Modulation of Gallbladder Contraction by the Oxidant Monochloramine

Author(s):  
T.S. Gaginella ◽  
C. Moummi ◽  
G.W. Gullikson
Digestion ◽  
1992 ◽  
Vol 53 (1-2) ◽  
pp. 67-71 ◽  
Author(s):  
L. Gullo ◽  
D. Ancona ◽  
R. Pezzilli ◽  
F. Fusconi ◽  
L.. Bolondi

1989 ◽  
Vol 97 (6) ◽  
pp. 1479-1484 ◽  
Author(s):  
Jose Behar ◽  
Kwang Y. Lee ◽  
William R. Thompson ◽  
Piero Biancani

1983 ◽  
pp. 152-156
Author(s):  
V. S. Chadwick ◽  
P. N. Maton ◽  
A. C. Selden

1977 ◽  
Vol 232 (5) ◽  
pp. E485
Author(s):  
S R Vigna ◽  
A Gorbman

Isometric contractions of coho salmon (Oncorhynchus kisutch) gallbladder longitudinal muscle strips were recorded in response to porcine cholecystokinin (CCK), octapeptide of CCK (OP-CCK), desulfated octapeptide of CCK (ds-OP-CCK), porcine heptadecapeptide gastrins I and II, and pentagastrin. Peak tonic contraction amplitude and peak rhythmic contraction frequency were used to construct concentration-response curves for each peptide. Observed maximal responses to each peptide were not significantly different; therefore, all peptides tested were equal in efficacy. CCK, OP-CCK, and gastrin II were equipotent, and ds-OP-CCK and gastrin I were equipotent. Conclusions: 1) porcine CCK can stimulate contraction of the coho salmon gallbladder; 2) tonic and rhythmic contractile responses are elicited in coho salmon gallbladder by agonists; 3) coho salmon gallbladder muscle cannot distinguish between agonists that differ in the location of a sulfated tyrosyl residue at position 6 versus position 7 from the C-terminus; and 4) the results of this study are consistent with the hypothesis that coho salmon gallbladder muscle contains a relatively primitive CCK receptor.


1984 ◽  
Vol 247 (1) ◽  
pp. G105-G111 ◽  
Author(s):  
T. E. Solomon ◽  
T. Yamada ◽  
J. Elashoff ◽  
J. Wood ◽  
C. Beglinger

We determined the relative molar potencies of structural analogues of porcine cholecystokinin (CCK-39, CCK-33, CCK-8, and caerulein). Peptide concentrations delivered in infusates or present in bathing medium were measured by radioimmunoassay. The presence of albumin prevented loss of CCK-39 and CCK-33 from solution to a greater degree than loss of CCK-8 and caerulein from solution. As much as 10-fold differences in CCK-33 and CCK-39 concentrations were seen in albumin-containing versus nonalbumin-containing infusates. The potency estimates calculated from radioimmunoassay-corrected concentrations with CCK-8 as standard (potency 1.00) were canine pancreatic secretion in vivo: CCK-39 4.1, CCK-33 2.2, and caerulein 2.1; rat pancreatic secretion in vivo: CCK-39 2.1, CCK-33 5.4, and caerulein 5.4; rat pancreatic secretion in vitro: CCK-33 1.7, and caerulein 1.2; guinea pig gallbladder contraction in vivo: CCK-33 1.3, and caerulein 0.9; and guinea pig gallbladder contraction in vitro: CCK-33 1.8, and caerulein 5.8. Our data indicate that CCK-8 is not more potent than longer analogues and suggest that larger forms of CCK may be important mediators of the biological actions of CCK.


2000 ◽  
Vol 94 (1-3) ◽  
pp. 9
Author(s):  
Pius Hildebrand ◽  
Lukas P. Degen ◽  
Annette Collet ◽  
Livio Rossi ◽  
Fuping Peng ◽  
...  

1990 ◽  
Vol 39 (4) ◽  
pp. 369-372 ◽  
Author(s):  
L. Marzio ◽  
F. Di Felice ◽  
V. Celiberti ◽  
O. Pieramico ◽  
L. Grossi ◽  
...  

1981 ◽  
Vol 26 (3) ◽  
pp. 214-217 ◽  
Author(s):  
Yolanda Lalyre ◽  
Donald E. Wilson ◽  
Jayashri Kidao ◽  
Calvin H. Hall ◽  
Vlastimil Capek

2003 ◽  
Vol 285 (2) ◽  
pp. G255-G265 ◽  
Author(s):  
Joseph R. Reeve ◽  
Gary M. Green ◽  
Peter Chew ◽  
Viktor E. Eysselein ◽  
David A. Keire

CCK-58 differs from CCK-8 in patterns of expression of pancreatic secretion of fluid and amylase and gallbladder contraction. These differences have physiological relevance only if CCK-58 release is stimulated by nutrients entering the intestine and if CCK-58 circulates in sizeable amounts. In this study, we report that when radiolabeled CCK-58 is added to rat blood and plasma is formed, there is extensive loss and degradation of the radioactive peptide. Therefore, a new method was developed to minimize loss and degradation of this label. This method recovered >85% of the label with no detectable degradation. Furthermore, the optimized method recovered all unlabeled exogenous cholecystokinin molecular forms in >80% yields. Blood from fasted rats and rats in which cholecystokinin release was stimulated by the trypsin inhibitor camostat contained only CCK-58 (3.5 ± 0.5 and 17 ± 1.5 fmol/ml, respectively). Because CCK-58 predominates in the blood, this molecular form should be used in studies on the physiology and pathophysiology of cholecystokinin.


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