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Chemical Compound Review:

Cck-jmv-180 (3S)-3-[[(1S)-2-carboxy-1...

Synonyms: AC1MHYMA, Jmv-180, Jmv 180, 119733-42-5

Schaeffer, P. et al., Asin, K.E. et al., Sato, S. et al., Stark, H.A. et al., Saluja, A.K. et al., et al.

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Disease relevance of Jmv-180

CCK-JMV-180 acts as an antagonist of the CCKA receptor in the human IMR-32 neuroblastoma cell line [1].
Coinfusion of CCK JMV-180, which abolishes pancreatitis, prevented cerulein-induced NF-kappaB activation [2].

Psychiatry related information on Jmv-180

In the present study, we examined the effects of CCK-JMV-180 on locomotor activity in the rat and on intake of a liquid diet in the rat and mouse [3].

High impact information on Jmv-180

In pancreatic acinar cells cholecystokinin and its analogs, caerulein and CCK-JMV-180, stimulate an increase in intracellular free [Ca2+] by releasing Ca2+ from non-mitochondrial intracellular pools [4].
CCK-JMV-180, an analogue of CCK-8-S which has been shown to activate 45Ca2+ efflux in rat cells in a manner similar to CCK-8-S, acted as a potent antagonist of CCK-8-S-induced 45Ca2+ efflux (IC50 = 50 nM) and inhibited [125I]CCK-8-S binding to IMR-32 cells (IC50 = 1.7 nM) [1].
CCK-JMV-180 (320 and 1000 micrograms/kg) failed to inhibit emptying when administered alone but dose dependently antagonized CCK induced inhibition of gastric emptying [5].
Differential effects of CCK-JMV-180 on food intake in rats and mice [3].
We examined the relationships between receptor occupation, calcium mobilization, and stimulated amylase release for cholecystokinin octapeptide (CCK-8) and for CCK-JMV-180, an analogue of the COOH-terminal heptapeptide of CCK having the structure Boc-Tyr(SO3)-Nle-Gly-Trp-Nle-Asp-2-phenylethyl ester using dispersed acini from rat pancreas [6].

Anatomical context of Jmv-180

In the present study, we used dispersed acini from rat pancreas to examine the effects of CCK-JMV-180, an analogue of the C-terminal heptapeptide of CCK (CCK-7) having the structure BOC-Tyr(SO3) Ahx-Gly-Trp-Ahx-Asp2 phenylethyl ester [7].

Associations of Jmv-180 with other chemical compounds

We have investigated both the production of inositol trisphosphate and changes in intracellular Ca2+ concentration in rat pancreatic acini in response to caerulein and CCK-JMV-180, two analogs of cholecystokinin [8].

Gene context of Jmv-180

Boc-Tyr(SO3)-Nle-Gly-Trp-Nle-Asp-2-phenylether ester (CCK-JMV-180) has been reported to be a CCK-based heptipeptide with novel in vitro properties [3].

References

CCK-JMV-180 acts as an antagonist of the CCKA receptor in the human IMR-32 neuroblastoma cell line. Schaeffer, P., Prabonnaud, V., Roux, M., Gully, D., Herbert, J.M. FEBS Lett. (1994) [Pubmed]
Early NF-kappaB activation is associated with hormone-induced pancreatitis. Gukovsky, I., Gukovskaya, A.S., Blinman, T.A., Zaninovic, V., Pandol, S.J. Am. J. Physiol. (1998) [Pubmed]
Differential effects of CCK-JMV-180 on food intake in rats and mice. Asin, K.E., Bednarz, L. Pharmacol. Biochem. Behav. (1992) [Pubmed]
CCK-JMV-180, an analog of cholecystokinin, releases intracellular calcium from an inositol trisphosphate-independent pool in rat pancreatic acini. Saluja, A.K., Dawra, R.K., Lerch, M.M., Steer, M.L. J. Biol. Chem. (1992) [Pubmed]
Cholecystokinin inhibits gastric emptying and contracts the pyloric sphincter in rats by interacting with low affinity CCK receptor sites. Moran, T.H., Kornbluh, R., Moore, K., Schwartz, G.J. Regul. Pept. (1994) [Pubmed]
Receptor occupation, calcium mobilization, and amylase release in pancreatic acini: effect of CCK-JMV-180. Sato, S., Stark, H.A., Martinez, J., Beaven, M.A., Jensen, R.T., Gardner, J.D. Am. J. Physiol. (1989) [Pubmed]
CCK-JMV-180: a peptide that distinguishes high-affinity cholecystokinin receptors from low-affinity cholecystokinin receptors. Stark, H.A., Sharp, C.M., Sutliff, V.E., Martinez, J., Jensen, R.T., Gardner, J.D. Biochim. Biophys. Acta (1989) [Pubmed]
Inositol trisphosphate independent increase of intracellular free calcium and amylase secretion in pancreatic acini. Saluja, A.K., Powers, R.E., Steer, M.L. Biochem. Biophys. Res. Commun. (1989) [Pubmed]

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