Comparative evaluation of linear and cyclic 99mTc-RGD peptides for targeting of integrins in tumor angiogenesis

Anticancer Res. 2006 Jan-Feb;26(1A):431-4.

Abstract

Cell adhesion molecules, such as integrins, play a vital role in angiogenesis, a key pathway for tumor growth, invasion and metastasis. The integrin alpha(v)beta(3), which recognizes the RGD sequence (Arg-Gly-Asp), may provide a target for in vivo tumor imaging. A linear and a cyclic RGD peptide derivative (RGDfK-His and cRGDfK-His, respectively), labelled via the precursor [99mTc(H2O)3(CO)3]+, were comparatively evaluated and their radiobiological properties were assessed in normal and tumor-bearing mice. Biodistribution studies showed non-specific uptake in all organs, rapid blood clearance and elimination via the hepatobiliary and urinary systems. Tumor uptake was higher for the cyclic radiolabelled derivative, as the both biodistribution and imaging studies suggested. The cRGDfK-His, labelled via the fac-[99mTc(CO)3]-core, may prove to be a useful tool for early tumor detection.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Breast Neoplasms / blood supply*
  • Breast Neoplasms / diagnostic imaging
  • Breast Neoplasms / metabolism*
  • Cell Line, Tumor
  • Female
  • Humans
  • Integrin alphaVbeta3 / metabolism*
  • Mice
  • Mice, Nude
  • Neovascularization, Pathologic / diagnostic imaging
  • Neovascularization, Pathologic / metabolism
  • Oligopeptides / chemistry
  • Oligopeptides / pharmacokinetics*
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / pharmacokinetics
  • Radionuclide Imaging
  • Radiopharmaceuticals / chemistry
  • Radiopharmaceuticals / pharmacokinetics*
  • Technetium Compounds / chemistry
  • Technetium Compounds / pharmacokinetics*
  • Tissue Distribution

Substances

  • Integrin alphaVbeta3
  • Oligopeptides
  • Peptides, Cyclic
  • Radiopharmaceuticals
  • Technetium Compounds
  • cyclic (arginyl-glycyl-aspartyl-phenylalanyl-lysyl)
  • arginyl-glycyl-aspartic acid