A role for muscle LIM protein (MLP) in vascular remodeling

J Mol Cell Cardiol. 2006 Apr;40(4):503-9. doi: 10.1016/j.yjmcc.2006.01.005. Epub 2006 Mar 6.

Abstract

Given the well-defined role of LIM-motif containing proteins in cytoskeletal organization, cell fate, and differentiation, we hypothesized that the regulation of LIM proteins played an integral role in vascular remodeling. We screened a compendium of cDNA microarray data from rat vascular smooth muscle cells (VSMC) for novel LIM-containing targets and identified muscle LIM protein (MLP), a gene previously thought to be only in striated muscle. Sequence analysis, RTQPCR and Western blotting reconfirmed expression of MLP in VSMC. MLP was elevated>10-fold 7 days following balloon injury in the rat carotid artery. Wire injury led to a significantly increased intima/media ratio in MLP -/- mice compared to wild-type controls (P<0.007, N=5). Fas-ligand and ceramide-induced apoptosis were significantly decreased in MLP deficient VSMC (n=6, P<0.001). Adenoviral-induced restoration of MLP significantly restored apoptotic response (N=6, P<0.001). These findings are the first to identify MLP in vascular smooth muscle and demonstrate that it plays a critical role in vascular remodeling. This is consistent with earlier findings demonstrating a role for MLP in striated muscle remodeling in response to load and stretch.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aorta / cytology
  • Aorta / metabolism
  • Apoptosis / physiology*
  • Calmodulin-Binding Proteins
  • Carotid Artery Injuries / metabolism
  • Cell Differentiation / physiology
  • Cells, Cultured
  • Cytoskeleton / physiology
  • Gene Expression Regulation / physiology*
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins / biosynthesis*
  • Membrane Proteins / genetics
  • Mice
  • Mice, Knockout
  • Microfilament Proteins
  • Muscle, Skeletal / metabolism
  • Myocytes, Smooth Muscle / cytology
  • Myocytes, Smooth Muscle / metabolism*
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction / methods
  • Vesicular Transport Proteins

Substances

  • Calmodulin-Binding Proteins
  • Intracellular Signaling Peptides and Proteins
  • Marcksl1 protein, mouse
  • Marcksl1 protein, rat
  • Membrane Proteins
  • Microfilament Proteins
  • Vesicular Transport Proteins