Potential of MALDI-TOF-based serum N-glycan analysis for the diagnosis and surveillance of breast cancer

Lee, Jong Won; Lee, Kyungsoo; Son, Byung Ho; Ko, Beom Seok; Kim, Hee Jeong; Chung, Il Yong; Kim, Jisun; Lee, Woochang; Ko, Marcia G.; Choi, Soojeong; Chang, Suhwan; Ko, Chung Kon; Lee, Sae Byul; Kim, Dong-Chan

doi:10.1038/s41598-020-76195-y

Cited by 20 publications

(14 citation statements)

References 20 publications

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“… 12 Nowadays, the disease‐related glycosylation alterations of serum and IgG have shown great potential in the biomarker field. 12 , 13 , 14 , 15 , 16…”

Section: Introductionmentioning

confidence: 99%

N‐glycan profiling alterations of serum and immunoglobulin G in immune thrombocytopenia

Wang

Huang

et al. 2021

Clinical Laboratory Analysis

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Background The glycosylation alterations of serum and IgG are involved in a variety of autoimmune and inflammatory diseases and have shown great potential in biomarker field. The diagnosis of immune thrombocytopenia (ITP) is exclusive. Our study aimed to discover the potential glyco‐biomarkers for auxiliary diagnosis of ITP. Methods The serum samples were obtained from 61 ITP patients and 35 healthy controls, and IgG samples were purified from 34 out of 61 ITP patients and 35 healthy controls. DNA sequencer‐assisted fluorophore‐assisted carbohydrate electrophoresis (DSA‐FACE) was used to analyze serum and IgG N‐glycan profiling. Results 6 of 12 serum N‐glycan peaks, 6 of 7 IgG N‐glycan peaks, serum fucosylation, and IgG galactosylation were significantly different between ITP patients and healthy controls (p < 0.05). IgG peak 7 showed good diagnostic efficacy for discriminating ITP patients from healthy individuals (AUC 0.967). ITP patients with severe thrombocytopenia had a significantly lower serum fucosylation than ITP patients with mild and moderate thrombocytopenia (p < 0.05). Serum fucosylation and serum peak 5 were correlated with platelet counts in ITP patients with severe thrombocytopenia, and the absolute values of correlation coefficient were both over 0.5. Conclusions The specific N‐glycan patterns of serum and IgG were observed in ITP patients. IgG peak 7 was a potential biomarker for auxiliary diagnosis of ITP.

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“… 12 Nowadays, the disease‐related glycosylation alterations of serum and IgG have shown great potential in the biomarker field. 12 , 13 , 14 , 15 , 16…”

Section: Introductionmentioning

confidence: 99%

N‐glycan profiling alterations of serum and immunoglobulin G in immune thrombocytopenia

Wang

Huang

et al. 2021

Clinical Laboratory Analysis

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“…Using this approach, they acquired global snapshots of major cellular N-linked glycoforms detected . Since then, the method to image N -glycans using MALDI has been continuously evolving − and has been applied to several tissues (i.e., liver, pancreas, valvular tissues (heart), breast cancer tissue, lung, cells, and biofluids (i.e., serum from breast cancer patients. , The method can be applied both on fresh frozen tissues and on FFPE samples or TMA. Recently, a novel technology, combining MALDI and immunohistochemistry (MALDI-IHC) has been published, using photocleavable mass-tagged (PC-MT) antibodies to visualize intact proteins and a group recently used targeted multiplexed imaging of MALDI-IHC to guide an untargeted bottom-up proteomics analysis of regions of interest based on the localization of the PC-MTs .…”

Section: Sample Preparation Protocolsmentioning

confidence: 99%

A Guide to MALDI Imaging Mass Spectrometry for Tissues

Moore,

Charkoftaki

2023

J. Proteome Res.

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Imaging mass spectrometry is a well-established technology that can easily and succinctly communicate the spatial localization of molecules within samples. This review communicates the recent advances in the field, with a specific focus on matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) applied on tissues. The general sample preparation strategies for different analyte classes are explored, including special considerations for sample types (fresh frozen or formalin-fixed,) strategies for various analytes (lipids, metabolites, proteins, peptides, and glycans) and how multimodal imaging strategies can leverage the strengths of each approach is mentioned. This work explores appropriate experimental design approaches and standardization of processes needed for successful studies, as well as the various data analysis platforms available to analyze data and their strengths. The review concludes with applications of imaging mass spectrometry in various fields, with a focus on medical research, and some examples from plant biology and microbe metabolism are mentioned, to illustrate the breadth and depth of MALDI IMS.

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“…In this context too, the Hex9HexNAc2 structure is especially elevated, which posits the incomplete trimming of pre‐golgi N‐glycan intermediates as a feature of breast cancer. Other MALDI‐based studies of N‐glycosylation in breast cancer serum have detected N‐glycan signatures which delineates recurrent versus non‐recurrent cancer, stage 1 breast cancer from healthy controls and signatures specific to the lymph node invasive subtype (Lee et al, 2020a, 2020b). Taken together, these studies on the complex glycosylation landscape of breast cancer by MALDI IMS are potentially exploitable for clinical surveillance, early detection or delineation of subtypes.…”

Section: Applications Of N‐glycan Imsmentioning

confidence: 99%

Applications and continued evolution of glycan imaging mass spectrometry

McDowell

Mehta

et al. 2021

Mass Spectrometry Reviews

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Glycosylation is an important posttranslational modifier of proteins and lipid conjugates critical for the stability and function of these macromolecules. Particularly important are N‐linked glycans attached to asparagine residues in proteins. N‐glycans have well‐defined roles in protein folding, cellular trafficking and signal transduction, and alterations to them are implicated in a variety of diseases. However, the non‐template driven biosynthesis of these N‐glycans leads to significant structural diversity, making it challenging to identify the most biologically and clinically relevant species using conventional analyses. Advances in mass spectrometry instrumentation and data acquisition, as well as in enzymatic and chemical sample preparation strategies, have positioned mass spectrometry approaches as powerful analytical tools for the characterization of glycosylation in health and disease. Imaging mass spectrometry expands upon these strategies by capturing the spatial component of a glycan's distribution in‐situ, lending additional insight into the organization and function of these molecules. Herein we review the ongoing evolution of glycan imaging mass spectrometry beginning with widely adopted tissue imaging approaches and expanding to other matrices and sample types with potential research and clinical implications. Adaptations of these techniques, along with their applications to various states of disease, are discussed. Collectively, glycan imaging mass spectrometry analyses broaden our understanding of the biological and clinical relevance of N‐glycosylation to human disease.

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Potential of MALDI-TOF-based serum N-glycan analysis for the diagnosis and surveillance of breast cancer

Cited by 20 publications

References 20 publications

N‐glycan profiling alterations of serum and immunoglobulin G in immune thrombocytopenia

N‐glycan profiling alterations of serum and immunoglobulin G in immune thrombocytopenia

A Guide to MALDI Imaging Mass Spectrometry for Tissues

Applications and continued evolution of glycan imaging mass spectrometry

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