cAMP and Ca(2+)-mediated secretion in parotid acinar cells is associated with reversible changes in the organization of the cytoskeleton.
The potential involvement of actin and fodrin (brain spectrin) in secretory events has been assessed in primary cultured guinea pig parotid acinar cells, using as a tool affinity purified anti-alpha-fodrin antibody, phalloidin, and immunofluorescence techniques. In resting parotid acinar cells fodrin and actin appeared as a continuous ring under the plasma membrane of most of the cells. Upon stimulation with secretagogues fodrin and actin labeling at the level of the plasma membrane disappeared almost completely. To establish a correlation between secretion and cytoskeletal changes at the individual cell level, anti-alpha-amylase-antibodies were used to label secreted amylase exposed at the surface of secreting cells. The number of cells expressing alpha-amylase on their surface followed bulk secretion of alpha-amylase. A strict correlation between secretion and alteration of the actin-fodrin labeling was observed at the individual cell level. The cytoskeletal changes occurred in parallel with secretion independently of the secretagogue used (carbamoylcholine in the presence of Ca2+, isoproterenol in presence or absence of Ca2+, forskolin, or dibutyryl-cyclic-AMP). The changes were reversible upon removal of the secretagogue. Since Ca2+, as well as cAMP-mediated secretion, was associated with the same kind of cytoskeletal changes, a reorganization of the cytoskeleton may play an essential part in regulated secretion.
Abteilung Klinische Biochemie, Universität Göttingen, Germany.
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Perrin
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Möller
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Hanke
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Söling
D015056:1-Methyl-3-isobutylxanthine / Q000494:pharmacology; D000199:Actins / Q000032:analysis; D000818:Animals; D015415:Biomarkers; D003994:Bucladesine / Q000494:pharmacology; D002118:Calcium / Q000502:physiology*; D002122:Calcium Chloride / Q000494:pharmacology; D002217:Carbachol / Q000494:pharmacology; D002352:Carrier Proteins / Q000032:analysis; D002478:Cells, Cultured; D005576:Colforsin / Q000494:pharmacology; D000242:Cyclic AMP / Q000502:physiology*; D003599:Cytoskeleton / Q000187:drug effects / Q000502:physiology* / Q000648:ultrastructure; D004533:Egtazic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D006168:Guinea Pigs; D007545:Isoproterenol / Q000494:pharmacology; D008297:Male; D008840:Microfilament Proteins / Q000032:analysis; D010306:Parotid Gland / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D000516:alpha-Amylases / Q000032:analysis / Q000378:metabolism*; D013049:Spectrin
D015056:1-Methyl-3-isobutylxanthine; D000199:Actins; D015415:Biomarkers; D003994:Bucladesine; D002118:Calcium; D002122:Calcium Chloride; D002217:Carbachol; D002352:Carrier Proteins; D005576:Colforsin; D000242:Cyclic AMP; D004533:Egtazic Acid; D007545:Isoproterenol; D008840:Microfilament Proteins; D000516:alpha-Amylases; D013049:Spectrin; C025603:1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid