Decreased serum levels of nucleolin protein fragment, as analyzed by bead-based proteomic technology, in multiple sclerosis patients compared to controls

Liu, Jianghong; Yin, Linlin; Dong, Hui; Xu, Erhe; Zhang, Lan; Liu, Yuan; Li, Lin; Jia, Jianping

doi:10.1016/j.jneuroim.2012.05.002

Cited by 20 publications

(17 citation statements)

References 33 publications

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“…They have been quantitated as unique peptides from pooled and individual patients and confirmed using antibody detection, LC-MS/MS, and gel slice identification from Western blots. The importance of fragmented forms of larger inflammatory marker proteins have been noted in the literature and include C-reactive protein, ApoE, nucleolin, and collagen among others; these fragments are released from tissue into the circulation (39,40).…”

Section: Discussionmentioning

confidence: 99%

Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective

Wasinger

Yau

Duo

et al. 2016

Molecular & Cellular Proteomics

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Breakdown of the protective gut barrier releases effector molecules and degradation products into the blood stream making serum and plasma ideal as a diagnostic medium. The enriched low mass proteome is unexplored as a source of differentiators for diagnosing and monitoring inflammatory bowel disease (IBD) activity, that is less invasive than colonoscopy. Differences in the enriched low mass plasma proteome (<25 kDa) were assessed by label-free quantitative mass-spectrometry. A panel of marker candidates were progressed to validation phase and "Tier-2" FDA-level validated quantitative assay. Proteins important in maintaining gut barrier function and homeostasis at the epithelial interface have been quantitated by multiple reaction monitoring in plasma and serum including both inflammatory; rheumatoid arthritis controls, and non-inflammatory healthy controls; ulcerative colitis (UC), and Crohn's disease (CD) patients. Detection by immunoblot confirmed presence at the protein level in plasma. Correlation analysis and receiver operator characteristics were used to report the sensitivity and specificity. Peptides differentiating controls from IBD originate from secreted phosphoprotein 24 (SPP24, p ‫؍‬ 0.000086, 0.009); whereas those in remission and healthy can be differentiated in UC by SPP24 (p ‫؍‬ 0.00023, 0.001), ␣-1-microglobulin (AMBP, p ‫؍‬ 0.006) and CD by SPP24 (p ‫؍‬ 0.019, 0.05). UC and CD can be differentiated by Guanylin (GUC2A, p ‫؍‬ 0.001), and Secretogranin-1 (CHGB p ‫؍‬ 0.035). Active and quiescent disease can also be differentiated in UC and CD by CHGB (p < 0.023) SPP24 (p < 0.023) and AMBP (UC p ‫؍‬ 0.046). Five peptides discriminating IBD activity and severity had very little-to-no correlation to erythrocyte sedimentation rate, C-reactive protein, white cell or platelet counts. Three of these peptides were found to be binding partners to SPP24 protein alongside other known matrix proteins. These proteins have the potential to improve diagnosis and evaluate IBD activity, reducing the need for more invasive techniques. Data are available via ProteomeXchange with identifier

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Section: Discussionmentioning

confidence: 99%

Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective

Wasinger

Yau

Duo

et al. 2016

Molecular & Cellular Proteomics

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“…Even though eradication of established disease was not possible, atherosclerotic lesion formation could be modified using AAVmediated gene transfer of the sMSR. 28) As nucleolin is also detected in serum, 29) nucleolin operation in vivo might also be a useful means of preventing and treating SRs-involved diseases, including atherosclerosis.…”

Section: Discussionmentioning

confidence: 99%

Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages

et al. 2015

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Scavenger receptors have a broad range of functions that include pathogen clearance, and identification of the scavenger receptor family has been of great benefit to the field of physiology. The shuttling-protein nucleolin has recently been shown to possess scavenger receptor-like activity. We therefore investigated whether or not nucleolin is a receptor for maleylated-bovine serum albumin (maleylated-BSA), which is a common ligand for scavenger receptors. Binding and phagocytosis of native control-BSA by thioglycollateelicited mouse peritoneal macrophages was weak, but that of maleylated-BSA was strong. Surface plasmonresonance analysis revealed that nucleolin strongly associated with maleylated-BSA but not control-BSA or maleic anhydride. Further, co-treatment of macrophages with anti-nucleolin antibody, but not control-immunoglobulin G, inhibited binding of maleylated-BSA. In addition, antineoplastic guanine rich oligonucleotide (AGRO), a nucleolin-specific oligonucleotide aptamer, inhibited binding of maleylated-BSA. Further, binding of maleylated-BSA to nucleolin-transfected HEK293 cells was higher than that by control HEK cells. These results indicate that nucleolin is a receptor that enables macrophages to recognize maleylated-BSA.

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“…43) Nucleolin also lacks a transmembrane domain, is detected in serum, and is reduced in quantity under conditions of neurodegenerative diseases. 19,20,44) Therefore, nucleolin operation in vivo may also be a useful means of preventing and treating toxic AGE-derived diseases.…”

Section: Discussionmentioning

confidence: 99%

Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin

Miki

Dambara

Tachibana

et al. 2014

Biological & Pharmaceutical Bulletin

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Advanced glycosylation end-products (AGEs) are non-enzymatically glycosylated proteins that play an important role in several diseases and aging processes, including angiopathy, renal failure, diabetic complications, and some neurodegenerative diseases. In particular, glyceraldehyde (GCA)-and glycolaldehyde (GOA)-derived AGEs are deemed toxic AGEs, due to their cytotoxicity. Recently, the shuttling-protein nucleolin has been shown to possess scavenger receptor-activity. Here, we investigated whether or not macrophages recognize toxic AGEs through nucleolin receptors expressed on their surface. Free amino acid groups and arginine residues found in bovine serum albumin (BSA) were time-dependently modified by incubation with GCA and GOA. In addition, average molecular size was increased by incubation with GCA and GOA. While GCA-treated BSA (GCA-BSA) and GOA-treated BSA (GOA-BSA) were recognized by thioglycollate-elicited mouse peritoneal macrophages in proportion to their respective aldehyde-modification ratios, aldehyde-untreated control-BSA was not. Surface plasmon-resonance analysis revealed that nucleolin strongly associated with GCA-BSA and GOA-BSA, but not with control-BSA. Further, pretreating macrophages with anti-nucleolin antibody, but not control-Immunoglobulin G, inhibited recognition of GCA-BSA and GOA-BSA by macrophages. Additionally, AGRO, a nucleolin-specific oligonucleotide aptamer, inhibited recognition of GCA-BSA and GOA-BSA. Moreover, nucleolin-transfected HEK293 cells recognized more GCA-BSA and GOA-BSA than control HEK cells did. Binding of nucleolin and GCA-BSA/GOA-BSA was also blocked by anti-nucleolin antibody at molecular level. These results indicate that nucleolin is a receptor that allows macrophages to recognize toxic AGEs.Key words advanced glycosylation end-product (AGE); glyceraldehyde; glycolaldehyde; macrophage; nucleolin; toxic AGE The modification, aggregation, and deposition of proteins are prominent events in many pathological processes and can play a direct role in tissue damage. Advanced glycation end-products (AGEs) are one type of post-translational modification product that form from non-enzymatic reactions between proteins and reducing sugars, dicarbonyl compounds, or reactive aldehydes such as α-hydroxyaldehyde, which are followed by several chemical modifications including crosslinking, rearrangement, and condensation.

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Decreased serum levels of nucleolin protein fragment, as analyzed by bead-based proteomic technology, in multiple sclerosis patients compared to controls

Cited by 20 publications

References 33 publications

Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective

Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective

Nucleolin Is a Receptor for Maleylated-Bovine Serum Albumin on Macrophages

Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin

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