CSF N-glycoproteomics for early diagnosis in Alzheimer's disease

Palmigiano, Angelo; Barone, Rita; Sturiale, Luisa; Sanfilippo, Cristina; Bua, Rosaria Ornella; Romeo, Donata Agata; Messina, Angela; Capuana, Maria Luisa; Maci, Tiziana; Pira, Francesco Le; Zappia, Mario; Garozzo, Domenico

doi:10.1016/j.jprot.2015.10.006

Cited by 93 publications

(83 citation statements)

References 25 publications

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“…It was suggested that due to lack of this sugar modification, BACE1 is directed towards late lysosomes, subjected to lysosomal degradation and thus less co-localized with APP [146]. Consistent with the above observation, an N -glycome profiling study indicated an increase in bisecting-GlcNAc type N -glycans and a decrease in overall sialylation in CSF from AD patients compared to normal controls [147]. The decrease in sialylated N -glycans in AD could be attributed to decreased sialyltransferase activity, which has been reported in serum as well as membrane and soluble fractions from postmortem brain from AD patients [148, 149].…”

Section: Changes In Brain Ecm In Neurodegenerative Conditionsmentioning

confidence: 58%

Extracellular matrix proteomics in schizophrenia and Alzheimer’s disease

Sethi

Zaia

2016

Anal Bioanal Chem

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Brain extracellular matrix (ECM) is a highly organized system that consists of collagens, non-collagenous proteins, glycoproteins, hyaluronan and proteoglycans (PGs). Recognized physiological roles of ECM include developmental regulation, tissue homeostasis, cell migration, proliferation, differentiation, neuronal plasticity, and neurite outgrowth. Aberrant ECM structure is associated with brain neurodegenerative conditions. This review focuses on two neurodegenerative conditions, schizophrenia (Sz) and Alzheimer's disease (AD), and summarizes recent findings of altered ECM components, including PGs, glycosaminoglycans (GAGs), proteins and glycoproteins, and proteins and genes related to other brain components. The scope includes immunohistochemical, genomics, transcriptomics, proteomics and glycomics studies, and a critical assessment of current state of proteomics studies for neurodegenerative disorders. The intent is to summarize the ECM molecular alterations associated with neurodegenerative pathophysiology.

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Section: Changes In Brain Ecm In Neurodegenerative Conditionsmentioning

confidence: 58%

Extracellular matrix proteomics in schizophrenia and Alzheimer’s disease

Sethi

Zaia

2016

Anal Bioanal Chem

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“…The two core pathological hallmarks of AD are amyloid plaques composed of amyloid β-peptide (Aβ) and neurofibrillary tangles composed of hyperphosphorylated microtubule-associated protein tau [31]. There is much evidence that alterations in glycosylation patterns influence the pathogenesis and progression of AD [32–35]. APP is processed into Aβ through β-secretase and γ-secretase, while the deposition of Aβ in the brain triggers neuronal dysfunction and death.…”

Section: Resultsmentioning

confidence: 99%

In-depth mapping of the mouse brain N-glycoproteome reveals widespread N-glycosylation of diverse brain proteins

Pan

Wang

et al. 2016

Oncotarget

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N-glycosylation is one of the most prominent and abundant posttranslational modifications of proteins. It is estimated that over 50% of mammalian proteins undergo glycosylation. However, the analysis of N-glycoproteins has been limited by the available analytical technology. In this study, we comprehensively mapped the N-glycosylation sites in the mouse brain proteome by combining complementary methods, which included seven protease treatments, four enrichment techniques and two fractionation strategies. Altogether, 13492 N-glycopeptides containing 8386 N-glycosylation sites on 3982 proteins were identified. After evaluating the performance of the above methods, we proposed a simple and efficient workflow for large-scale N-glycosylation site mapping. The optimized workflow yielded 80% of the initially identified N-glycosylation sites with considerably less effort. Analysis of the identified N-glycoproteins revealed that many of the mouse brain proteins are N-glycosylated, including those proteins in critical pathways for nervous system development and neurological disease. Additionally, several important biomarkers of various diseases were found to be N-glycosylated. These data confirm that N-glycosylation is important in both physiological and pathological processes in the brain, and provide useful details about numerous N-glycosylation sites in brain proteins.

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“…A large number of studies using different methodologies have been published in association with different phenotypes, such as breast, colon, liver, skin, ovary, bladder cancer, and neurological disorders and various structural alterations such as s sialylation, fucosylation, degree of branching, and the expression of specific glycosyltransferases (Azevedo et al, 2017;Christiansen et al, 2014;Palmigiano et al, 2016). For example, cerebrospinal fluid N-glycoproteomics was used for early diagnosis in Alzheimer's disease.…”

Section: Glycoproteomicsmentioning

confidence: 99%

Rise of Systems Glycobiology and Personalized Glycomedicine: Why and How to Integrate Glycomics with Multiomics Science?

Kunej

2019

OMICS: A Journal of Integrative Biology

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Glycomics is a rapidly emerging subspecialty of system sciences that evaluates the structures and functions of glycans in biological systems. Moreover, glycomics informs allied scholarships such as systems glycobiology and personalized glycomedicine that collectively aim to explain the role of glycans in person-to-person and between-population variations in disease susceptibility and response to health interventions such as drugs, nutrition, and vaccines. For glycomics to make greater, systems-scale, contributions to biology and medical research, it is facing a new developmental challenge: transition from single omics to multiomics integrative technology platforms. A comprehensive map of all possible connections between glycomics and other omics types has not yet been developed. Glycomics aims to discover a complex interplay of molecular interactions; however, little is known about the regulatory networks controlling these complex processes. In addition, the glycomics knowledgebase is presently scattered across various publications and databases, and therefore does not enable a holistic or systems view of this study field. Therefore, researchers are not always aware, for example, that a given analyzed genetic locus is linked with glycans, and that there are also glycomics determinants of complex phenotypes in health and biology. This review presents several published examples of glycomics science in association with other omics levels, such as genomics, transcriptomics, proteomics, metabolomics, epigenomics, ncRNomics, lipidomics, and interactomics. I also highlight the salient knowledge gaps and suggest future research directions. Understanding the interconnections of glycomics with other omics technologies will facilitate multiomics science and knowledge integration, enhance development of systems glycobiology and personalized glycomedicine.

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CSF N-glycoproteomics for early diagnosis in Alzheimer's disease

Cited by 93 publications

References 25 publications

Extracellular matrix proteomics in schizophrenia and Alzheimer’s disease

Extracellular matrix proteomics in schizophrenia and Alzheimer’s disease

In-depth mapping of the mouse brain N-glycoproteome reveals widespread N-glycosylation of diverse brain proteins

Rise of Systems Glycobiology and Personalized Glycomedicine: Why and How to Integrate Glycomics with Multiomics Science?

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