title: Calponin phosphorylation in cerebral cortex microvessels mediates sustained vasoconstriction after brain trauma.
abstract: OBJECTIVE
  The purpose of this study was to determine the molecular and biochemical changes in the contractile protein, calponin (Cp), which temporally coincide with a previously reported state of sustained contractility following traumatic brain injury (TBI).
  
  
  METHODS
  Double immunofluorescence, western analysis and two-dimensional non-equilibrium pH gradient gel electrophoresis (NEPHGE)/SDS-PAGE techniques were utilized to determine both the location and extent of Cp within smooth muscle cells (SM) and the phosphorylation state of Cp following TBI, as induced using a weight drop acceleration impact model.
  
  
  RESULTS
  Double immunofluorescence for Cp and SM indicate that following injury, Cp migrates from the cytosol to a location subjacent to the SM membrane. Western analysis revealed a significant increase in Cp protein expression following injury that was maintained up to 48 hours post-injury. Combined Western analysis and NEPHGE indicated that Cp is phosphorylated following TBI.
  
  
  CONCLUSIONS
  Cp migration and phosphorylation may underlie the mechanism for increased vasoreactivity leading to hypoperfusion following TBI.
authors.affiliation: Department of Anatomy and Cell Biology, Scott Hall, Room No. 9312, Wayne State University School of Medicine, 540 E. Canfield, Detroit, MI 48201, USA.
authors.forename: Christian W
authors.initials: CW
authors.lastname: Kreipke
authors.forename: Randy
authors.initials: R
authors.lastname: Morgan
authors.forename: George
authors.initials: G
authors.lastname: Roberts
authors.forename: Mihir
authors.initials: M
authors.lastname: Bagchi
authors.forename: José A
authors.initials: JA
authors.lastname: Rafols
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D001930:Brain Injuries / Q000473:pathology* / Q000503:physiopathology*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002540:Cerebral Cortex / Q000378:metabolism / Q000473:pathology*; D004195:Disease Models, Animal; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D008297:Male; D008833:Microcirculation / Q000378:metabolism*; D008840:Microfilament Proteins / Q000378:metabolism*; D008954:Models, Biological; D010766:Phosphorylation; D021381:Protein Transport / Q000502:physiology; D051381:Rats; D017207:Rats, Sprague-Dawley; D013997:Time Factors; D014661:Vasoconstriction / Q000502:physiology*; D000096985:Calponins
chemical_list: D000199:Actins; D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D000096985:Calponins; C498862:Acta2 protein, rat