Tensin is expressed in glomerular mesangial cells and is related to their attachment to surrounding extracellular matrix

J Histochem Cytochem. 2004 May;52(5):683-91. doi: 10.1177/002215540405200512.

Abstract

Glomerular expression of tensin was immunohistochemically studied in normal and diseased rat kidneys to determine whether tensin might be related to specific binding in individual glomerular cells. Normal rat kidneys displayed an intense immunofluorescence reaction for tensin along the basal aspects of proximal and distal tubule cells and parietal epithelial cells of Bowman's capsules. In glomeruli, a positive reaction for tensin was detected only in the mesangial areas. Immunoelectron microscopy revealed a positive reaction in the mesangial cell (MC) processes. RT-PCR and immunoprecipitation demonstrated mRNA and protein levels of tensin in cultured rat MCs. Mesangial tensin expression was decreased when the mesangium was injured by Habu snake venom. During the regenerative process after mesangiolysis, tensin expression was not detected in early-phase proliferating MCs that did not have extracellular matrix (ECM). The expression of tensin recovered in late-phase proliferating MCs, which became attached to regenerated ECM. It appears that tensin is related to MC attachment to surrounding ECM, which suggests that signal transduction regulated by tensin may be related to a specific mechanism of MC matrix regeneration. Furthermore, tensin can act as a marker for rat MCs because the expression of tensin was detected only in MCs in glomeruli.

MeSH terms

  • Animals
  • Cell Adhesion
  • Cells, Cultured
  • Extracellular Matrix / physiology*
  • Glomerular Mesangium / metabolism*
  • Glomerular Mesangium / physiology
  • Immunohistochemistry
  • Microfilament Proteins / biosynthesis*
  • Microscopy, Immunoelectron
  • Nephritis / chemically induced
  • Nephritis / metabolism
  • Nephritis / pathology
  • Rats
  • Rats, Sprague-Dawley
  • Reverse Transcriptase Polymerase Chain Reaction
  • Tensins
  • Trimeresurus
  • Viper Venoms

Substances

  • Microfilament Proteins
  • Tensins
  • Tns1 protein, rat
  • Viper Venoms