These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Binding analysis of amino-terminal and carboxyl-terminal regions of the 39-kDa protein to the low density lipoprotein receptor-related protein.
    Author: Warshawsky I, Bu G, Schwartz AL.
    Journal: J Biol Chem; 1994 Feb 04; 269(5):3325-30. PubMed ID: 7508911.
    Abstract:
    A 39-kDa protein binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP/alpha 2MR) and inhibits the binding of ligands to this receptor. We recently reported that inhibition of tissue-type plasminogen activator binding to LRP/alpha 2MR is mediated by both amino-terminal and carboxyl-terminal regions of the 39-kDa protein, whereas inhibition of alpha 2-macroglobulin-proteinase binding is mediated only by amino-terminal regions. In this report we show that amino-terminal and carboxyl-terminal regions of the 39-kDa protein bind specifically and with high affinity to LRP/alpha 2MR on rat hepatoma MH1C1 cells. Following binding, these amino-terminal and carboxyl-terminal regions of the 39-kDa protein are each rapidly endocytosed and degraded with kinetics identical to the full-length 39-kDa protein. Competition binding experiments with these constructs demonstrate that amino-terminal and carboxyl-terminal regions of the 39-kDa protein compete with one another for binding to LRP/alpha 2MR. A model is proposed in which amino-terminal and carboxyl-terminal regions of the 39-kDa protein bind to different sites on LRP/alpha 2MR in order to inhibit ligand binding.
    [Abstract] [Full Text] [Related] [New Search]