Pharmacologic and genetic approaches define human pancreatic β cell mitogenic targets of DYRK1A inhibitors

JCI Insight. 2020 Jan 16;5(1):e132594. doi: 10.1172/jci.insight.132594.

Abstract

Small molecule inhibitors of dual specificity, tyrosine phosphorylation-regulated kinase 1A (DYRK1A), including harmine and others, are able to drive human β cell regeneration. While DYRK1A is certainly a target of this class, whether it is the only or the most important target is uncertain. Here, we employ a combined pharmacologic and genetic approach to refine the potential mitogenic targets of the DYRK1A inhibitor family in human islets. A combination of human β cell RNA sequencing, DYRK1A inhibitor kinome screens, pharmacologic inhibitors, and targeted silencing of candidate genes confirms that DYRK1A is a central target. Surprisingly, however, DYRK1B also proves to be an important target: silencing DYRK1A results in an increase in DYRK1B. Simultaneous silencing of both DYRK1A and DYRK1B yields greater β cell proliferation than silencing either individually. Importantly, other potential kinases, such as the CLK and the GSK3 families, are excluded as important harmine targets. Finally, we describe adenoviruses that are able to silence up to 7 targets simultaneously. Collectively, we report that inhibition of both DYRK1A and DYRK1B is required for induction of maximal rates of human β cell proliferation, and we provide clarity for future efforts in structure-based drug design for human β cell regenerative drugs.

Keywords: Beta cells; Diabetes; Endocrinology; Metabolism.

Publication types

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

MeSH terms

  • Adolescent
  • Adult
  • Aged
  • Cell Proliferation / drug effects
  • Dyrk Kinases
  • Female
  • Gene Expression
  • Glycogen Synthase Kinase 3 / genetics
  • Glycogen Synthase Kinase 3 / metabolism
  • Harmine / metabolism
  • Harmine / pharmacology
  • Humans
  • Insulin-Secreting Cells / metabolism*
  • Insulinoma
  • Male
  • Middle Aged
  • Mitogens / metabolism*
  • Phosphorylation
  • Protein Kinase Inhibitors / pharmacology*
  • Protein Serine-Threonine Kinases / drug effects*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / drug effects*
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism
  • Young Adult

Substances

  • Mitogens
  • Protein Kinase Inhibitors
  • Harmine
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Glycogen Synthase Kinase 3