Mass spectrometry identification of granins and other proteins secreted by neuroblastoma cells

Tumour Biol. 2013 Jun;34(3):1773-81. doi: 10.1007/s13277-013-0716-0. Epub 2013 Mar 22.

Abstract

We used mass spectrometry-based protein identification to determine the presence of granins and other proteins in the mouse neuroblastoma secretome. We detected polypeptides derived from four members of the granin family: chromogranin A, chromogranin B, secretogranin III, and VGF. Many of them are derived from previously described biologically active regions; however, for VGF and CgB, we detected peptides not related to known bioactivities. Along with granins, we identified 115 other proteins secreted by mouse neuroblastoma cells, belonging to different functional categories. Fifty-six out of 119 detected proteins possess the signal fragments required for translocation into endoplasmic reticulum. Sequences of remaining 63 proteins were analyzed using SecretomeP algorithm to determine probability of nonclassical secretion. Identified proteins are involved in the regulation of cell cycle, proliferation, apoptosis, angiogenesis, proteolysis, and cell adhesion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Biomarkers, Tumor / metabolism*
  • Blotting, Western
  • Cell Adhesion
  • Cell Cycle
  • Cell Movement
  • Cell Proliferation
  • Chromatography, Liquid
  • Chromogranins / metabolism*
  • Mice
  • Molecular Sequence Data
  • Neuroblastoma / metabolism*
  • Peptide Fragments / analysis*
  • Proteins / metabolism*
  • Proteome / metabolism*
  • Sequence Homology, Amino Acid
  • Tandem Mass Spectrometry*
  • Tumor Cells, Cultured

Substances

  • Biomarkers, Tumor
  • Chromogranins
  • Peptide Fragments
  • Proteins
  • Proteome