Surface N-glycoproteome patterns reveal key proteins of neuronal differentiation

Tyleckova, Jirina; Valeková, Ivona; Žižková, Martina; Rakocyova, Michaela; Marsala, Silvia; Maršala, Martin; Gadher, Suresh Jivan; Kovářová, Hana

doi:10.1016/j.jprot.2015.11.008

Cited by 14 publications

(12 citation statements)

References 37 publications

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“…In addition, antibody-based techniques allow highly sensitive quantification of low abundant proteins, such as secreted growth and trophic or chemotactic factors (Skalnikova et al, 2011;Valekova et al, 2015). Using such techniques, we have previously characterized changes in cellular and signaling proteins during differentiation of porcine NSCs (Skalnikova et al, 2007(Skalnikova et al, , 2008 and in cell surface N-glycoproteins of human NSCs (Tyleckova et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Proteomic Characterization of Human Neural Stem Cells and Their Secretome During in vitro Differentiation

Cervenka

Tyleckova

Skalníková

et al. 2021

Front. Cell. Neurosci.

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Cell therapies represent a promising approach to slow down the progression of currently untreatable neurodegenerative diseases (e.g., Alzheimer's and Parkinson's disease or amyotrophic lateral sclerosis), as well as to support the reconstruction of functional neural circuits after spinal cord injuries. In such therapies, the grafted cells could either functionally integrate into the damaged tissue, partially replacing dead or damaged cells, modulate inflammatory reaction, reduce tissue damage, or support neuronal survival by secretion of cytokines, growth, and trophic factors. Comprehensive characterization of cells and their proliferative potential, differentiation status, and population purity before transplantation is crucial to preventing safety risks, e.g., a tumorous growth due to the proliferation of undifferentiated stem cells. We characterized changes in the proteome and secretome of human neural stem cells (NSCs) during their spontaneous (EGF/FGF2 withdrawal) differentiation and differentiation with trophic support by BDNF/GDNF supplementation. We used LC-MS/MS in SWATH-MS mode for global cellular proteome profiling and quantified almost three thousand cellular proteins. Our analysis identified substantial protein differences in the early stages of NSC differentiation with more than a third of all the proteins regulated (including known neuronal and NSC multipotency markers) and revealed that the BDNF/GDNF support affected more the later stages of the NSC differentiation. Among the pathways identified as activated during both spontaneous and BDNF/GDNF differentiation were the HIF-1 signaling pathway, Wnt signaling pathway, and VEGF signaling pathway. Our follow-up secretome analysis using Luminex multiplex immunoassay revealed significant changes in the secretion of VEGF and IL-6 during NSC differentiation. Our results further demonstrated an increased expression of neuropilin-1 as well as catenin β-1, both known to participate in the regulation of VEGF signaling, and showed that VEGF-A isoform 121 (VEGF121), in particular, induces proliferation and supports survival of differentiating cells.

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Section: Introductionmentioning

confidence: 99%

Proteomic Characterization of Human Neural Stem Cells and Their Secretome During in vitro Differentiation

Cervenka

Tyleckova

Skalníková

et al. 2021

Front. Cell. Neurosci.

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“…Unlike for the hematopoietic lineage, only a limited number of cell surface antigens has previously been assessed on human neural cells . To identify novel neural lineage markers, complementing proteomics approaches , a comprehensive high‐throughput human cell surface antigen screen was conducted. Most antigens analyzed using the screening panel (BD Lyoplate) are classified under the CD nomenclature and have been frequently used for immunophenotyping.…”

Section: Resultsmentioning

confidence: 99%

“…The isolation of specific neural cell types using cluster of differentiation (CD) antigens expressed on the cell surface has been established as a proof of principle . However, a full characterization of the neural surfaceome is currently not available . By exploiting a range of complementary systems ncluding hESCs, long‐term expandable NSCs derived from hiPSCs and immortalized neural precursor cell lines, we performed a comprehensive analysis of neural CD antigen expression.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive Cell Surface Antigen Analysis Identifies Transferrin Receptor Protein-1 (CD71) as a Negative Selection Marker for Human Neuronal Cells

et al. 2019

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Cell state‐, developmental stage‐, and lineage‐specific combinatorial expression of cluster of differentiation (CD) molecules enables the identification of cellular subsets via multicolor flow cytometry. We describe an exhaustive characterization of neural cell types by surface antigens, exploiting human pluripotent stem cell‐derived neural cell systems. Using multiwell screening approaches followed by detailed validation of expression patterns and dynamics, we exemplify a strategy for resolving cellular heterogeneity in stem cell paradigms. In addition to providing a catalog of surface antigens expressed in the neural lineage, we identified the transferrin receptor‐1 (CD71) to be differentially expressed in neural stem cells and differentiated neurons. In this context, we describe a role for N‐Myc proto‐oncogene (MYCN) in maintaining CD71 expression in proliferating neural cells. We report that in vitro human stem cell‐derived neurons lack CD71 surface expression and that the observed differential expression can be used to identify and enrich CD71− neuronal derivatives from heterogeneous cultures. stem cells 2019;37:1293–1306

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“…CSC technology has also been applied to mouse myoblast cells, mouse β -cells, hepatoma cells, leukemia cells, pluripotent stem cells, Drosophila Kc167 cells, and neuronal progenitor cells. 145,156–163 Recently, Wollscheid and co-workers used CSC technology to identify cell-surface proteins in 41 human and 31 mouse cell lines. 164 This work is summarized in a publically available resource: the Cell Surface Protein Atlas (CSPA).…”

Section: Enrichment Of Glycoproteins and Glycopeptidesmentioning

confidence: 99%

Chemical Glycoproteomics

Palaniappan

Bertozzi²

2016

Chem. Rev.

247

205

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Chemical tools have accelerated progress in glycoscience, reducing experimental barriers to studying protein glycosylation, the most widespread and complex form of posttranslational modification. For example, chemical glycoproteomics technologies have enabled the identification of specific glycosylation sites and glycan structures that modulate protein function in a number of biological processes. This field is now entering a stage of logarithmic growth, during which chemical innovations combined with mass spectrometry advances could make it possible to fully characterize the human glycoproteome. In this review, we describe the important role that chemical glycoproteomics methods are playing in such efforts. We summarize developments in four key areas: enrichment of glycoproteins and glycopeptides from complex mixtures, emphasizing methods that exploit unique chemical properties of glycans or introduce unnatural functional groups through metabolic labeling and chemoenzymatic tagging; identification of sites of protein glycosylation; targeted glycoproteomics; and functional glycoproteomics, with a focus on probing interactions between glycoproteins and glycan-binding proteins. Our goal with this survey is to provide a foundation on which continued technological advancements can be made to promote further explorations of protein glycosylation.

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Surface N-glycoproteome patterns reveal key proteins of neuronal differentiation

Cited by 14 publications

References 37 publications

Proteomic Characterization of Human Neural Stem Cells and Their Secretome During in vitro Differentiation

Proteomic Characterization of Human Neural Stem Cells and Their Secretome During in vitro Differentiation

Comprehensive Cell Surface Antigen Analysis Identifies Transferrin Receptor Protein-1 (CD71) as a Negative Selection Marker for Human Neuronal Cells

Chemical Glycoproteomics

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