Inhibitory effects of human and porcine alpha-amylase on CCK-8-stimulated lipase secretion of isolated rat pancreatic acini.
Previously we have demonstrated inhibitory effects of the plant lectin wheat germ agglutinin (WGA) on (125)I-CCK-8 binding to pancreatic AR42J cells as well as on CCK-8-stimulated Ca(2+) release and alpha-amylase secretion of rat pancreatic acini or acinar cells. Therefore, it is entirely conceivable that alpha-amylase having several lectin-like carbohydrate recognition domains can modulate the CCK-8 stimulated lipase secretion. Human alpha-amylase, purified from pancreatic juice by affinity chromatography to homogeneity, and commercial porcine pancreatic alpha-amylase inhibit CCK-8-stimulated lipase secretion of rat pancreatic acini in a concentration-dependent manner. Acarbose, a specific inhibitor of alpha-amylase, was without effect on CCK-8-induced cellular lipase secretion. The data presented here provide evidence for a regulatory function of alpha-amylase in CCK-8-stimulated pancreatic secretion.
Jonas
Ludwig
L
Department of Pathology, Faculty of Medicine, University of Rostock, Germany. ludwig.jonas@med.uni-rostock.de
Mikkat
Ulrike
U
Lehmann
Renate
R
Schareck
Wolfgang
W
Walzel
Hermann
H
Schröder
Werner
W
Lopp
Hilja
H
Püssa
Tönu
T
Toomik
Peeter
P
D000372:Agglutination Tests; D000595:Amino Acid Sequence; D000818:Animals; D002470:Cell Survival / Q000187:drug effects; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010189:Pancreatic Juice / Q000201:enzymology / Q000378:metabolism; D020799:Pancrelipase / Q000187:drug effects / Q000378:metabolism*; D051381:Rats; D012844:Sincalide / Q000494:pharmacology*; D013552:Swine; D000516:alpha-Amylases / Q000302:isolation & purification / Q000494:pharmacology*
D020799:Pancrelipase; D000516:alpha-Amylases; D012844:Sincalide