Harnessing insulin- and leptin-induced oxidation of PTP1B for therapeutic development

Nat Commun. 2018 Jan 18;9(1):283. doi: 10.1038/s41467-017-02252-2.

Abstract

The protein tyrosine phosphatase PTP1B is a major regulator of glucose homeostasis and energy metabolism, and a validated target for therapeutic intervention in diabetes and obesity. Nevertheless, it is a challenging target for inhibitor development. Previously, we generated a recombinant antibody (scFv45) that recognizes selectively the oxidized, inactive conformation of PTP1B. Here, we provide a molecular basis for its interaction with reversibly oxidized PTP1B. Furthermore, we have identified a small molecule inhibitor that mimics the effects of scFv45. Our data provide proof-of-concept that stabilization of PTP1B in an inactive, oxidized conformation by small molecules can promote insulin and leptin signaling. This work illustrates a novel paradigm for inhibiting the signaling function of PTP1B that may be exploited for therapeutic intervention in diabetes and obesity.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Anti-Obesity Agents / chemistry*
  • Anti-Obesity Agents / metabolism
  • Benzophenanthridines / chemistry
  • Benzophenanthridines / metabolism
  • Binding Sites
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Humans
  • Hypoglycemic Agents / chemistry*
  • Hypoglycemic Agents / metabolism
  • Insulin / chemistry
  • Insulin / metabolism
  • Isoquinolines / chemistry
  • Isoquinolines / metabolism
  • Leptin / chemistry
  • Leptin / metabolism
  • Levamisole / chemistry
  • Levamisole / metabolism
  • Molecular Docking Simulation
  • Oxidation-Reduction
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / antagonists & inhibitors*
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / chemistry
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / genetics
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Single-Chain Antibodies / chemistry*
  • Single-Chain Antibodies / genetics
  • Single-Chain Antibodies / metabolism
  • Small Molecule Libraries / chemistry*
  • Small Molecule Libraries / metabolism

Substances

  • Anti-Obesity Agents
  • Benzophenanthridines
  • Enzyme Inhibitors
  • Hypoglycemic Agents
  • Insulin
  • Isoquinolines
  • Leptin
  • Recombinant Proteins
  • Single-Chain Antibodies
  • Small Molecule Libraries
  • Levamisole
  • sanguinarine
  • chelerythrine
  • PTPN1 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1