Recruitment and retention: factors that affect pericyte migration

Cell Mol Life Sci. 2014 Jan;71(2):299-309. doi: 10.1007/s00018-013-1432-z. Epub 2013 Aug 4.

Abstract

Pericytes are critical for vascular morphogenesis and contribute to several pathologies, including cancer development and progression. The mechanisms governing pericyte migration and differentiation are complex and have not been fully established. Current literature suggests that platelet-derived growth factor/platelet-derived growth factor receptor-β, sphingosine 1-phosphate/endothelial differentiation gene-1, angiopoietin-1/tyrosine kinase with immunoglobulin-like and EGF-like domains 2, angiopoietin-2/tyrosine kinase with immunoglobulin-like and EGF-like domains 2, transforming growth factor β/activin receptor-like kinase 1, transforming growth factor β/activin receptor-like kinase 5, Semaphorin-3A/Neuropilin, and matrix metalloproteinase activity regulate the recruitment of pericytes to nascent vessels. Interestingly, many of these pathways are directly affected by secreted protein acidic and rich in cysteine (SPARC). Here, we summarize the function of these factors in pericyte migration and discuss if and how SPARC might influence these activities and thus provide an additional layer of control for the recruitment of vascular support cells. Additionally, the consequences of targeted inhibition of pericytes in tumors and the current understanding of pericyte recruitment in pathological environments are discussed.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Movement
  • Humans
  • Intercellular Signaling Peptides and Proteins / metabolism
  • Metalloendopeptidases / metabolism
  • Myocytes, Smooth Muscle / cytology
  • Myocytes, Smooth Muscle / metabolism
  • Neovascularization, Physiologic
  • Osteonectin / metabolism
  • Pericytes / cytology
  • Pericytes / metabolism*
  • Protein Kinases / metabolism
  • Signal Transduction
  • Vesicular Transport Proteins / metabolism

Substances

  • Intercellular Signaling Peptides and Proteins
  • Osteonectin
  • SPARC protein, human
  • Vesicular Transport Proteins
  • Protein Kinases
  • Metalloendopeptidases