Effect of bovine pancreatic polypeptide on basal pancreatic and biliary outputs in man

1979 ◽  
Vol 24 (1) ◽  
pp. 11-14 ◽  
Author(s):  
G. R. Greenberg ◽  
R. F. McCloy ◽  
V. S. Chadwick ◽  
T. E. Adrian ◽  
J. H. Baron ◽  
...  
1991 ◽  
Vol 156 (1) ◽  
pp. 567-582
Author(s):  
PETER BRÄUNIG

The suboesophageal ganglion of the migratory locust Locusta migratoria contains a pair of large neurosecretory cells located posteriorly, close to the sagittal plane. By means of double labelling, it is shown that the cells are immunoreactive to bovine pancreatic polypeptide. Using a combination of electrophysiological, neuroanatomical and immunocytochemical methods, it is shown that the neurones project into the corpora cardiaca with ascending anterior axons and into the lateral cardiac nerve cords with posterior axons that descend into the thoracic and abdominal nerve cord.


1987 ◽  
Vol 252 (3) ◽  
pp. G384-G391
Author(s):  
G. Z. Pan ◽  
L. Lu ◽  
J. M. Qian ◽  
B. G. Xue

In dispersed acini from rat pancreas, it was found that bovine pancreatic polypeptide (BPP) and its C-fragment hexapeptide amide (PP-6), at concentrations of 0.1 and 30 microM, respectively, could significantly inhibit amylase secretion stimulated by carbachol (P less than 0.01 or 0.05, respectively), and this inhibition by BPP was dose dependent. 45Ca outflux induced by carbachol was also inhibited by BPP or PP-6, but they had no effect on cholecystokinin octapeptide- (CCK-8) or A23187-stimulated 45Ca outflux. BPP was also capable of displacing the specific binding of [3H]quinuclidinyl benzilate to its receptors, and it possessed a higher affinity (ki 35 nM) than carbachol (Ki 1.8 microM) in binding with M-receptors. It is concluded from this study that BPP acts as an antagonist of muscarinic cholinergic receptors in rat pancreatic acini. In addition, BPP inhibited the potentiation of amylase secretion caused by the combination of carbachol plus secretin or vasoactive intestinal peptide. This may be a possible explanation of the inhibitory effect of BPP on secretin-induced pancreatic enzyme secretion shown in vivo, since pancreatic enzyme secretion stimulated by secretin under experimental conditions may be the result of potentiation of enzyme release produced by the peptide in combination with a cholinergic stimulant.


1980 ◽  
Vol 1 ◽  
pp. S79 ◽  
Author(s):  
D.S. O'Briain ◽  
Y. Dayal ◽  
A. Tischler ◽  
R.A. DeLellis ◽  
H.J. Wolfe

1985 ◽  
Vol 248 (3) ◽  
pp. G277-G280 ◽  
Author(s):  
I. L. Taylor ◽  
R. Garcia

Congenitally obese mice are hyperphagic, suggesting that their obesity is secondary to defects in normal satiety mechanisms. The present study compares the effects of caerulein, bombesin, and pancreatic polypeptide (three equimolar doses each of 3, 9, and 27 nmol/kg) on food intake in 10 pairs of lean and obese mice. After the intraperitoneal injection of saline, obese mice eat 240% more of a liquid meal (Magnacal) than their lean littermates (P less than 0.01). All three doses of caerulein significantly inhibited food intake in both obese and lean mice. Although the highest dose of bombesin significantly decreased food intake in both obese and lean mice, the lowest dose was only effective in obese mice. In contrast, none of these doses of pancreatic polypeptide had a significant effect on food intake in either lean or obese mice. A dose of bovine pancreatic polypeptide of 200 nmol/kg was required to significantly reduce food intake in lean and obese mice. This study demonstrates that obese mice respond to satiety signals and may even be more sensitive than their lean littermates to some messengers. In addition, the previously described reversal of this obesity syndrome by pancreatic polypeptide in doses of approximately 2.5 and 25 nmol X kg-1 X day-1 is unlikely to be due to effects of this peptide on food intake.


Endocrinology ◽  
1980 ◽  
Vol 106 (4) ◽  
pp. 1178-1181 ◽  
Author(s):  
STANLEY S. SCHWART ◽  
BARBARA CORKEY ◽  
JOHN R. WILLIAMSON ◽  
ARTHUR H. RUBENSTEIN

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