Specific, high affinity receptors for insulin-like growth factor ii in the rat kidney glomerulus

Academic Article


  • Flat renal glomeruli were isolated by a technique involving kidney perfusion with a solution containing magnetic iron oxide particles, followed by homogenization, sieving, and concentration over a strong magnet. Isolated glomeruli were treated with 1% Triton X-100 to solubilize plasma membrane components, while insoluble basement membrane components were removed by centrifugation. [125I]Insulin-like growth factor II (IGF-II) binding to this preparation was competitively inhibited by increasing amounts of unlabeled IGF-II, with 50% inhibition at an IGF-II concentration of 1 ng/ml. [125I]IGF-II was covalently cross-linked with disuccinimidyl suberate to its receptor in rat renal glomeruli and a specific high mol wt (255,000) band could be identified on autoradiograms of dodecyl sulfatepolyacrylamide gels. [125I]IGF-II binding and cross-linking to this band was inhibited by a polyclonal antibody against the type II IGF receptor. These results demonstrate for the first time that the isolated rat renal glomerulus contains a high affinity receptor for IGF-II. © 1988 by The Endocrine Society.
  • Authors

    Published In

  • Endocrinology  Journal
  • Digital Object Identifier (doi)

    Author List

  • Haskell JF; Pillion DJ; Meezan E
  • Start Page

  • 774
  • End Page

  • 780
  • Volume

  • 123
  • Issue

  • 2