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  1. Article ; Online: ANGPTL3 deficiency impairs lipoprotein production and produces adaptive changes in hepatic lipid metabolism.

    Burks, Kendall H / Xie, Yan / Gildea, Michael / Jung, In-Hyuk / Mukherjee, Sandip / Lee, Paul / Pudupakkam, Upasana / Wagoner, Ryan / Patel, Ved / Santana, Katherine / Alisio, Arturo / Goldberg, Ira J / Finck, Brian N / Fisher, Edward A / Davidson, Nicholas O / Stitziel, Nathan O

    Journal of lipid research

    2024  Volume 65, Issue 2, Page(s) 100500

    Abstract: Angiopoietin-like protein 3 (ANGPTL3) is a hepatically secreted protein and therapeutic target for reducing plasma triglyceride-rich lipoproteins and low-density lipoprotein (LDL) cholesterol. Although ANGPTL3 modulates the metabolism of circulating ... ...

    Abstract Angiopoietin-like protein 3 (ANGPTL3) is a hepatically secreted protein and therapeutic target for reducing plasma triglyceride-rich lipoproteins and low-density lipoprotein (LDL) cholesterol. Although ANGPTL3 modulates the metabolism of circulating lipoproteins, its role in triglyceride-rich lipoprotein assembly and secretion remains unknown. CRISPR-associated protein 9 (CRISPR/Cas9) was used to target ANGPTL3 in HepG2 cells (ANGPTL3
    MeSH term(s) Angiopoietin-Like Protein 3 ; Angiopoietin-like Proteins/metabolism ; Apolipoprotein B-100/genetics ; Apolipoprotein B-100/metabolism ; Lipid Metabolism/genetics ; Lipoproteins/metabolism ; Liver/metabolism ; Triglycerides/metabolism
    Chemical Substances Angiopoietin-Like Protein 3 ; Angiopoietin-like Proteins ; Apolipoprotein B-100 ; Lipoproteins ; Triglycerides ; ANGPTL3 protein, human
    Language English
    Publishing date 2024-01-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80154-9
    ISSN 1539-7262 ; 0022-2275
    ISSN (online) 1539-7262
    ISSN 0022-2275
    DOI 10.1016/j.jlr.2024.100500
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 175: Show issues Location:
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  2. Article ; Online: Author Correction: SVEP1 is an endogenous ligand for the orphan receptor PEAR1.

    Elenbaas, Jared S / Pudupakkam, Upasana / Ashworth, Katrina J / Kang, Chul Joo / Patel, Ved / Santana, Katherine / Jung, In-Hyuk / Lee, Paul C / Burks, Kendall H / Amrute, Junedh M / Mecham, Robert P / Halabi, Carmen M / Alisio, Arturo / Di Paola, Jorge / Stitziel, Nathan O

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1511

    Language English
    Publishing date 2023-03-17
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-37005-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: SVEP1 is an endogenous ligand for the orphan receptor PEAR1.

    Elenbaas, Jared S / Pudupakkam, Upasana / Ashworth, Katrina J / Kang, Chul Joo / Patel, Ved / Santana, Katherine / Jung, In-Hyuk / Lee, Paul C / Burks, Kendall H / Amrute, Junedh M / Mecham, Robert P / Halabi, Carmen M / Alisio, Arturo / Di Paola, Jorge / Stitziel, Nathan O

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 850

    Abstract: Sushi, von Willebrand factor type A, EGF and pentraxin domain containing 1 (SVEP1) is an extracellular matrix protein that causally promotes vascular disease and associates with platelet reactivity in humans. Here, using a human genomic and proteomic ... ...

    Abstract Sushi, von Willebrand factor type A, EGF and pentraxin domain containing 1 (SVEP1) is an extracellular matrix protein that causally promotes vascular disease and associates with platelet reactivity in humans. Here, using a human genomic and proteomic approach, we identify a high affinity, disease-relevant, and potentially targetable interaction between SVEP1 and the orphan receptor Platelet and Endothelial Aggregation Receptor 1 (PEAR1). This interaction promotes PEAR1 phosphorylation and disease associated AKT/mTOR signaling in vascular cells and platelets. Mice lacking SVEP1 have reduced platelet activation, and exogenous SVEP1 induces PEAR1-dependent activation of platelets. SVEP1 and PEAR1 causally and concordantly relate to platelet phenotypes and cardiovascular disease in humans, as determined by Mendelian Randomization. Targeting this receptor-ligand interaction may be a viable therapeutic strategy to treat or prevent cardiovascular and thrombotic disease.
    MeSH term(s) Humans ; Animals ; Mice ; Blood Platelets/metabolism ; Ligands ; Proteomics ; Receptors, Cell Surface/metabolism ; Platelet Aggregation ; Cell Adhesion Molecules/metabolism
    Chemical Substances Ligands ; Receptors, Cell Surface ; PEAR1 protein, human ; SVEP1 protein, human ; Cell Adhesion Molecules
    Language English
    Publishing date 2023-02-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-36486-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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