. Furthermore, glycoproteins and glycans in seminal plasma are functional in maintaining spermatozoa structure and stability. Therefore, aberrant glycosylation may cause alteration of semen function and even infertility. Currently, mass spectrometry-based technologies have allowed large-scale profiling of glycans and glycoproteins in human semen. Quantitative analysis of semen glycosylation has also indicated many involved glycoproteome issues in male infertility and the potential biomarkers for diagnosis of male infertility in clinical. This review summarizes the role of glycosylation during spermatozoa development, the large-scale profiling of glycome and glycoproteome in human semen, as well as the association of aberrant glycosylation with infertility.
Topics: Epididymis; Glycosylation; Humans; Infertility, Male; Male; Semen; Spermatozoa
PubMed: 32875803
DOI: 10.1021/acs.jproteome.9b00795 -
Annual Review of Biochemistry 1987
Review
Topics: Fungal Proteins; Glycoproteins; Glycosylation; Oligosaccharides; Saccharomyces cerevisiae
PubMed: 3304149
DOI: 10.1146/annurev.bi.56.070187.004411 -
Glycobiology Sep 2010While each of the three domains of life on Earth possesses unique traits and relies on characteristic biological strategies, some processes are common to Eukarya,... (Review)
Review
While each of the three domains of life on Earth possesses unique traits and relies on characteristic biological strategies, some processes are common to Eukarya, Bacteria and Archaea. Once believed to be restricted to Eukarya, it is now clear that Bacteria and Archaea are also capable of performing N-glycosylation. However, in contrast to Bacteria, where this posttranslational modification is still considered a rare event, numerous species of Archaea, isolated from a wide range of environments, have been reported to contain proteins bearing Asn-linked glycan moieties. Analysis of the chemical composition of the Asn-linked polysaccharides decorating archaeal proteins has, moreover, revealed the use of a wider variety of sugar subunits than seen in either eukaryal or bacterial glycoproteins. Still, although first reported some 30 years ago, little had been known of the steps or components involved in the archaeal version of this universal posttranslational modification. Now, with the availability of sufficient numbers of genome sequences and the development of appropriate experimental tools, molecular analysis of archaeal N-glycosylation pathways has become possible. Accordingly using halophilic, methanogenic and thermophilic model species, insight into the biosynthesis and attachment of N-linked glycans decorating archaeal glycoproteins is starting to amass. In this review, current understanding of N-glycosylation in Archaea is described.
Topics: Archaea; Carbohydrate Metabolism; Carbohydrate Sequence; Carbohydrates; Ecosystem; Glycosylation; Molecular Sequence Data; Protein Processing, Post-Translational; Proteins
PubMed: 20371512
DOI: 10.1093/glycob/cwq055 -
Current Opinion in Chemical Biology Jun 2024Protein glycosylation is one of the most common and important post-translational modifications of proteins involved in regulating glycoprotein functions. The... (Review)
Review
Protein glycosylation is one of the most common and important post-translational modifications of proteins involved in regulating glycoprotein functions. The chemoenzymatic glycan labeling strategy allows rapid, efficient, and selective interrogation of glycoproteins. Glycoproteomics identifies protein glycosylation events at a large scale, providing information such as peptide sequences, glycan structures, and glycosylated sites. This review discusses the recent development of chemoenzymatic labeling strategies for glycoprotein analysis, mainly including glycoprotein and glycosite profiling. Furthermore, we highlight the chemoenzymatic enrichment approaches in mass spectrometry analysis for three classes of glycan modifications, including N-glycosylation, O-GlcNAcylation, and mucin-type O-glycosylation. Finally, we highlight the emerging trends in new tools and cutting-edge technologies available for glycoproteomic research.
Topics: Glycosylation; Glycoproteins; Humans; Proteomics; Polysaccharides; Protein Processing, Post-Translational; Animals; Mass Spectrometry; Staining and Labeling
PubMed: 38678979
DOI: 10.1016/j.cbpa.2024.102460 -
Antonie Van Leeuwenhoek Feb 1992
Review
Topics: Animals; Fungal Proteins; Glycosylation; Saccharomyces cerevisiae
PubMed: 1580614
DOI: 10.1007/BF00580620 -
Expert Review of Proteomics Feb 2018Protein glycosylation is recognized as an important post-translational modification, with specific substructures having significant effects on protein folding,... (Review)
Review
Protein glycosylation is recognized as an important post-translational modification, with specific substructures having significant effects on protein folding, conformation, distribution, stability and activity. However, due to the structural complexity of glycans, elucidating glycan structure-function relationships is demanding. The fine detail of glycan structures attached to proteins (including sequence, branching, linkage and anomericity) is still best analysed after the glycans are released from the purified or mixture of glycoproteins (glycomics). The technologies currently available for glycomics are becoming streamlined and standardized and many features of protein glycosylation can now be determined using instruments available in most protein analytical laboratories. Areas covered: This review focuses on the current glycomics technologies being commonly used for the analysis of the microheterogeneity of monosaccharide composition, sequence, branching and linkage of released N- and O-linked glycans that enable the determination of precise glycan structural determinants presented on secreted proteins and on the surface of all cells. Expert commentary: Several emerging advances in these technologies enabling glycomics analysis are discussed. The technological and bioinformatics requirements to be able to accurately assign these precise glycan features at biological levels in a disease context are assessed.
Topics: Biomarkers; Glycomics; Glycosylation; Humans; Molecular Diagnostic Techniques; Polysaccharides; Protein Processing, Post-Translational; Proteome
PubMed: 29285957
DOI: 10.1080/14789450.2018.1421946 -
Hua Xi Kou Qiang Yi Xue Za Zhi = Huaxi... Jun 2018Protein glycosylation is one of the most important protein post-translational modifications that can affect life activities by endowing the protein with various... (Review)
Review
Protein glycosylation is one of the most important protein post-translational modifications that can affect life activities by endowing the protein with various structural and functional features. Saliva is an easy-to-obtain, noninvasive body fluid that contains components originating from serum, gingival crevicular fluid, and oropharyngeal mucosae. In recent years, understanding of saliva has been constantly updated with the developments in related research. Studies have shown that salivary proteins can be used as diagnostic markers for certain diseases, and changes of protein glycosylation in saliva are generally considered to be related to many diseases. In this review, salivary protein glycosylation and its relationship with systemic and oral diseases were discussed.
Topics: Gingival Crevicular Fluid; Glycosylation; Humans; Mouth Diseases; Saliva; Salivary Proteins and Peptides
PubMed: 29984939
DOI: 10.7518/hxkq.2018.03.020