Glycosylation and Cardiovascular Diseases

Dashti, Hesam; Porras, Maria Angelica Pabon; Mora, Samia

doi:10.1007/978-3-030-70115-4_15

Cited by 11 publications

(8 citation statements)

References 137 publications

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“…Glycosylation is a post-translational modification (PTM) implicated in viral infection, 1,2 T cell activation and differentiation, 3 reproductive health, 4 and cardiovascular disease. 5 Changes in glycosylation macrohetereogeneity (site occupancy) and microheterogeneity (distinct glycoforms on one site) are known to be relevant in receptor pattern recognition by influenza A viruses, 6 interaction of plasma proteins, 7 cancer, 8,9 and protein/glycan interactions, 10 among many others. This highlights the need to accurately detect changes in glycan localization and composition.…”

Section: Introductionmentioning

confidence: 99%

A systematic comparison of current bioinformatic tools for glycoproteomics data

Rangel-Angarita

Mahoney

Ince

et al. 2022

Preprint

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Glycosylation is one of the most common post-translational modifications and generates an enormous amount of proteomic diversity; changes in glycosylation are associated with nearly all disease states. Intact glycoproteomics seeks to determine the site-localization and composition of glycans along a protein backbone via mass spectrometry. Following data acquisition, raw files are analyzed using search algorithms to define peptide sequence, glycan composition, and site localization. Glycoproteomics is rapidly expanding, creating the pressing need to establish bioinformatic community standards. Recently, several new search algorithms were released, many of which vary in terms of search strategy, localization system, score cutoffs, and glycan databases, thus warranting a comprehensive comparison of these new programs along with existing programs. Here, we analyzed three common samples: an enriched cell lysate, a mixture of 6 glycoproteins, and a mucin-domain glycoprotein. All raw files were searched with comparable parameters among software and the results were extensively manually validated to compare accuracy and completion of the output. Our results highlight the continued need for manual validation of glycopeptide spectral matches, especially for O-glycopeptides. Despite this, O-Pair outperformed all other programs in correct identification of O-glycopeptides and its localization system proved to be useful. On the other hand, Byonic and pGlyco performed best for N-glycoproteomics; the former was best for proteome-wide searches, but the latter identified more N-glycosites in less complex samples. Overall, we summarize the strengths, weaknesses, and potential improvements for these search algorithms.

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Section: Introductionmentioning

confidence: 99%

A systematic comparison of current bioinformatic tools for glycoproteomics data

Rangel-Angarita

Mahoney

Ince

et al. 2022

Preprint

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show abstract

“…For instance, glycosylation is integral in viral infection, 6−8 T cell activation and differentiation, 9 and its dysregulation has been observed in a plethora of diseases. 4,10,11 While mass spectrometry (MS) is the premier technique to characterize glycoproteins, the study of intact glycopeptides presents challenges not faced during typical proteomic studies. For instance, glycopeptides are often suppressed by unmodi-fied peptides.…”

Section: ■ Introductionmentioning

confidence: 99%

False-Positive Glycopeptide Identification via In-FAIMS Fragmentation

Rangel-Angarita,

Mahoney,

Kwon

et al. 2023

JACS Au

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High-field asymmetric waveform ion mobility spectrometry (FAIMS) separates glycopeptides in the gas phase prior to mass spectrometry (MS) analysis, thus offering the potential to analyze glycopeptides without prior enrichment. Several studies have demonstrated the ability of FAIMS to enhance glycopeptide detection but have primarily focused on N-glycosylation. Here, we evaluated FAIMS for O-glycoprotein and mucin-domain glycoprotein analysis using samples of varying complexity. We demonstrated that FAIMS was useful in increasingly complex samples as it allowed for the identification of more glycosylated species. However, during our analyses, we observed a phenomenon called “in FAIMS fragmentation” (IFF) akin to in source fragmentation but occurring during FAIMS separation. FAIMS experiments showed a 2- to 5-fold increase in spectral matches from IFF compared with control experiments. These results were also replicated in previously published data, indicating that this is likely a systemic occurrence when using FAIMS. Our study highlights that although there are potential benefits to using FAIMS separation, caution must be exercised in data analysis because of prevalent IFF, which may limit its applicability in the broader field of O-glycoproteomics.

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“…Alterations in total the plasma protein and IgG glycosylation have also been reported in many other diseases and conditions, and have shown potential as biomarkers [ 18 ]. IgG in particular has been implicated in a variety of inflammatory and metabolic conditions, such as rheumatoid arthritis, obesity, cardiovascular disease (CVD), and aging [ 19 , 20 ]. IgG is an important modulator of the immune system, and through its effector functions, can have pro- or anti-inflammatory effects.…”

Section: Introductionmentioning

confidence: 99%

The N-Glycosylation of Total Plasma Proteins and IgG in Atrial Fibrillation

et al. 2023

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Atrial fibrillation is a disease with a complex pathophysiology, whose occurrence and persistence are caused not only by aberrant electrical signaling in the heart, but by the development of a susceptible heart substrate. These changes, such as the accumulation of adipose tissue and interstitial fibrosis, are characterized by the presence of inflammation. N-glycans have shown great promise as biomarkers in different diseases, specifically those involving inflammatory changes. To assess the changes in the N-glycosylation of the plasma proteins and IgG in atrial fibrillation, we analyzed the N-glycosylation of 172 patients with atrial fibrillation, before and six months after a pulmonary vein isolation procedure, with 54 cardiovascularly healthy controls. An analysis was performed using ultra-high-performance liquid chromatography. We found one oligomannose N-glycan structure from the plasma N-glycome and six IgG N-glycans, mainly revolving around the presence of bisecting N-acetylglucosamine, that were significantly different between the case and control groups. In addition, four plasma N-glycans, mostly oligomannose structures and a derived trait that was related to them, were found to be different in the patients who experienced an atrial fibrillation recurrence during the six-month follow-up. IgG N-glycosylation was extensively associated with the CHA2DS2-VASc score, confirming its previously reported associations with the conditions that make up the score. This is the first study looking at the N-glycosylation patterns in atrial fibrillation and warrants further investigation into the prospect of glycans as biomarkers for atrial fibrillation.

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Glycosylation and Cardiovascular Diseases

Cited by 11 publications

References 137 publications

A systematic comparison of current bioinformatic tools for glycoproteomics data

A systematic comparison of current bioinformatic tools for glycoproteomics data

False-Positive Glycopeptide Identification via In-FAIMS Fragmentation

The N-Glycosylation of Total Plasma Proteins and IgG in Atrial Fibrillation

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