Interaction of nNOS with PSD-95 negatively controls regenerative repair after stroke

J Neurosci. 2014 Oct 1;34(40):13535-48. doi: 10.1523/JNEUROSCI.1305-14.2014.

Abstract

Stroke is a major public health concern. The lack of effective therapies heightens the need for new therapeutic targets. Mammalian brain has the ability to rewire itself to restore lost functionalities. Promoting regenerative repair, including neurogenesis and dendritic remodeling, may offer a new therapeutic strategy for the treatment of stroke. Here, we report that interaction of neuronal nitric oxide synthase (nNOS) with the protein postsynaptic density-95 (PSD-95) negatively controls regenerative repair after stroke in rats. Dissociating nNOS-PSD-95 coupling in neurons promotes neuronal differentiation of neural stem cells (NSCs), facilitates the migration of newborn cells into the injured area, and enhances neurite growth of newborn neurons and dendritic spine formation of mature neurons in the ischemic brain of rats. More importantly, blocking nNOS-PSD-95 binding during the recovery stage improves stroke outcome via the promotion of regenerative repair in rats. Histone deacetylase 2 in NSCs may mediate the role of nNOS-PSD-95 association. Thus, nNOS-PSD-95 can serve as a target for regenerative repair after stroke.

Keywords: HDAC2; PSD-95; nNOS; neurogenesis; stem cells; stroke.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain / pathology
  • Brain / ultrastructure
  • Cell Differentiation / physiology
  • Cells, Cultured
  • Cerebral Cortex / cytology
  • Coculture Techniques
  • Disease Models, Animal
  • Disks Large Homolog 4 Protein
  • Embryo, Mammalian
  • Glucose / deficiency
  • Histone Deacetylase 2 / genetics
  • Histone Deacetylase 2 / metabolism
  • Hypoxia / physiopathology
  • Infarction, Middle Cerebral Artery / physiopathology
  • Infarction, Middle Cerebral Artery / surgery*
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Male
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Neural Stem Cells / physiology
  • Neural Stem Cells / transplantation*
  • Neurogenesis / physiology
  • Neurons / metabolism
  • Neurons / pathology
  • Neurons / ultrastructure
  • Nitric Oxide Synthase Type I / genetics
  • Nitric Oxide Synthase Type I / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Regeneration / physiology*

Substances

  • Disks Large Homolog 4 Protein
  • Dlg4 protein, rat
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Nitric Oxide Synthase Type I
  • Hdac2 protein, rat
  • Histone Deacetylase 2
  • Glucose