Activation of latent transforming growth factor-beta1 by nitric oxide in macrophages: role of soluble guanylate cyclase and MAP kinases.

The inducible nitric oxide (NO) synthase and the cytokine transforming growth factor-[beta]1 (TGF-[beta]1), both central modulators of wound healing, interact reciprocally: TGF-[beta]1 generally suppresses iNOS expression, while NO can induce and activate latent TGF-[beta]1. We have shown that chemi...

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Publicado en:Wound Repair & Regeneration Vol. 17; no. 4; pp. 578 - 589
Autores principales: Metukuri MR, Namas R, Gladstone C, Clermont T, Jefferson B, Barclay D, Hermus L, Billiar TR, Zamora R, Vodovotz Y
Formato: equations & formulas pictorial research tables/charts Journal Article
Publicado: Wiley-Blackwell Jul/Aug2009
Acceso en línea:Ver este registro en EBSCOhost
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      dt: Jul/Aug2009
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        10.1111/j.1524-475x.2009.00509.x
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        atl: Activation of latent transforming growth factor-beta1 by nitric oxide in macrophages: role of soluble guanylate cyclase and MAP kinases.
      aug:
        au:
          Metukuri MR
          Namas R
          Gladstone C
          Clermont T
          Jefferson B
          Barclay D
          Hermus L
          Billiar TR
          Zamora R
          Vodovotz Y
        affil: Department of Surgery, University of Pittsburgh, Pittsburgh, Pennsylvania
      sug:
        subj:
          Growth Substances Metabolism
          Macrophages Physiology
          Nitric Oxide Metabolism
          Transforming Growth Factor beta
          Blotting, Northern
          Blotting, Western
          Data Analysis Software
          Descriptive Statistics
          Fisher's Exact Test
          Funding Source
          Immunohistochemistry
          In Vitro Studies
          Mann-Whitney U Test
          One-Way Analysis of Variance
          Post Hoc Analysis
          T-Tests
          Tissue Culture Techniques
          Wound Healing Physiology
          Human
      ab: The inducible nitric oxide (NO) synthase and the cytokine transforming growth factor-[beta]1 (TGF-[beta]1), both central modulators of wound healing, interact reciprocally: TGF-[beta]1 generally suppresses iNOS expression, while NO can induce and activate latent TGF-[beta]1. We have shown that chemical NO activates recombinant human latent TGF-[beta]1 by S-nitrosation of the latency-associated peptide (LAP), a cleaved portion of pro-TGF-[beta]1 that maintains TGF-[beta]1 in a biologically-inactive state. We hypothesized that cell-associated TGF-[beta]1 could be activated by NO via known NO-inducible signaling pathways (soluble guanylate cyclase [sGC] and mitogen-activated protein [MAP] kinases). Treatment of mouse RAW 264.7 macrophage-like cells with the NO donor S-nitroso-N-acetyl-D,L-penicillamine (SNAP) led to a dose- and time-dependent increase in cell-associated active and latent TGF-[beta]1, as assessed by quantitative immunocytochemistry for active TGF-[beta]1 vs. LAP and partially validated by western blot analysis. Treatment with the sGC inhibitor 1,H-[1,2,4]oxadiazole[4,3-a]quinoxalon-1-one (ODQ) reduced both active and latent TGF-[beta]1 dose-dependently. SNAP, in the presence or absence of ODQ or the MAP kinase inhibitors, did not affect steady-state TGF-[beta]1 mRNA levels. Treatment with inhibitors specific for JNK1/2, ERK1/2, and p38 MAP kinases suppressed SNAP-induced active and latent TGF-[beta]1. Treatment with the cell-permeable cGMP analog 8-Br-cGMP increased both active and latent TGF-[beta]1. However, TGF-[beta]1 activation induced by 8-Br-cGMP was not blocked by MAP kinase inhibitors. Our findings suggest that NO activates latent TGF-[beta]1 via activation of sGC and generation of cGMP and separately via MAP kinase activation, and may shed insight into the mechanisms by which both cGMP production and MAP kinase activation enhance wound healing.
      pubtype: Academic Journal
      doctype:
        equations & formulas
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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