(±)-Palmitoylcarnitine chloride, Protein kinase C (PKC) inhibitor

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Hsp90 Geminin and IDH1 represent different yet significant proteins with distinct mechanical functions. Heat shock protein 90 (Hsp90) acts as a molecular chaperone stabilizing and folding other proteins with a molecular weight of around 90 kDa. It plays an important role in maintaining cellular protein homeostasis and is expressed across various cell types. Additionally Hsp90 interacts with multiple client proteins including protein kinase C (PKC) serving as a chaperone to ensure their functional conformation. Geminin acts as a DNA replication inhibitor by preventing the re-replication of DNA during the cell cycle. It is ubiquitously expressed in proliferating cells and has implications in cell cycle regulation. IDH1 (Isocitrate dehydrogenase 1) having a mass of approximately 47 kDa catalyzes the conversion of isocitrate to alpha-ketoglutarate in the cytoplasm and is most prominently expressed in the liver among other tissues.

Biological function summary

Hsp90 chaperones stabilize numerous signaling proteins contributing to essential cellular processes such as cell growth and apoptosis. It forms a complex with co-chaperones to facilitate the folding and activation of client proteins some of which are critical oncogenes. Geminin inhibits DNA replication by binding to Cdt1 preventing it from initiating re-replication within a single cell cycle. This regulation ensures genomic integrity during cell division. IDH1 participates in cellular metabolism by contributing to the citric acid cycle and plays a role in protecting cells from oxidative damage through the production of NADPH.

Pathways

Hsp90 is integral to the signal transduction and stress response pathways interacting with proteins like protein kinase C (PKC) and steroid hormone receptors. These pathways are critical for cellular response to external stimuli and stress as well as for regulating cell cycle progression. Geminin is part of the DNA replication and cell cycle pathways; it regulates the transition between G1 and S phases in conjunction with cyclins and CDKs. IDH1 contributes to metabolic pathways including the citric acid cycle and lipid biosynthesis by regulating energy production and reducing equivalents.

Associated diseases and disorders

Aberrant Hsp90 activity links to various cancers including breast cancer due to its role in stabilizing oncogenic proteins such as mutant PKC. Targeting Hsp90 can disrupt these protein interactions and contribute to potential cancer therapies. Geminin's dysregulation can lead to unregulated DNA replication and in turn tumorigenesis as seen in certain aneuploid cancers. IDH1 mutations are associated with metabolic disorders like glioma altering the cell’s metabolic state and contributing to oncogenesis. In gliomas IDH1 mutation produces the onco-metabolite 2-hydroxyglutarate which can interfere with cellular differentiation and contribute to the disease progression.