LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 5 of total 5

Search options

  1. Article: Quantitative Proteomic Analysis Reveals Impaired Axonal Guidance Signaling in Human Postmortem Brain Tissues of Chronic Traumatic Encephalopathy.

    Bi, Baibin / Choi, Han-Pil / Hyeon, Seung Jae / Sun, Shengnan / Su, Ning / Liu, Yuguang / Lee, Junghee / Kowall, Neil W / McKee, Ann C / Yang, Jing-Hua / Ryu, Hoon

    Experimental neurobiology

    2019  Volume 28, Issue 3, Page(s) 362–375

    Abstract: Chronic traumatic encephalopathy (CTE) is a distinct neurodegenerative disease that associated with repetitive head trauma. CTE is neuropathologically defined by the perivascular accumulation of abnormally phosphorylated tau protein in the depths of the ... ...

    Abstract Chronic traumatic encephalopathy (CTE) is a distinct neurodegenerative disease that associated with repetitive head trauma. CTE is neuropathologically defined by the perivascular accumulation of abnormally phosphorylated tau protein in the depths of the sulci in the cerebral cortices. In advanced CTE, hyperphosphorylated tau protein deposits are found in widespread regions of brain, however the mechanisms of the progressive neurodegeneration in CTE are not fully understood. In order to identify which proteomic signatures are associated with CTE, we prepared RIPA-soluble fractions and performed quantitative proteomic analysis of postmortem brain tissue from individuals neuropathologically diagnosed with CTE. We found that axonal guidance signaling pathwayrelated proteins were most significantly decreased in CTE. Immunohistochemistry and Western blot analysis showed that axonal signaling pathway-related proteins were down regulated in neurons and oligodendrocytes and neuron-specific cytoskeletal proteins such as TUBB3 and CFL1 were reduced in the neuropils and cell body in CTE. Moreover, oligodendrocyte-specific proteins such as MAG and TUBB4 were decreased in the neuropils in both gray matter and white matter in CTE, which correlated with the degree of axonal injury and degeneration. Our findings indicate that deregulation of axonal guidance proteins in neurons and oligodendrocytes is associated with the neuropathology in CTE. Together, altered axonal guidance proteins may be potential pathological markers for CTE.
    Language English
    Publishing date 2019-06-26
    Publishing country Korea (South)
    Document type Journal Article
    ZDB-ID 2639017-6
    ISSN 2093-8144 ; 1226-2560
    ISSN (online) 2093-8144
    ISSN 1226-2560
    DOI 10.5607/en.2019.28.3.362
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: Label-free quantitative proteomics unravels the importance of RNA processing in glioma malignancy.

    Bi, Baibin / Li, Feng / Guo, Jisheng / Li, Cuiling / Jing, Ruirui / Lv, Xin / Chen, Xinjun / Wang, Fengqin / Azadzoi, Kazem M / Wang, Lin / Liu, Yuguang / Yang, Jing-Hua

    Neuroscience

    2017  Volume 351, Page(s) 84–95

    Abstract: Glioma, one of the most common cancers in human, is classified to different grades according to the degrees of malignancy. Glioblastoma (GBM) is known to be the most malignant (Grade IV) whereas low-grade astrocytoma (LGA, Grade II) is relatively benign. ...

    Abstract Glioma, one of the most common cancers in human, is classified to different grades according to the degrees of malignancy. Glioblastoma (GBM) is known to be the most malignant (Grade IV) whereas low-grade astrocytoma (LGA, Grade II) is relatively benign. The mechanism underlying the pathogenesis and progression of glioma malignancy remains unclear. Here we report a quantitative proteomic study to elucidate the differences between GBM and LGA using liquid chromatography and tandem mass spectrometry followed by label-free quantification. A total of 136 proteins were differentially expressed in GBM for at least five folds in comparison with LGA. Ontological analysis revealed a close correlation between GBM-associated proteins and RNA processing. Interaction network analysis indicated that the GBM-associated proteins in the RNA processing were linked to crucial signaling transduction modulators including epidermal growth factor receptor (EGFR), signal transducer and activator of transcription 1 (STAT1), and mitogen-activated protein kinase 1 (MAPK1), which were further connected to the proteins important for neuronal structural integrity, development and functions. Upregulation of 40S ribosomal protein S5 (RPS5), Ferritin Heavy chain (FTH1) and STAT1, and downregulation of tenascin R (TNR) were validated as representatives by immune assays. In summary, we revealed a panel of GBM-associated proteins and the important modulators centered at the RNA-processing network in glioma malignancy that may become novel biomarkers and help elucidate the underlying mechanism.
    MeSH term(s) Adult ; Astrocytoma/genetics ; Astrocytoma/metabolism ; Brain Neoplasms/genetics ; Brain Neoplasms/metabolism ; Cell Line, Tumor ; Female ; Gene Expression Regulation, Neoplastic ; Glioblastoma/genetics ; Glioblastoma/metabolism ; Glioma/genetics ; Glioma/pathology ; Humans ; Male ; Middle Aged ; Proteomics/methods ; RNA/genetics ; Signal Transduction/genetics
    Chemical Substances RNA (63231-63-0)
    Language English
    Publishing date 2017-03-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 196739-3
    ISSN 1873-7544 ; 0306-4522
    ISSN (online) 1873-7544
    ISSN 0306-4522
    DOI 10.1016/j.neuroscience.2017.03.023
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Yersinia pestis acetyltransferase-mediated dual acetylation at the serine and lysine residues enhances the auto-ubiquitination of ubiquitin ligase MARCH8 in human cells.

    Li, Cuiling / Wang, Daoguang / Lv, Xin / Jing, Ruirui / Bi, Baibin / Chen, Xinjun / Guo, Jisheng / Wang, Fengqin / Sun, Shengnan / Azadzoi, Kazem M / Yang, Jing-Hua

    Cell cycle (Georgetown, Tex.)

    2017  Volume 16, Issue 7, Page(s) 649–659

    Abstract: Lysine acetylation is known as a post translational modification (PTM) by histone acetyltransferases (HAT) that modifies histones and non-histone proteins to regulate gene expression. Serine acetylation, however, is reported in mammalian hosts by serine ... ...

    Abstract Lysine acetylation is known as a post translational modification (PTM) by histone acetyltransferases (HAT) that modifies histones and non-histone proteins to regulate gene expression. Serine acetylation, however, is reported in mammalian hosts by serine acetyltransferase of Yersinia pestis (YopJ) during infection. The protein target and cellular function of bacterial YopJ in mammalian systems are not fully addressed. Here we report dual acetylation at the serine and lysine residues by transiently expressed serine acetyltransferase YopJ mimicking Y. pestis infection in HeLa cells. Using shotgun proteomics followed by label-free quantification, we demonstrate an increase of dual acetylation in YopJ transfected human cells, including 10 Ser- (YopJ/non-YopJ 1.3-fold, p = 0.02) and 8 Lys- (YopJ/non-YopJ 3.5-fold, p = 0.00003) acetylation sites. Specifically, YopJ expression augments acetylation of membrane-associated E3 ubiquitin ligase MARCH8 at the serine residue Sac44, Sac71 and Sac253, and the lysine residue Kac247 and Kac252. YopJ-mediated Ser- and Lys-acetylation of MARCH8 is further confirmed by Western blotting using the specific antibodies against MARCH8 Sac71 and pan-acetyl lysine. Functional study demonstrates that YopJ-mediated Ser- and Lys-acetylation affects the auto-ubiquitination of MARCH8. The mutant C172A of YopJ previously shown to abolish the acetyltransferase activity also reduces Ser- and Lys-acetylation and diminishes the auto-ubiquitination of MARCH8. In support, MARCH8 is indeed acetylated at serine and lysine in vitro by purified YopJ but the activity is reduced by the C172A mutant in YopJ. Our study provides evidence that bacterial serine acetyltransferase YopJ mediates Ser- and Lys-acetylation and affects auto-ubiquitination of ubiquitin ligase MARCH8 in human cells.
    MeSH term(s) Acetylation ; Amino Acid Sequence ; Bacterial Proteins/metabolism ; Biocatalysis ; HeLa Cells ; Histone Acetyltransferases/metabolism ; Humans ; Immunoassay ; Lysine/metabolism ; Peptides/chemistry ; Peptides/metabolism ; Reproducibility of Results ; Serine/metabolism ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Yersinia pestis
    Chemical Substances Bacterial Proteins ; Peptides ; Serine (452VLY9402) ; Histone Acetyltransferases (EC 2.3.1.48) ; MARCHF8 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2017-01-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.1080/15384101.2017.1281481
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article ; Online: MiR-7-5p is frequently downregulated in glioblastoma microvasculature and inhibits vascular endothelial cell proliferation by targeting RAF1.

    Liu, Zhiguo / Liu, Yuguang / Li, Lianling / Xu, Zhenkuan / Bi, Baibin / Wang, Yunyan / Li, Jian Yi

    Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine

    2014  Volume 35, Issue 10, Page(s) 10177–10184

    Abstract: The aberrant expression of microRNAs (miRNAs) is always associated with tumor development and progression. Microvascular proliferation is one of the unique pathologic features of glioblastoma (GBM) . In this study, the microvasculature from GBM or normal ...

    Abstract The aberrant expression of microRNAs (miRNAs) is always associated with tumor development and progression. Microvascular proliferation is one of the unique pathologic features of glioblastoma (GBM) . In this study, the microvasculature from GBM or normal brain tissue derived from neurosurgeries was purified and total RNA was isolated from purified microvasculature. The difference of miRNA expression profiles between glioblastoma microvasculature and normal brain capillaries was investigated. It was found that miR-7-5p in GBM microvessels was significantly reduced compared with that in normal brain capillaries. In the in vitro experiments, overexpression of miR-7-5p significantly inhibited human umbilical vein endothelial cell proliferation. Forced expression of miR-7-5p in human umbilical vein endothelial cells in vitro significantly reduced the protein level of RAF1 and repressed the activity of the luciferase, a reporter vector carrying the 3'-untranslated region of RAF1. These findings indicate that RAF1 is one of the miR-7-5p target genes. Furthermore, a significant inverse correlation between miR-7-5p expression and RAF1 protein level in GBM microvasculature was found. These data suggest that miR-7-5p functions as a tumor suppressor gene to regulate GBM microvascular endothelial cell proliferation potentially by targeting the RAF1 oncogene, implicating an important role for miR-7-5p in the pathogenesis of GBM. It may serve as a guide for the antitumor angiogenesis drug development.
    MeSH term(s) Adult ; Aged ; Brain Neoplasms/blood supply ; Brain Neoplasms/genetics ; Brain Neoplasms/pathology ; Cell Proliferation ; Down-Regulation ; Endothelial Cells/metabolism ; Endothelial Cells/pathology ; Female ; Gene Expression Regulation, Neoplastic/genetics ; Genes, Tumor Suppressor ; Glioblastoma/blood supply ; Glioblastoma/genetics ; Glioblastoma/pathology ; Humans ; Male ; MicroRNAs/genetics ; Microvessels/metabolism ; Microvessels/pathology ; Middle Aged ; Oligonucleotide Array Sequence Analysis ; Proto-Oncogene Proteins c-raf/genetics ; Proto-Oncogene Proteins c-raf/metabolism ; Real-Time Polymerase Chain Reaction ; Transcriptome
    Chemical Substances MIRN7 microRNA, human ; MicroRNAs ; Proto-Oncogene Proteins c-raf (EC 2.7.11.1)
    Language English
    Publishing date 2014-07-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 605825-5
    ISSN 1423-0380 ; 0289-5447 ; 1010-4283
    ISSN (online) 1423-0380
    ISSN 0289-5447 ; 1010-4283
    DOI 10.1007/s13277-014-2318-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article ; Online: Unraveling molecular effects of ADAR1 overexpression in HEK293T cells by label-free quantitative proteomics.

    Guo, Jisheng / Wang, Xiaoyue / Lü, Xin / Jing, Ruirui / Li, Junqiang / Li, CuiLing / Wang, Daoguang / Bi, Baibin / Chen, Xinjun / Wang, Fengqin / Sun, Shengnan / Gong, Jing / Azadzoi, Kazem M / Yang, Jing-Hua

    Cell cycle (Georgetown, Tex.)

    2016  Volume 15, Issue 12, Page(s) 1591–1601

    Abstract: ADAR1 is a double-stranded RNA (dsRNA) editing enzyme that specifically converts adenosine to inosine. ADAR1 is ubiquitously expressed in eukaryotes and participate in various cellular processes such as differentiation, proliferation and immune responses. ...

    Abstract ADAR1 is a double-stranded RNA (dsRNA) editing enzyme that specifically converts adenosine to inosine. ADAR1 is ubiquitously expressed in eukaryotes and participate in various cellular processes such as differentiation, proliferation and immune responses. We report here a new proteomics study of HEK293T cells with and without ADAR1 overexpression. The up- and down-regulated proteins by ADAR1 overexpression are identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by label-free protein quantification. Totally 1,495 proteins (FDR < 0.01) are identified, among which 211 are up- and 159 are down-regulated for at least 1.5-fold (n = 3, p < 0.05). Gene ontology analysis reveals that these ADAR1-regulated proteins are involved in protein translation and cell cycle regulation. Bioinformatics analysis identifies a closely related network consistent for the protein translation machinery and a tightly connected network through proliferating cell nuclear antigen (PCNA)-interactions. Up-regulation of the proteins in the PCNA-mediated cell proliferation network is confirmed by Western blotting. In addition, ADAR1 overexpression is confirmed to increase cell proliferation in HEK293T cells and A549 cells. We conclude that ADAR1 overexpression modulates the protein translation and cell cycle networks through PCNA-mediated protein-protein interaction to promote cell proliferation in HEK293 cells.
    MeSH term(s) Adenosine Deaminase/genetics ; Adenosine Deaminase/metabolism ; Base Sequence ; Cell Cycle/genetics ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/metabolism ; Gene Expression Regulation ; Gene Ontology ; Gene Regulatory Networks ; HEK293 Cells ; Humans ; Karyopherins/genetics ; Karyopherins/metabolism ; Ku Autoantigen/genetics ; Ku Autoantigen/metabolism ; Molecular Sequence Annotation ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Proliferating Cell Nuclear Antigen/genetics ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Interaction Mapping ; Proteomics/methods ; RNA Splicing Factors/genetics ; RNA Splicing Factors/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Signal Transduction
    Chemical Substances Karyopherins ; Nuclear Proteins ; Proliferating Cell Nuclear Antigen ; RNA Splicing Factors ; RNA-Binding Proteins ; XPO5 protein, human ; ADAR protein, human (EC 3.5.4.37) ; Adenosine Deaminase (EC 3.5.4.4) ; XRCC5 protein, human (EC 3.6.4.12) ; Ku Autoantigen (EC 4.2.99.-) ; DNA Repair Enzymes (EC 6.5.1.-) ; PRPF19 protein, human (EC 6.5.1.-)
    Language English
    Publishing date 2016-04-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.1080/15384101.2016.1176657
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top