N-glycosylation patterns of HSA/CD24 from different cell lines and brain homogenates: a comparison

Ohl, Christiane; Albach, Claus; Altevogt, Peter; Schmitz, Brigitte

doi:10.1016/s0300-9084(03)00107-x

Cited by 23 publications

(25 citation statements)

References 37 publications

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“…CD24 is a GPI-anchored membrane glycoprotein possesses several potential N - and O -glycosylation sites, which are extensively used so that strikingly high apparent molecular weights are observed ranging from 28-70kDa [46]. In the cytoplasm the protein appears as a single ∼30kDa protein.…”

Section: Resultsmentioning

confidence: 99%

BRCA1-IRIS overexpression promotes and maintains the tumor initiating phenotype: implications for triple negative breast cancer early lesions

et al. 2016

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Tumor-initiating cells (TICs) are cancer cells endowed with self-renewal, multi-lineage differentiation, increased chemo-resistance, and in breast cancers the CD44+/CD24-/ALDH1+ phenotype. Triple negative breast cancers show lack of BRCA1 expression in addition to enhanced basal, epithelial-to-mesenchymal transition (EMT), and TIC phenotypes. BRCA1-IRIS (hereafter IRIS) is an oncogene produced by the alternative usage of the BRCA1 locus. IRIS is involved in induction of replication, transcription of selected oncogenes, and promoting breast cancer cells aggressiveness. Here, we demonstrate that IRIS overexpression (IRISOE) promotes TNBCs through suppressing BRCA1 expression, enhancing basal-biomarkers, EMT-inducers, and stemness-enforcers expression. IRISOE also activates the TIC phenotype in TNBC cells through elevating CD44 and ALDH1 expression/activity and preventing CD24 surface presentation by activating the internalization pathway EGFR→c-Src→cortactin. We show that the intrinsic sensitivity to an anti-CD24 cross-linking antibody-induced cell death in membranous CD24 expressing/luminal A cells could be acquired in cytoplasmic CD24 expressing IRISOE TNBC/TIC cells through IRIS silencing or inactivation. We show that fewer IRISOE TNBC/TICs cells form large tumors composed of TICs, resembling TNBCs early lesions in patients that contain metastatic precursors capable of disseminating and metastasizing at an early stage of the disease. IRIS-inhibitory peptide killed these IRISOE TNBC/TICs, in vivo and prevented their dissemination and metastasis. We propose IRIS inactivation could be pursued to prevent dissemination and metastasis from early TNBC tumor lesions in patients.

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Section: Resultsmentioning

confidence: 99%

BRCA1-IRIS overexpression promotes and maintains the tumor initiating phenotype: implications for triple negative breast cancer early lesions

et al. 2016

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“…Two reports in 2009 identifying CD24 in mouse brain with structures containing α2,3-linked NeuAc, disialyl motifs, Lewis x sLe x or HNK-1 epitopes in O-glycans [37], and α2, 3-linked N-acetylneuraminic acid (NeuAc), Lewis x H antigens, bisecting N-acetylglucosamine in N-glycans [38] ( Table 1). Evidence shows that the glycosylation pattern seems to be variable in different tissues, which may account for the functional diversity of CD24 [39]. There are several ligands found to bind to CD24 protein, including P-selectin is expressed by many cell types, including immature lymphocytes, developing neuronal cells, regenerating muscle cells, granulocytes, monocytes, dendritic cells, macrophages, keratinocytes, epidermal Langerhans cells, epithelial cells, and erythrocytes [40], sialic-acid-binding immunoglobulin-like lectin-G (Siglec-G, mouse) or Siglec 10 (human) [41], neural recognition molecule L1 [42], TAG-1, Contactin [43], and some damage-associated molecular patterns (DAMPs) such as HMGB1 [41].…”

Section: Glycosylation Pattern Ligands Of Cd24mentioning

confidence: 99%

CD24: from a Hematopoietic Differentiation Antigen to a Genetic Risk Factor for Multiple Autoimmune Diseases

Tan

Zhao

Xiang

et al. 2015

Clinic Rev Allerg Immunol

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The autoantibody is an essential characteristic of inflammatory disorders, including autoimmune diseases. Although the exact pathogenic mechanisms of these diseases remain elusive, accumulated evidence has implicated that genetic factors play important roles in autoimmune inflammation. Among these factors, CD24 was first identified as a heat-stable antigen in 1978 and first successfully cloned in 1990. Thereafter, its functional roles have been intensively investigated in various human diseases, especially autoimmune diseases and cancers. It is currently known that CD24 serves as a costimulatory factor of T cells that regulate their homeostasis and proliferation, while in B cells, CD24 is functionally involved in cell activation and differentiation. CD24 can enhance autoimmune diseases in terms of its protective role in the clonal deletion of autoreactive thymocytes. Furthermore, CD24 deficiency has been linked to mouse experimental autoimmune encephalomyelitis. Finally, CD24 genetic variants, including single-nucleotide polymorphisms and deletions, are etiologically relevant to autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus. Therefore, CD24 is a promising biomarker and novel therapeutic target for autoimmune diseases.

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“…We could show that all six potential N-glycosylation sites of NCAM from adult mouse brain are modified, at least one of these (N-1) only partially. The differential approach employed here should be particularly valuable in the case of highly heterogeneous glycosylations as found for glycoproteins from different cellular systems and species [15,16,17,26,27,31,32,33,34,35,36,37,38,39,40]. Direct MALDI-TOF-MS studies of glycopeptides have shown pronounced heterogeneous structures on single N-glycosylation sites of NCAM [26].…”

Section: Discussionmentioning

confidence: 99%

“…N-1 was not detected in bovine NCAM and neither N-1 nor N-4 could be identified in murine NCAM in the glycosylated or the non-glycosylated form which may be explained by the strategy in these studies employing enrichment of glycopeptides with antibodies against PSA or HNK-1. Most likely N-1 and N-4 carry acidic and neutral glycans of the types as identified in several studies to be conserved between rodent, bovine, and human brain glycoproteins [15,16,17,27,35,36,37,38,39,40]. Such heterogeneities, and additional problems observed by proteolytic and hydrolytic side-reactions upon deglycosylation may complicate the mass spectrometric analysis of glycosylation sites, thus rendering high-resolution MS approaches particularly valuable as a general method to define glycosylation site usage in glycoproteins.…”

Section: Discussionmentioning

confidence: 99%

Identification of N -glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry

Albach

Damoc

Denzinger

et al. 2004

Analytical and Bioanalytical Chemistry

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Mass spectrometry has been shown in recent years to be a powerful tool to determine accurate molecular masses and sequences of peptides and proteins and post-translational modifications such as glycosylation, phosphorylation, and sulfation. For glycosylation, it has been increasingly recognized to be of pivotal importance to identify whether potential glycosylation sites are actually modified by glycans, because functions of proteins may be modulated or depend on the presence of glycans at specific sites. Several recent reports have established that mass spectrometric techniques such as matrix-assisted laser desorption/ionization or electrospray ionization mass spectrometry (MALDI-TOF or ESI-MS, respectively) with or without preceding HPLC and in combination with PNGase F treatment are suited to analyze whether consensus sequences for N-glycosylation are glycosylated or not. Here we report the mass spectrometric analysis of the six potential N-glycosylation sites of the neural cell adhesion molecule NCAM from adult mouse brain. Unmodified peptides and glycopeptides each carrying a single glycosylation site were generated from NCAM by AspN and trypsin treatment and submitted to reversed-phase HPLC with or without prior enzymatic release of N-glycans. The resulting peptides were analyzed by MALDI-TOF-MS. In addition, high-resolution Fourier transform-ion cyclotron resonance (MALDI-FTICR) mass spectrometry was performed after in-gel deglycosylation and subsequent trypsin digestion. By using these procedures all six consensus sequences were shown to be glycosylated; the observation of an unmodified peptide with the consensus sequence N-1 indicates only partial glycosylation at this site.

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N-glycosylation patterns of HSA/CD24 from different cell lines and brain homogenates: a comparison

Cited by 23 publications

References 37 publications

BRCA1-IRIS overexpression promotes and maintains the tumor initiating phenotype: implications for triple negative breast cancer early lesions

BRCA1-IRIS overexpression promotes and maintains the tumor initiating phenotype: implications for triple negative breast cancer early lesions

CD24: from a Hematopoietic Differentiation Antigen to a Genetic Risk Factor for Multiple Autoimmune Diseases

Identification of N -glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry

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