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  1. Article ; Online: Safety of fluconazole in kidney transplant recipients for prevention of coccidioidomycosis.

    Reddy, Laya / Thompson Iii, George R / Tuznik, Natascha / Zolfaghari, Tina A / Dray, Joy Vongspanich / Ames, Janneca / Ho, Daniel / Crabtree, Scott / Fine, Jeffrey / Wilson, Machelle D / Alnimri, Muna / Cohen, Stuart H / Koff, Alan

    Medical mycology

    2024  Volume 62, Issue 3

    Abstract: Coccidioides is an endemic fungus that causes infections ranging from mild respiratory illness to life-threatening disease, and immunocompromised hosts such as solid organ transplant recipients are at higher risk for disseminated infection and mortality. ...

    Abstract Coccidioides is an endemic fungus that causes infections ranging from mild respiratory illness to life-threatening disease, and immunocompromised hosts such as solid organ transplant recipients are at higher risk for disseminated infection and mortality. Our center administers fluconazole prophylaxis to kidney transplant recipients residing in geographic areas with higher incidences of coccidioidomycosis. However, because drug-drug interactions occur between triazoles and immunosuppressants used in transplant medicine, we undertook a study to ascertain whether fluconazole prophylaxis was associated with any important safety outcomes in kidney transplant recipients. This retrospective study evaluated patients who had undergone kidney transplantation between 2016 and 2019. Data on patient demographics, transplant-related clinical information, use of fluconazole prophylaxis (200 mg daily for 6-12 months post-transplant), and patient outcomes were obtained. The primary outcome was mean estimated glomerular filtration rate (eGFR) at 12 months, comparing those who received fluconazole prophylaxis to those who did not. Secondary outcomes included mean eGFR at 3 months, 6 months, and 9 months post-transplant, patient survival, biopsy-proven graft rejection, graft loss, or a new requirement for post-transplant dialysis, all within 12 months post-transplant. The mean eGFR at 12 months was similar between both groups, with 66.4 ml/min/1.73 m² in the fluconazole prophylaxis group vs. 64.3 ml/min/1.73 m² in the non-fluconazole prophylaxis group (P = 0.55). Secondary outcomes were similar across both groups. Multivariable linear regression found no significant association between fluconazole use and graft function. Fluconazole prophylaxis for prevention of coccidioidomycosis was not associated with adverse graft outcomes in kidney transplant recipients.
    MeSH term(s) Humans ; Fluconazole/adverse effects ; Coccidioidomycosis/epidemiology ; Coccidioidomycosis/veterinary ; Antifungal Agents/adverse effects ; Kidney Transplantation/adverse effects ; Kidney Transplantation/veterinary ; Retrospective Studies ; Transplant Recipients
    Chemical Substances Fluconazole (8VZV102JFY) ; Antifungal Agents
    Language English
    Publishing date 2024-03-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 1421796-x
    ISSN 1460-2709 ; 1369-3786
    ISSN (online) 1460-2709
    ISSN 1369-3786
    DOI 10.1093/mmy/myae017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 520: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Distinct Dibasic Cleavage Specificities of Neuropeptide-Producing Cathepsin L and Cathepsin V Cysteine Proteases Compared to PC1/3 and PC2 Serine Proteases.

    Yoon, Michael C / Ames, Janneca / Mosier, Charles / Jiang, Zhenze / Podvin, Sonia / O'Donoghue, Anthony J / Hook, Vivian

    ACS chemical neuroscience

    2022  Volume 13, Issue 2, Page(s) 245–256

    Abstract: Neuropeptides, functioning as peptide neurotransmitters and hormones, are generated from proneuropeptide precursors by proteolytic processing at dibasic residue sites (i.e., KR, RK, KK, RR). The cysteine proteases cathepsin L and cathepsin V, combined ... ...

    Abstract Neuropeptides, functioning as peptide neurotransmitters and hormones, are generated from proneuropeptide precursors by proteolytic processing at dibasic residue sites (i.e., KR, RK, KK, RR). The cysteine proteases cathepsin L and cathepsin V, combined with the serine proteases proprotein convertases 1 and 2 (PC1/3 and PC2), participate in proneuropeptide processing to generate active neuropeptides. To compare the dibasic cleavage properties of these proteases, this study conducted global, unbiased substrate profiling of these processing proteases using a diverse peptide library in multiplex substrate profiling by mass spectrometry (MSP-MS) assays. MSP-MS utilizes a library of 228 14-mer peptides designed to contain all possible protease cleavage sites, including the dibasic residue sites of KR, RK, KK, and RR. The comprehensive MSP-MS analyses demonstrated that cathepsin L and cathepsin V cleave at the N-terminal side and between the dibasic residues (e.g., ↓K↓R, ↓R↓K, and K↓K), with a preference for hydrophobic residues at the P2 position of the cleavage site. In contrast, the serine proteases PC1/3 and PC2 displayed cleavage at the C-terminal side of dibasic residues of a few peptide substrates. Further analyses with a series of dipeptide-AMC and tripeptide-AMC substrates containing variant dibasic sites with hydrophobic P2 residues indicated the preferences of cathepsin L and cathepsin V to cleave between dibasic residue sites with preferences for flanking hydrophobic residues at the P2 position consisting of Leu, Trp, Phe, and Tyr. Such hydrophobic amino acids reside in numerous proneuropeptides such as pro-NPY and proenkephalin that are known to be processed by cathepsin L. Notably, cathepsin L displayed the highest specific activity that was 10-, 64-, and 1268-fold greater than cathepsin V, PC1/3, and PC2, respectively. Peptide-AMC substrates with dibasic residues confirmed that PC1/3 and P2 cleaved almost exclusively at the C-terminal side of dibasic residues. These data demonstrate distinct dibasic cleavage site properties and a broad range of proteolytic activities of cathepsin L and cathepsin V, compared to PC1/3 and PC2, which participate in producing neuropeptides for cell-cell communication.
    MeSH term(s) Amino Acid Sequence ; Cathepsin L/metabolism ; Cathepsins ; Cysteine Proteases ; Protein Processing, Post-Translational ; Serine Endopeptidases ; Serine Proteases
    Chemical Substances Cathepsins (EC 3.4.-) ; Cysteine Proteases (EC 3.4.-) ; Serine Proteases (EC 3.4.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Cathepsin L (EC 3.4.22.15)
    Language English
    Publishing date 2022-01-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 1948-7193
    ISSN (online) 1948-7193
    DOI 10.1021/acschemneuro.1c00653
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mutant Presenilin 1 Dysregulates Exosomal Proteome Cargo Produced by Human-Induced Pluripotent Stem Cell Neurons.

    Podvin, Sonia / Jones, Alexander / Liu, Qing / Aulston, Brent / Mosier, Charles / Ames, Janneca / Winston, Charisse / Lietz, Christopher B / Jiang, Zhenze / O'Donoghue, Anthony J / Ikezu, Tsuneya / Rissman, Robert A / Yuan, Shauna H / Hook, Vivian

    ACS omega

    2021  Volume 6, Issue 20, Page(s) 13033–13056

    Abstract: The accumulation and propagation of hyperphosphorylated tau (p-Tau) is a neuropathological hallmark occurring with neurodegeneration of Alzheimer's disease (AD). Extracellular vesicles, exosomes, have been shown to initiate tau propagation in the brain. ... ...

    Abstract The accumulation and propagation of hyperphosphorylated tau (p-Tau) is a neuropathological hallmark occurring with neurodegeneration of Alzheimer's disease (AD). Extracellular vesicles, exosomes, have been shown to initiate tau propagation in the brain. Notably, exosomes from human-induced pluripotent stem cell (iPSC) neurons expressing the AD familial A246E mutant form of presenilin 1 (mPS1) are capable of inducing tau deposits in the mouse brain after
    Language English
    Publishing date 2021-05-13
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.1c00660
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Dysregulation of Exosome Cargo by Mutant Tau Expressed in Human-induced Pluripotent Stem Cell (iPSC) Neurons Revealed by Proteomics Analyses.

    Podvin, Sonia / Jones, Alexander / Liu, Qing / Aulston, Brent / Ransom, Linnea / Ames, Janneca / Shen, Gloria / Lietz, Christopher B / Jiang, Zhenze / O'Donoghue, Anthony J / Winston, Charisse / Ikezu, Tsuneya / Rissman, Robert A / Yuan, Shauna / Hook, Vivian

    Molecular & cellular proteomics : MCP

    2020  Volume 19, Issue 6, Page(s) 1017–1034

    Abstract: Accumulation and propagation of hyperphosphorylated Tau (p-Tau) is a common neuropathological hallmark associated with neurodegeneration of Alzheimer's disease (AD), frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), and related ... ...

    Abstract Accumulation and propagation of hyperphosphorylated Tau (p-Tau) is a common neuropathological hallmark associated with neurodegeneration of Alzheimer's disease (AD), frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), and related tauopathies. Extracellular vesicles, specifically exosomes, have recently been demonstrated to participate in mediating Tau propagation in brain. Exosomes produced by human induced pluripotent stem cell (iPSC)-derived neurons expressing mutant Tau (mTau), containing the P301L and V337M Tau mutations of FTDP-17, possess the ability to propagate p-Tau pathology after injection into mouse brain. To gain an understanding of the mTau exosome cargo involved in Tau pathogenesis, these pathogenic exosomes were analyzed by proteomics and bioinformatics. The data showed that mTau expression dysregulates the exosome proteome to result in 1) proteins uniquely present only in mTau, and not control exosomes, 2) the absence of proteins in mTau exosomes, uniquely present in control exosomes, and 3) shared proteins which were significantly upregulated or downregulated in mTau compared with control exosomes. Notably, mTau exosomes (not control exosomes) contain ANP32A (also known as I1PP2A), an endogenous inhibitor of the PP2A phosphatase which regulates the phosphorylation state of p-Tau. Several of the mTau exosome-specific proteins have been shown to participate in AD mechanisms involving lysosomes, inflammation, secretases, and related processes. Furthermore, the mTau exosomes lacked a substantial portion of proteins present in control exosomes involved in pathways of localization, vesicle transport, and protein binding functions. The shared proteins present in both mTau and control exosomes represented exosome functions of vesicle-mediated transport, exocytosis, and secretion processes. These data illustrate mTau as a dynamic regulator of the biogenesis of exosomes to result in acquisition, deletion, and up- or downregulation of protein cargo to result in pathogenic mTau exosomes capable of
    MeSH term(s) Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Animals ; Brain/metabolism ; Brain/pathology ; Cells, Cultured ; Chromatography, Liquid ; Computational Biology ; Exosomes/metabolism ; Exosomes/pathology ; Gene Ontology ; Humans ; Induced Pluripotent Stem Cells/metabolism ; Mutation ; Neurons/metabolism ; Neurons/pathology ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Binding ; Protein Interaction Maps ; Protein Phosphatase 2/antagonists & inhibitors ; Protein Phosphatase 2/metabolism ; Proteomics ; RNA-Binding Proteins/metabolism ; Tandem Mass Spectrometry ; tau Proteins/genetics ; tau Proteins/metabolism
    Chemical Substances ANP32A protein, human ; MAPT protein, human ; Nuclear Proteins ; RNA-Binding Proteins ; tau Proteins ; Protein Phosphatase 2 (EC 3.1.3.16)
    Language English
    Publishing date 2020-04-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1074/mcp.RA120.002079
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5599: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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