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  1. Article ; Online: Proteomic Analysis of Cyclic Ketamine Compounds Ability to Induce Neural Differentiation in Human Adult Mesenchymal Stem Cells.

    Santos, Jerran / Milthorpe, Bruce Kenneth / Padula, Matthew Paul

    International journal of molecular sciences

    2019  Volume 20, Issue 3

    Abstract: Neural regeneration is of great interest due to its potential to treat traumatic brain injuries and diseases that impact quality of life. Growth factor mediated differentiation can take up to several weeks to months to produce the cell of interest ... ...

    Abstract Neural regeneration is of great interest due to its potential to treat traumatic brain injuries and diseases that impact quality of life. Growth factor mediated differentiation can take up to several weeks to months to produce the cell of interest whereas chemical stimulation may be as minimal as a few hours. The smaller time scale is of great clinical relevance. Adipose derived stem cells (ADSCs) were treated for up to 24 h with a novel differentiation media containing the cyclic ketamine compounds to direct neurogenic induction. The extent of differentiation was investigated by proteome changes occurring during the process. The treatments indicated the ADSCs responded favorably to the neurogenic induction media by presenting a number of morphological cues of neuronal phenotype previously seen and a higher cell population post induction compared to previous studies. Furthermore, approximately 3500 proteins were analyzed and identified by mass spectrometric iTRAQ analyses. The bioinformatics analyses revealed hundreds of proteins whose expression level changes were statistically significant and biologically relevant to neurogenesis and annotated as being involved in neurogenic development. Complementing this, the Bioplex cytokine assay profiles present evidence of decreased panel of stress response cytokines and a relative increase in those involved in neurogenesis.
    MeSH term(s) Adipose Tissue/cytology ; Adipose Tissue/metabolism ; Cell Differentiation/drug effects ; Cells, Cultured ; Culture Media/chemistry ; Culture Media/pharmacology ; Gene Expression Regulation/drug effects ; Gene Regulatory Networks/drug effects ; Humans ; Ketamine/pharmacology ; Mass Spectrometry ; Mesenchymal Stem Cells/cytology ; Mesenchymal Stem Cells/metabolism ; Neurogenesis ; Neurons/cytology ; Neurons/drug effects ; Neurons/metabolism ; Proteomics/methods
    Chemical Substances Culture Media ; Ketamine (690G0D6V8H)
    Language English
    Publishing date 2019-01-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20030523
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Correction: Santos, J.,

    Santos, Jerran / Milthorpe, Bruce Kenneth / Padula, Matthew Paul

    International journal of molecular sciences

    2019  Volume 20, Issue 14

    Abstract: The authors wish to make the following corrections to this paper [ ... ]. ...

    Abstract The authors wish to make the following corrections to this paper [...].
    Language English
    Publishing date 2019-07-19
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20143542
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules.

    Widjaja, Michael / Berry, Iain James / Jarocki, Veronica Maria / Padula, Matthew Paul / Dumke, Roger / Djordjevic, Steven Philip

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 6384

    Abstract: Mycoplasma pneumoniae is a genome reduced pathogen and causative agent of community acquired pneumonia. The major cellular adhesin, P1, localises to the tip of the attachment organelle forming a complex with P40 and P90, two cleavage fragments derived by ...

    Abstract Mycoplasma pneumoniae is a genome reduced pathogen and causative agent of community acquired pneumonia. The major cellular adhesin, P1, localises to the tip of the attachment organelle forming a complex with P40 and P90, two cleavage fragments derived by processing Mpn142, and other molecules with adhesive and mobility functions. LC-MS/MS analysis of M. pneumoniae M129 proteins derived from whole cell lysates and eluents from affinity matrices coupled with chemically diverse host molecules identified 22 proteoforms of P1. Terminomics was used to characterise 17 cleavage events many of which were independently verified by the identification of semi-tryptic peptides in our proteome studies and by immunoblotting. One cleavage event released
    MeSH term(s) A549 Cells ; Adhesins, Bacterial/metabolism ; Bacterial Adhesion ; Blood Proteins/metabolism ; Cytoskeletal Proteins/metabolism ; Host-Pathogen Interactions ; Humans ; Mycoplasma pneumoniae/pathogenicity ; Protein Binding ; Protein Processing, Post-Translational
    Chemical Substances Adhesins, Bacterial ; Blood Proteins ; Cytoskeletal Proteins ; adhesin, Mycoplasma pneumoniae
    Language English
    Publishing date 2020-04-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-63136-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y.

    Jarocki, Veronica Maria / Raymond, Benjamin Bernard Armando / Tacchi, Jessica Leigh / Padula, Matthew Paul / Djordjevic, Steven Philip

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 14585

    Abstract: Mycoplasma hyopneumoniae is an economically-devastating and geographically-widespread pathogen that colonises ciliated epithelium, and destroys mucociliary function. M. hyopneumoniae devotes ~5% of its reduced genome to encode members of the P97 and P102 ...

    Abstract Mycoplasma hyopneumoniae is an economically-devastating and geographically-widespread pathogen that colonises ciliated epithelium, and destroys mucociliary function. M. hyopneumoniae devotes ~5% of its reduced genome to encode members of the P97 and P102 adhesin families that are critical for colonising epithelial cilia, but mechanisms to impair mucociliary clearance and manipulate host immune response to induce a chronic infectious state have remained elusive. Here we identified two surface exposed M. hyopneumoniae proteases, a putative Xaa-Pro aminopeptidase (MHJ_0659; PepP) and a putative oligoendopeptidase F (MHJ_0522; PepF), using immunofluorescence microscopy and two orthogonal proteomic methodologies. MHJ_0659 and MHJ_0522 were purified as polyhistidine fusion proteins and shown, using a novel MALDI-TOF MS assay, to degrade four pro-inflammatory peptides that regulate lung homeostasis; bradykinin (BK), substance P (SP), neurokinin A (NKA) and neuropeptide Y (NPY). These findings provide insight into the mechanisms used by M. hyopneumoniae to influence ciliary beat frequency, impair mucociliary clearance, and initiate a chronic infectious disease state in swine, features that are a hallmark of disease caused by this pathogen.
    MeSH term(s) Adhesins, Bacterial/metabolism ; Aminopeptidases/metabolism ; Animals ; Bacterial Proteins/metabolism ; Bradykinin/chemistry ; Immunity, Innate ; Metalloendopeptidases/metabolism ; Mycoplasma hyopneumoniae/enzymology ; Neurokinin A/chemistry ; Neuropeptide Y/chemistry ; Proteomics ; Substance P/chemistry ; Swine ; Trypsin/chemistry
    Chemical Substances Adhesins, Bacterial ; Bacterial Proteins ; Neuropeptide Y ; Substance P (33507-63-0) ; Neurokinin A (86933-74-6) ; Aminopeptidases (EC 3.4.11.-) ; Trypsin (EC 3.4.21.4) ; Metalloendopeptidases (EC 3.4.24.-) ; Oligoendopeptidase F (EC 3.4.24.-) ; Bradykinin (S8TIM42R2W)
    Language English
    Publishing date 2019-10-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-51116-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Elongation factor Tu is a multifunctional and processed moonlighting protein.

    Widjaja, Michael / Harvey, Kate Louise / Hagemann, Lisa / Berry, Iain James / Jarocki, Veronica Maria / Raymond, Benjamin Bernard Armando / Tacchi, Jessica Leigh / Gründel, Anne / Steele, Joel Ricky / Padula, Matthew Paul / Charles, Ian George / Dumke, Roger / Djordjevic, Steven Philip

    Scientific reports

    2017  Volume 7, Issue 1, Page(s) 11227

    Abstract: Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens ... ...

    Abstract Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens Staphylococcus aureus (Sa
    MeSH term(s) Computational Biology ; Fibrinolysin/metabolism ; Host-Pathogen Interactions ; Membrane Proteins/metabolism ; Models, Molecular ; Mycoplasma hyopneumoniae/enzymology ; Mycoplasma hyopneumoniae/genetics ; Mycoplasma pneumoniae/enzymology ; Mycoplasma pneumoniae/genetics ; Peptide Elongation Factor Tu/metabolism ; Plasminogen/metabolism ; Protein Binding ; Staphylococcus aureus/enzymology ; Staphylococcus aureus/genetics ; Virulence Factors/metabolism
    Chemical Substances Membrane Proteins ; Virulence Factors ; Plasminogen (9001-91-6) ; Fibrinolysin (EC 3.4.21.7) ; Peptide Elongation Factor Tu (EC 3.6.1.-)
    Language English
    Publishing date 2017-09-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-10644-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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