Pubmed-entry ::= {
  pmid 18180332,
  medent {
    em std {
      year 2008,
      month 5,
      day 2
    },
    cit {
      title {
        name "Dynamic regulation of endothelial NOS mediated by competitive
 interaction with alpha-actinin-4 and calmodulin."
      },
      authors {
        names ml {
          "Hiroi Y",
          "Guo Z",
          "Li Y",
          "Beggs AH",
          "Liao JK"
        },
        affil str "Vascular Medicine Research, Brigham & Women's Hospital, 65
 Landsdowne Street, Boston, MA 02139, USA."
      },
      from journal {
        title {
          iso-jta "FASEB J.",
          ml-jta "FASEB J",
          issn "1530-6860",
          name "FASEB journal : official publication of the Federation of
 American Societies for Experimental Biology"
        },
        imp {
          date std {
            year 2008,
            month 5
          },
          volume "22",
          issue "5",
          pages "1450-1457",
          language "eng",
          pubstatus ppublish,
          history {
            {
              pubstatus aheadofprint,
              date std {
                year 2008,
                month 1,
                day 7
              }
            },
            {
              pubstatus pubmed,
              date std {
                year 2008,
                month 1,
                day 9,
                hour 9,
                minute 0
              }
            },
            {
              pubstatus medline,
              date std {
                year 2008,
                month 5,
                day 29,
                hour 9,
                minute 0
              }
            },
            {
              pubstatus other,
              date std {
                year 2008,
                month 1,
                day 9,
                hour 9,
                minute 0
              }
            }
          }
        }
      },
      ids {
        pii "fj.07-9309com",
        doi "10.1096/fj.07-9309com",
        pubmed 18180332,
        other {
          db "pmc",
          tag str "PMC2515824"
        },
        other {
          db "mid",
          tag str "NIHMS55924"
        }
      }
    },
    abstract "Alpha-actinins are critical components of the actin
 cytoskeleton. Here we show that alpha-actinins serve another important
 biological function by binding to and competitively inhibiting
 calcium-dependent activation of endothelial NOS (eNOS). Alpha-actinin-2 was
 found to associate with eNOS in a yeast two-hybrid screen. In vascular
 endothelial cells, which only express alpha-actinin-1 and -4, alpha-actinin-4
 interacted and colocalized with eNOS. Addition of alpha-actinin-4 directly
 inhibited eNOS recombinant protein, and overexpression of alpha-actinin-4
 inhibited eNOS activity in eNOS-transfected COS-7 cells and bovine aortic
 endothelial cells (BAECs). In contrast, knockdown of alpha-actinin-4 by siRNA
 increased eNOS activity in BAECs. The alpha-actinin-4-binding site on eNOS
 was mapped to a central region comprising the calmodulin-binding domain, and
 the eNOS-binding site on alpha-actinin-4 was mapped to the fourth
 spectrin-like rod domain, R4. Treatment of endothelial cells with a calcium
 ionophore, A23187, decreased alpha-actinin-4-eNOS interaction, leading to
 translocation of alpha-actinin-4 from plasma membrane to cytoplasm. Indeed,
 addition of calmodulin displaced alpha-actinin-4 binding to eNOS and
 increased eNOS activity. These findings indicate that eNOS activity in
 vascular endothelial cells is tonically and dynamically regulated by
 competitive interaction with alpha-actinin-4 and calmodulin.",
    mesh {
      {
        term "Actinin",
        qual {
          {
            mp TRUE,
            subh "physiology"
          }
        }
      },
      {
        term "Animals"
      },
      {
        term "Calmodulin",
        qual {
          {
            mp TRUE,
            subh "physiology"
          }
        }
      },
      {
        term "Cattle"
      },
      {
        term "Cells, Cultured"
      },
      {
        term "Endothelial Cells",
        qual {
          {
            subh "drug effects"
          },
          {
            mp TRUE,
            subh "enzymology"
          }
        }
      },
      {
        term "Humans"
      },
      {
        term "Microfilament Proteins",
        qual {
          {
            mp TRUE,
            subh "physiology"
          }
        }
      },
      {
        term "Nitric Oxide Synthase Type III",
        qual {
          {
            subh "antagonists & inhibitors"
          },
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Two-Hybrid System Techniques"
      }
    },
    substance {
      {
        type nameonly,
        name "ACTN4 protein, human"
      },
      {
        type nameonly,
        name "Calmodulin"
      },
      {
        type nameonly,
        name "Microfilament Proteins"
      },
      {
        type cas,
        cit "11003-00-2",
        name "Actinin"
      },
      {
        type ec,
        cit "1.14.13.39",
        name "Nitric Oxide Synthase Type III"
      }
    },
    idnum {
      "AR044345/AR/NIAMS NIH HHS",
      "HL052233/HL/NHLBI NIH HHS",
      "P50 NS010828-300036/NS/NINDS NIH HHS",
      "P50 NS010828-310036/NS/NINDS NIH HHS",
      "P50 NS010828-320036/NS/NINDS NIH HHS",
      "R01 AR044345-10/AR/NIAMS NIH HHS",
      "R01 AR044345-11/AR/NIAMS NIH HHS",
      "R01 DK062729-04/DK/NIDDK NIH HHS",
      "R01 DK062729-05/DK/NIDDK NIH HHS",
      "R01 HL052233-10/HL/NHLBI NIH HHS",
      "R01 HL052233-11/HL/NHLBI NIH HHS",
      "R01 HL052233-12/HL/NHLBI NIH HHS",
      "R01 HL070274-03/HL/NHLBI NIH HHS",
      "R01 HL070274-04/HL/NHLBI NIH HHS",
      "R01 HL070274-05/HL/NHLBI NIH HHS",
      "R01 HL080187-01A1/HL/NHLBI NIH HHS",
      "R01 HL080187-02/HL/NHLBI NIH HHS",
      "R01 HL080187-03/HL/NHLBI NIH HHS"
    },
    pmid 18180332,
    pub-type {
      "Journal Article",
      "Research Support, N.I.H., Extramural",
      "Research Support, Non-U.S. Gov't"
    },
    status medline
  }
}

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