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  1. AU="Grabauskas, Titas"
  2. AU=Sra Harnoor Kaur
  3. AU="Petra Macaskill"
  4. AU=Bramwell Edwin
  5. AU="Enríquez, Paula"
  6. AU="Uysal, Ismihan Ilknur"
  7. AU="Fernandes, Adriana Barrinha"
  8. AU="Goodwin, David G"
  9. AU="Hill, Jonathan C"
  10. AU="Chankasingh, Kyle"
  11. AU="Narayanasami, Uma"
  12. AU="Chen, Ruichao"
  13. AU=Li Xuefeng AU=Li Xuefeng
  14. AU="Stef J.F. Letteboer"
  15. AU="Gewurz, H"
  16. AU="Linares, Mauricio"
  17. AU="Gnesi, Marco"
  18. AU="Park, Jinny"
  19. AU="Hill, Benjamin D"
  20. AU=Huang Chunfa
  21. AU="Skonieczny, Paul"
  22. AU="LIVINGSTON, M S"
  23. AU="Lidia Gonzalez-Quereda"
  24. AU="Korkmaz, Asli"
  25. AU="Patel, Mrinal"
  26. AU="Louis Chauvel"
  27. AU="Jampen, Laurent"
  28. AU="Tan, Jiacheng"
  29. AU="Weiss, Jonathan D"

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  1. Artikel: Cardiovascular disease and lung cancer.

    de Jesus, Mikhail / Chanda, Anindita / Grabauskas, Titas / Kumar, Manish / Kim, Agnes S

    Frontiers in oncology

    2024  Band 14, Seite(n) 1258991

    Abstract: Lung cancer is the second most common cancer worldwide and the leading cause of cancer-related death. While survival rates have improved with advancements in cancer therapeutics, additional health challenges have surfaced. Cardiovascular disease (CVD) is ...

    Abstract Lung cancer is the second most common cancer worldwide and the leading cause of cancer-related death. While survival rates have improved with advancements in cancer therapeutics, additional health challenges have surfaced. Cardiovascular disease (CVD) is a leading cause of morbidity and mortality in patients with lung cancer. CVD and lung cancer share many risk factors, such as smoking, hypertension, diabetes, advanced age, and obesity. Optimal management of this patient population requires a full understanding of the potential cardiovascular (CV) complications of lung cancer treatment. This review outlines the common shared risk factors, the spectrum of cardiotoxicities associated with lung cancer therapeutics, and prevention and management of short- and long-term CVD in patients with non-small cell (NSCLC) and small cell (SCLC) lung cancer. Due to the medical complexity of these patients, multidisciplinary collaborative care among oncologists, cardiologists, primary care physicians, and other providers is essential.
    Sprache Englisch
    Erscheinungsdatum 2024-02-12
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2649216-7
    ISSN 2234-943X
    ISSN 2234-943X
    DOI 10.3389/fonc.2024.1258991
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: HCN as a Mediator of Urinary Homeostasis: Age-Associated Changes in Expression and Function in Adrenergic Detrusor Relaxation.

    Al-Naggar, Iman M / Hardy, Cara C / Taweh, Omar G / Grabauskas, Titas / Mulkey, Daniel K / Kuchel, George A / Smith, Phillip P

    The journals of gerontology. Series A, Biological sciences and medical sciences

    2018  Band 74, Heft 3, Seite(n) 325–329

    Abstract: The Hyperpolarization activated, cyclic nucleotide gated (HCN) channel is a candidate mediator of neuroendocrine influence over detrusor tonus during filling. In other tissues, HCN loss with aging is linked to declines in rhythmicity and function. We ... ...

    Abstract The Hyperpolarization activated, cyclic nucleotide gated (HCN) channel is a candidate mediator of neuroendocrine influence over detrusor tonus during filling. In other tissues, HCN loss with aging is linked to declines in rhythmicity and function. We hypothesized that HCN has an age-sensitive expression profile and functional role in adrenergic bladder relaxation. HCN was examined in bladders from young (2-6 months) and old (18-24 months) C57BL/6 female mice, using qRT-PCR, RNAScope, and Western blots. Isometric tension studies were conducted using bladder strips from young wild-type (YWT), old wild-type (OWT), and young HCN1 knock-out (YKO) female mice to test the role HCN in effects of β-adrenergic stimulation. Hcn1 is the dominant HCN isoform RNA in the mouse bladder wall, and is diminished with age. Location of Hcn RNA within the mouse bladder wall is isoform-specific, with HCN1 limited to the detrusor layer. Passively-tensioned YWT bladder strips are relaxed by isoproterenol in the presence of HCN function, where OWT strips are relaxed only in the presence of HCN blockade. HCN has an age-specific expression and function in adrenergic detrusor relaxation in mouse bladder strips.
    Mesh-Begriff(e) Adrenergic beta-Agonists/pharmacology ; Animals ; Female ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/metabolism ; Isoproterenol/pharmacology ; Mice ; Mice, Inbred C57BL ; Muscle Relaxation/drug effects ; Muscle Relaxation/physiology ; Muscle Tonus/drug effects ; Muscle Tonus/physiology ; Tissue Culture Techniques ; Urinary Bladder/metabolism ; Urinary Bladder/physiopathology
    Chemische Substanzen Adrenergic beta-Agonists ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; Isoproterenol (L628TT009W)
    Sprache Englisch
    Erscheinungsdatum 2018-08-20
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1223643-3
    ISSN 1758-535X ; 1079-5006
    ISSN (online) 1758-535X
    ISSN 1079-5006
    DOI 10.1093/gerona/gly137
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Soluble α-synuclein-antibody complexes activate the NLRP3 inflammasome in hiPSC-derived microglia.

    Trudler, Dorit / Nazor, Kristopher L / Eisele, Yvonne S / Grabauskas, Titas / Dolatabadi, Nima / Parker, James / Sultan, Abdullah / Zhong, Zhenyu / Goodwin, Marshall S / Levites, Yona / Golde, Todd E / Kelly, Jeffery W / Sierks, Michael R / Schork, Nicholas J / Karin, Michael / Ambasudhan, Rajesh / Lipton, Stuart A

    Proceedings of the National Academy of Sciences of the United States of America

    2021  Band 118, Heft 15

    Abstract: Parkinson's disease is characterized by accumulation of α-synuclein (αSyn). Release of oligomeric/fibrillar αSyn from damaged neurons may potentiate neuronal death in part via microglial activation. Heretofore, it remained unknown if oligomeric/fibrillar ...

    Abstract Parkinson's disease is characterized by accumulation of α-synuclein (αSyn). Release of oligomeric/fibrillar αSyn from damaged neurons may potentiate neuronal death in part via microglial activation. Heretofore, it remained unknown if oligomeric/fibrillar αSyn could activate the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family pyrin domain-containing 3 (NLRP3) inflammasome in human microglia and whether anti-αSyn antibodies could prevent this effect. Here, we show that αSyn activates the NLRP3 inflammasome in human induced pluripotent stem cell (hiPSC)-derived microglia (hiMG) via dual stimulation involving Toll-like receptor 2 (TLR2) engagement and mitochondrial damage. In vitro, hiMG can be activated by mutant (A53T) αSyn secreted from hiPSC-derived A9-dopaminergic neurons. Surprisingly, αSyn-antibody complexes enhanced rather than suppressed inflammasome-mediated interleukin-1β (IL-1β) secretion, indicating these complexes are neuroinflammatory in a human context. A further increase in inflammation was observed with addition of oligomerized amyloid-β peptide (Aβ) and its cognate antibody. In vivo, engraftment of hiMG with αSyn in humanized mouse brain resulted in caspase-1 activation and neurotoxicity, which was exacerbated by αSyn antibody. These findings may have important implications for antibody therapies aimed at depleting misfolded/aggregated proteins from the human brain, as they may paradoxically trigger inflammation in human microglia.
    Mesh-Begriff(e) Amyloid beta-Peptides/immunology ; Antibodies/immunology ; Cell Differentiation ; Cells, Cultured ; Humans ; Induced Pluripotent Stem Cells/cytology ; Inflammasomes/metabolism ; Microglia/cytology ; Microglia/immunology ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Parkinson Disease/immunology ; Toll-Like Receptor 2/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/immunology
    Chemische Substanzen Amyloid beta-Peptides ; Antibodies ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; TLR2 protein, human ; Toll-Like Receptor 2 ; alpha-Synuclein
    Sprache Englisch
    Erscheinungsdatum 2021-04-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2025847118
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 1148: Hefte anzeigen Standort:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
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