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Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but...
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Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
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Targeting Insulin Receptor with a Novel Internalizing Aptamer.

Margherita Iaboni1,2, Raffaela Fontanella3, Anna Rienzo4

  • 1Department of Molecular Medicine and Medical Biotechnology, "Federico II" University of Naples, Naples, Italy.

Molecular Therapy. Nucleic Acids
|September 21, 2016
PubMed
Summary

Researchers developed a novel RNA aptamer, GL56, that targets the insulin receptor (IR). This aptamer inhibits IR signaling in cancer cells and can deliver therapeutic agents, showing promise for cancer treatment.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Nucleic acid aptamers are promising therapeutic antagonists for disease-associated proteins.
  • Systematic Evolution of Ligands by Exponential enrichment (SELEX) is a key method for aptamer selection.
  • Aptamers offer advantages over antibodies in diagnostics and therapeutics due to their size and chemical properties.

Purpose of the Study:

  • To describe a novel, nuclease-resistant RNA aptamer, GL56, that specifically recognizes the insulin receptor (IR).
  • To evaluate the potential of GL56 as an inhibitor of IR-dependent signaling and as a delivery tool for IR-expressing cancers.

Main Methods:

  • Isolation of aptamers using a cell-based SELEX method to enrich for internalizing aptamers.
  • Characterization of aptamer specificity, including discrimination between IR and insulin-like growth factor receptor 1.
  • Assessment of aptamer internalization and inhibition of IR-dependent signaling in cancer cells.

Main Results:

  • A novel RNA aptamer, GL56, was identified that specifically binds to the insulin receptor (IR).
  • GL56 demonstrates rapid internalization into target cells and distinguishes IR from the homologous IGF-1R.
  • The aptamer inhibits IR-dependent signaling in cancer cells expressing high levels of IR.

Conclusions:

  • GL56 is a potent RNA aptamer inhibitor of insulin receptor signaling.
  • GL56 exhibits potential as a therapeutic agent and delivery vehicle for IR-dependent cancers.
  • The findings highlight the translational potential of GL56 for cancer treatment strategies targeting the insulin receptor.