CCK x Bcl-2

Last update 08 May 2025

Basic Info

Related Targets

CCKBcl-2

Drugs associated with CCK x Bcl-2

CN115385890

Patent Mining

Target

Bcl-2 x CCK

Mechanism-

Active Org.

Hangzhou Qingzhenghong Technology Co., Ltd.

Originator Org.

Hangzhou Qingzhenghong Technology Co., Ltd.

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with CCK x Bcl-2

100 Translational Medicine associated with CCK x Bcl-2

0 Patents (Medical) associated with CCK x Bcl-2

Literatures (Medical) associated with CCK x Bcl-2

01 Jul 2020·Journal of Cellular Biochemistry

Protective effect of cholecystokinin octapeptide on angiotensin II‐induced apoptosis in H9c2 cardiomyoblast cells

Article

Author: Hong, Mingyang ; Fu, Lu ; Wei, Limu ; Chen, Lin ; Yu, Huan ; Zhang, Jingqi ; Dong, Xiaoying ; Wang, Can

AbstractCholecystokinin (CCK) and its receptors are expressed in mammalian cardiomyocytes and are involved in cardiovascular system regulation; however, the exact effect and underlying mechanism of CCK in cardiomyocyte apoptosis remain to be elucidated. We examined whether sulfated CCK octapeptide (CCK‐8) protects H9c2 cardiomyoblast cells against angiotensin II (Ang II)‐induced apoptosis. The H9c2 cardiomyoblasts were subjected to Ang II with or without CCK‐8 and the viability and apoptotic rate were detected using a Cell Counting Kit‐8 assay, Hoechst 33342 staining, terminal deoxyribonucleotide transferase‐mediated nick‐end labeling assays, and flow cytometry. In addition, specific antiapoptotic mechanisms of CCK‐8 were investigated using specific CCK1 (Devazepide) or CCK2 (L365260) receptor antagonists, or the PI3K inhibitor LY294002. The expression of CCK, CCK1 receptor, CCK2 receptor, Akt, p‐Akt, Bad, p‐Bad, Bax, Bcl‐2, and caspase‐3 were detected by Western blot analysis and real‐time polymerase chain reaction. We found that CCK and its receptor messenger RNA (mRNA) and protein are expressed in H9c2 cardiomyoblasts. Ang II‐induced increased levels of CCK mRNA and protein expression and decreased levels of CCK1 receptor protein and mRNA. Pretreatment of CCK‐8 attenuated Ang II‐induced cell toxicity and apoptosis. In addition, pretreatment of H9c2 cells with CCK‐8 markedly induced expression of p‐Akt, p‐bad, and Bcl‐2 and decreased the expression levels of Bax and caspase‐3. The protective effects of CCK‐8 were partly abolished by Devazepide or LY294002. Our results suggest that CCK‐8 protects H9c2 cardiomyoblasts from Ang II‐induced apoptosis partly via activation of the CCK1 receptor and the phosphatidyqinositol‐3 kinase/protein kinase B (PI3K/Akt) signaling pathway.

01 Aug 2013·NeuropeptidesQ3 · MEDICINE

Cholecystokinin-8 induces brain-derived neurotrophic factor expression in noradrenergic neuronal cells

Q3 · MEDICINE

Article

Author: Hong Sung Chun ; Cheol Kyu T Hwang ; Do Kyung Kim

The sulfated cholecystokinin octapeptide (CCK-8S) is one of the most abundant CCK fragment in the brain, but the effects of CCK-8S on locus coeruleus (LC) noradrenergic (NA) neuronal cells activity have not been studied. In this study, we investigated the effects of CCK-8S on the expression of brain-derived neurotrophic factor (BDNF) in LC NA neuronal cell line, LC3541. Results showed that CCK-8S (10 nM) elevates BDNF levels time-dependently and by 1.82-fold after 4h of incubation. In addition, pretreatment with CCK-8S reversed H₂O₂ (100 μM)-mediated down-regulation of BDNF expression, and effectively suppressed H₂O₂-induced caspase-3 activation. Furthermore, CCK-8S markedly induced expression of neuronal survival markers, such as extracellular signal-regulated kinase 1/2 (ERK 1/2), Akt/protein kinase B (PKB), Bcl-2, and peroxisome proliferators-activated receptor gamma coactivator-1α (PGC-1α). Pharmacological inhibitors of ERK 1/2, Akt/PKB, and protein kinase A (PKA) reversed CCK-8S-mediated BDNF induction in LC3541 cells. These results suggest the first evidence that CCK-8S can protect noradrenergic neurons and enhance the expression of BDNF via ERK 1/2-Akt/PKB-PKA-dependent pathways.

01 Oct 2010·Pflügers Archiv - European Journal of PhysiologyQ4 · MEDICINE

Inhibitors of Bcl-2 protein family deplete ER Ca2+ stores in pancreatic acinar cells

Q4 · MEDICINE

Article

Author: Ferdek, Pawel ; Gerasimenko, Julia ; Pandol, Stephen J. ; Gukovskaya, Anna S. ; Fischer, Lars

Physiological stimulation of pancreatic acinar cells by cholecystokinin and acetylcholine activate a spatial-temporal pattern of cytosolic [Ca(+2)] changes that are regulated by a coordinated response of inositol 1,4,5-trisphosphate receptors (IP(3)Rs), ryanodine receptors (RyRs) and calcium-induced calcium release (CICR). For the present study, we designed experiments to determine the potential role of Bcl-2 proteins in these patterns of cytosolic [Ca(+2)] responses. We used small molecule inhibitors that disrupt the interactions between prosurvival Bcl-2 proteins (i.e. Bcl-2 and Bcl-xl) and proapoptotic Bcl-2 proteins (i.e. Bax) and fluorescence microfluorimetry techniques to measure both cytosolic [Ca(+2)] and endoplasmic reticulum [Ca(+2)]. We found that the inhibitors of Bcl-2 protein interactions caused a slow and complete release of intracellular agonist-sensitive stores of calcium. The release was attenuated by inhibitors of IP(3)Rs and RyRs and substantially reduced by strong [Ca(2+)] buffering. Inhibition of IP(3)Rs and RyRs also dramatically reduced activation of apoptosis by BH3I-2'. CICR induced by different doses of BH3I-2' in Bcl-2 overexpressing cells was markedly decreased compared with control. The results suggest that Bcl-2 proteins regulate calcium release from the intracellular stores and suggest that the spatial-temporal patterns of agonist-stimulated cytosolic [Ca(+2)] changes are regulated by differential cellular distribution of interacting pairs of prosurvival and proapoptotic Bcl-2 proteins.

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