Cell polarity defines three distinct domains in pancreatic β-cells

J Cell Sci. 2017 Jan 1;130(1):143-151. doi: 10.1242/jcs.185116. Epub 2016 Feb 26.

Abstract

The structural organisation of pancreatic β-cells in the islets of Langerhans is relatively unknown. Here, using three-dimensional (3D) two-photon, 3D confocal and 3D block-face serial electron microscopy, we demonstrate a consistent in situ polarisation of β-cells and define three distinct cell surface domains. An apical domain located at the vascular apogee of β-cells, defined by the location of PAR-3 (also known as PARD3) and ZO-1 (also known as TJP1), delineates an extracellular space into which adjacent β-cells project their primary cilia. A separate lateral domain, is enriched in scribble and Dlg, and colocalises with E-cadherin and GLUT2 (also known as SLC2A2). Finally, a distinct basal domain, where the β-cells contact the islet vasculature, is enriched in synaptic scaffold proteins such as liprin. This 3D analysis of β-cells within intact islets, and the definition of distinct domains, provides new insights into understanding β-cell structure and function.

Keywords: Diabetes; Insulin; Islet; Polarity; β-Cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Blood Vessels / cytology
  • Cell Polarity*
  • Glucose Transporter Type 2 / metabolism
  • Humans
  • Insulin-Secreting Cells / cytology*
  • Insulin-Secreting Cells / metabolism
  • Insulin-Secreting Cells / ultrastructure
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Mice
  • Nerve Tissue Proteins / metabolism
  • SAP90-PSD95 Associated Proteins
  • Synapses / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Glucose Transporter Type 2
  • Intracellular Signaling Peptides and Proteins
  • Nerve Tissue Proteins
  • SAP90-PSD95 Associated Proteins
  • scribble protein, mouse