Ultrastructural localization of cytoskeletal proteins in pancreatic secretory cells

Can J Biochem Cell Biol. 1985 Jun;63(6):680-90. doi: 10.1139/o85-085.


Actin, myosin, and keratin immunoreactive sites have been localized with high resolution in pancreatic exocrine cells, by applying the protein A-gold technique on tissues processed at low temperature conditions. The labeling by gold particles was found at the level of the cell web and closely associated with the limiting membranes of the immature and mature secretory granules, as well as those of the "trans" cisternae of the Golgi apparatus. These results, together with those obtained in the study on the localization of secretory proteins in exocrine pancreatic cells, demonstrate that cytoskeletal proteins are present at sites where maturation and (or) concentration of the secretory proteins occur. Thus, besides the role that cytoskeletal proteins must play in the transport of the secretory granules from the Golgi to the plasma membrane, they may also be involved in the process of protein maturation and (or) concentration.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / analysis
  • Animals
  • Cytoskeletal Proteins / analysis*
  • Diaphragm / ultrastructure
  • Duodenum / ultrastructure
  • Keratins / analysis
  • Microscopy, Electron
  • Muscle, Smooth / ultrastructure
  • Myosins / analysis
  • Organ Specificity
  • Pancreas / cytology
  • Pancreas / ultrastructure*
  • Rats
  • Skin / ultrastructure


  • Actins
  • Cytoskeletal Proteins
  • Keratins
  • Myosins