Pflügers Archiv

, Volume 429, Issue 6, pp 805–808 | Cite as

Cholecystokinin-octapeptide affects the fluorescence signal of a single pancreatic acinar cell loaded with the acrylodan-labelled MARCKS peptide, a protein kinase C substrate

  • A. Ngezahayo
  • F. Lang
  • H. -A. Kolb
Original Article Transport Processes, Metabolism and Endocrinology; Kidney, Gastrointestinal Tract, and Exocrine Glands


We used a fluorescent derivative of the myristoylated, alanine-rich C kinase substrate (MARCKS) peptide as a probe for protein kinase C (PKC) activation by cholecystokinin-octapeptide (CCK-8) in isolated pancreatic acinar cell pairs. The diffusion of the acrylodan-labelled MARCKS-peptide into the cell interior could be monitored by the increase of fluorescence in the whole-cell patch-clamp configuration. Addition of 10 pM CCK-8 to the bath induced repetitive fluctuations of the fluorescent signal in the time range of 4–5 min. With 1 nM CCK-8 a sustained decrease of the signal was observed. Addition of polymyxin B, a specific inhibitor of PKC activation, to the pipette filling solution suppressed the CCK-8-induced change of fluorescence. The data indicate activation of PKC by CCK-8 in pancreatic acinar cells and could be compared with the previously studied CCK-8-induced gap junction uncoupling.

Key words

Fluorescent MARCKS peptide Protein kinase C activation Cholecystokinin Pancreatic acinar cells Patch-clamp 


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Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • A. Ngezahayo
    • 1
  • F. Lang
    • 1
  • H. -A. Kolb
    • 1
  1. 1.University of TübingenInstitute of Physiology ITübingenGermany

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