Rottlerin is a lipid of Polyketides (PK) class. Rottlerin is associated with abnormalities such as PARAGANGLIOMAS 2, Hyperostosis, Diffuse Idiopathic Skeletal, Virus Diseases, Perisylvian syndrome and Autoimmune disease (systemic) NOS. The involved functions are known as Apoptosis, Regulation, Signal Transduction, inhibitors and Proteasome Inhibitors [MoA]. Rottlerin often locates in Clone, Membrane, Body tissue, Plasma membrane and soluble. The associated genes with Rottlerin are XIAP gene, GAPDH gene, ICAM1 gene, P4HTM gene and TNFSF10 gene. The related lipids are Promega, Fatty Acids, Sphingolipids, Lipopolysaccharides and Saponin. The related experimental models are Mouse Model, Xenograft Model and Cancer Model.
To understand associated biological information of rottlerin, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
rottlerin is suspected in Infection, Morphologically altered structure, Ischemia, Pulmonary Edema, Asthma, Cardiovascular Diseases and other diseases in descending order of the highest number of associated sentences.
Disease | Cross reference | Weighted score | Related literature |
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We collected disease MeSH terms mapped to the references associated with rottlerin
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
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Cancer Model are used in the study 'Rottlerin stimulates apoptosis in pancreatic cancer cells through interactions with proteins of the Bcl-2 family.' (Ohno I et al., 2010) and Cancer Model are used in the study 'Rottlerin induces Wnt co-receptor LRP6 degradation and suppresses both Wnt/β-catenin and mTORC1 signaling in prostate and breast cancer cells.' (Lu W et al., 2014).
Mouse Model are used in the study 'Neuroprotective effect of protein kinase C delta inhibitor rottlerin in cell culture and animal models of Parkinson's disease.' (Zhang D et al., 2007).
Xenograft Model are used in the study 'Rottlerin stimulates apoptosis in pancreatic cancer cells through interactions with proteins of the Bcl-2 family.' (Ohno I et al., 2010).
Model | Cross reference | Weighted score | Related literatures |
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Authors | Title | Published | Journal | PubMed Link |
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Glaser S et al. | Dopaminergic inhibition of secretin-stimulated choleresis by increased PKC-gamma expression and decrease of PKA activity. | 2003 | Am. J. Physiol. Gastrointest. Liver Physiol. | pmid:12505882 |
Li C et al. | Regulation of CCK-induced amylase release by PKC-delta in rat pancreatic acinar cells. | 2004 | Am. J. Physiol. Gastrointest. Liver Physiol. | pmid:15217780 |
Satoh K et al. | Involvement of myristoylated alanine-rich C kinase substrate phosphorylation and translocation in cholecystokinin-induced amylase release in rat pancreatic acini. | 2016 | Am. J. Physiol. Gastrointest. Liver Physiol. | pmid:26744470 |
Satoh K et al. | Phosphorylation of myristoylated alanine-rich C kinase substrate is involved in the cAMP-dependent amylase release in parotid acinar cells. | 2009 | Am. J. Physiol. Gastrointest. Liver Physiol. | pmid:19372103 |
Ohno I et al. | Rottlerin stimulates apoptosis in pancreatic cancer cells through interactions with proteins of the Bcl-2 family. | 2010 | Am. J. Physiol. Gastrointest. Liver Physiol. | pmid:19762431 |
Fryer RM et al. | Essential activation of PKC-delta in opioid-initiated cardioprotection. | 2001 | Am. J. Physiol. Heart Circ. Physiol. | pmid:11179083 |
Rao VU et al. | PKC-epsilon regulation of extracellular signal-regulated kinase: a potential role in phenylephrine-induced cardiocyte growth. | 2004 | Am. J. Physiol. Heart Circ. Physiol. | pmid:14975926 |
Cordeiro B et al. | BKCa channel activation increases cardiac contractile recovery following hypothermic ischemia/reperfusion. | 2015 | Am. J. Physiol. Heart Circ. Physiol. | pmid:26071546 |
Kato K et al. | Caspase-mediated protein kinase C-delta cleavage is necessary for apoptosis of vascular smooth muscle cells. | 2009 | Am. J. Physiol. Heart Circ. Physiol. | pmid:19837952 |
Cho CH et al. | Localization of VEGFR-2 and PLD2 in endothelial caveolae is involved in VEGF-induced phosphorylation of MEK and ERK. | 2004 | Am. J. Physiol. Heart Circ. Physiol. | pmid:14704231 |