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Home / Equine Research Bank / EMBO J / Fusion pore expansion in horse eosinophils is modulated by C...
The EMBO journal1998; 17(15); 4340-4345; doi: 10.1093/emboj/17.15.4340

Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms.

Abstract: Using the patch-clamp technique, we studied the role of protein phosphorylation and dephosphorylation on the exocytotic fusion of secretory granules with the plasma membrane in horse eosinophils. Phorbol 12-myristate 13-acetate (PMA) had no effect on the amplitude and dynamics of degranulation, indicating that the formation of fusion pores is insensitive to activation of protein kinase C (PKC). Fusion pore expansion, however, was accelerated approximately 2-fold by PMA, and this effect was abolished by staurosporine. Elevating intracellular Ca2+ to 1.5 microM also resulted in a 2-fold acceleration of pore expansion; this effect was not prevented by staurosporine, indicating that intracellular Ca2+ and activation of PKC accelerate fusion pore expansion via distinct mechanisms. However, fusion pores can expand fully even when PKC is inhibited. In contrast, the phosphatase inhibitor alpha-naphthylphosphate inhibits exocytotic fusion and slows fusion pore expansion. These results demonstrate that, subsequent to its formation, fusion pore expansion is under control of proteins subject to functional changes based on their phosphorylation states.
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Publication Date: 1998-08-04 PubMed ID: 9687502PubMed Central: PMC1170767DOI: 10.1093/emboj/17.15.4340Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates how fusion pore (connection points between secretory granules and plasma membrane in cells) expansion in horse eosinophils (a type of white blood cells) is influenced by protein kinase C (PKC) and calcium levels, employing two separate mechanisms.

Overview of the Research

  • The researchers made use of the patch-clamp technique to understand the impact of protein phosphorylation and dephosphorylation (the addition and removal of phosphate groups from proteins, which regulate their functions) on the exocytotic fusion (the process where secretory granules merge with the plasma membrane to release substances outside the cell) in horse eosinophils.
  • Phorbol 12-myristate 13-acetate (PMA), a compound known to activate protein kinase C (PKC), had no significant effect on the initial formation of fusion pores.

Role of PMA and Staurosporine

  • Despite having no effect on the formation of fusion pores, PMA was found to double the speed of fusion pore expansion.
  • The acceleration of fusion pore expansion by PMA was nullified by staurosporine – a potent inhibitor of protein kinases, pointing towards a reaction pathway regulated by PKC.

Influence of Intracellular Ca2+

  • Intracellular calcium ion concentration (1.5 microM) also doubled the speed of fusion pore expansion, a phenomenon unaffected by staurosporine, thus indicating two separate regulatory pathways for fusion pore expansion – one controlled by PKC and the other by intracellular calcium.

Role of Phosphatase Inhibitor

  • Alpha-naphthylphosphate, a phosphatase inhibitor used in the study, hindered exocytotic fusion and slowed down the fusion pore expansion. Phosphatase is an enzyme that removes phosphate groups from a protein.
  • This implies that the fusion pore expansion is controlled by proteins whose functionality is influenced by their phosphorylation states.

Conclusion

  • Even when PKC is inhibited, fusion pores have the ability to still expand fully, showcasing resilience in the biological system’s mechanisms.
  • The findings demonstrate two discrete mechanisms for control of fusion pore expansion in horse eosinophils, one regulated by activation of PKC and the other by intracellular Ca2+. Furthermore, proteins, based on their phosphorylation states, hold some level of control over the expansion of the fusion pore following its formation.

Cite This Article

APA
Scepek S, Coorssen JR, Lindau M. (1998). Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms. EMBO J, 17(15), 4340-4345. https://doi.org/10.1093/emboj/17.15.4340

Publication

The EMBO journal
ISSN: 0261-4189
NlmUniqueID: 8208664
Country: England
Language: English
Volume: 17
Issue: 15
Pages: 4340-4345

Researcher Affiliations

Scepek, S
  • Department of Molecular Cell Research, Max-Planck-Institute for Medical Research, Heidelberg, Germany.
Coorssen, J R
    Lindau, M

      MeSH Terms

      • Animals
      • Calcium / physiology
      • Cell Degranulation / drug effects
      • Cell Degranulation / physiology
      • Cell Membrane / drug effects
      • Cell Membrane / physiology
      • Eosinophils / drug effects
      • Eosinophils / physiology
      • Exocytosis / drug effects
      • Exocytosis / physiology
      • Guanosine 5'-O-(3-Thiotriphosphate) / antagonists & inhibitors
      • Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
      • Horses
      • Membrane Fusion / drug effects
      • Membrane Fusion / physiology
      • Naphthalenes / pharmacology
      • Organophosphorus Compounds / pharmacology
      • Patch-Clamp Techniques
      • Protein Kinase C / physiology
      • Tetradecanoylphorbol Acetate / pharmacology
      • Time Factors

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