4.7 Article

Proteomic Profiling of Intra-Islet Features Reveals Substructure-Specific Protein Signatures

Journal

MOLECULAR & CELLULAR PROTEOMICS
Volume 21, Issue 12, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.mcpro.2022.100426

Keywords

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Funding

  1. Pfizer Worldwide Research and Development
  2. National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [5R01DK122160-03]
  3. NIH NIGMS [GM103493]
  4. U.S. Department of Energy [DE-AC05- 76RLO 1830]

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Despite their small size, islets of Langerhans play a crucial role in maintaining systemic energy balance in the body. This study uses advanced technologies to investigate the protein profiles of different features within the islet, revealing unique protein signatures in the inner vasculature that indicate increased innervation and intra-islet neuron-like crosstalk. The data also prove useful in identifying localized structure-specific drug-target interactions.
Despite their diminutive size, islets of Langerhans play a large role in maintaining systemic energy balance in the body. New technologies have enabled us to go from studying the whole pancreas to isolated whole islets, to partial islet sections, and now to islet substructures iso-lated from within the islet. Using a microfluidic nanodroplet-based proteomics platform coupled with laser capture microdissection and field asymmetric waveform ion mobility spectrometry, we present an in-depth investigation of protein profiles specific to fea-tures within the islet. These features include the islet-acinar interface vascular tissue, inner islet vasculature, isolated endocrine cells, whole islet with vasculature, and acinar tissue from around the islet. Compared to interface vasculature, unique protein signatures observed in the inner vasculature indicate increased innervation and intra-islet neuron-like crosstalk. We also demonstrate the utility of these data for identifying localized structure-specific drug-target interactions using existing protein/drug bind-ing databases.

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