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Positional isomerism markedly affects the growth inhibition of colon cancer cells by NOSH-aspirin: COX inhibition and modeling.

Vannini F, Chattopadhyay M, Kodela R, Rao PP, Kashfi K - Redox Biol (2015)

Bottom Line: We also analyzed the effect of these compounds on proliferation and apoptosis in HT-29 cells.The reduction of cell growth appeared to be mediated through inhibition of proliferation, and induction of apoptosis.These results suggest that the three positional isomers of NOSH-aspirin have the same biological actions, but that o-NOSH-ASA displayed the strongest anti-neoplastic potential.

View Article: PubMed Central - PubMed

Affiliation: Department of Physiology, Pharmacology and Neuroscience, Sophie Davis School of Biomedical Education, City University of New York Medical School, New York, NY 10031, United States.

No MeSH data available.


Related in: MedlinePlus

Docking of positional isomers of NOSH-ASA to the active site of cyclooxygenase-2. Hydrogen atoms are not shown for clarity. Polar and nonpolar interactions are colored coded and details are provided in text.
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f0025: Docking of positional isomers of NOSH-ASA to the active site of cyclooxygenase-2. Hydrogen atoms are not shown for clarity. Polar and nonpolar interactions are colored coded and details are provided in text.

Mentions: It should be noted that in vivo, the positional isomers of NOSH-ASA may form a number of metabolites as suggested in Fig. 5. Among them, proposed metabolites 1–5 are capable of exhibiting COX inhibition on their own. Furthermore, depending on the dose, frequency and routes of administration, a fraction of intact NOSH-aspirin derivatives can interact and inhibit the COX enzymes (Fig.6).


Positional isomerism markedly affects the growth inhibition of colon cancer cells by NOSH-aspirin: COX inhibition and modeling.

Vannini F, Chattopadhyay M, Kodela R, Rao PP, Kashfi K - Redox Biol (2015)

Docking of positional isomers of NOSH-ASA to the active site of cyclooxygenase-2. Hydrogen atoms are not shown for clarity. Polar and nonpolar interactions are colored coded and details are provided in text.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4556775&req=5

f0025: Docking of positional isomers of NOSH-ASA to the active site of cyclooxygenase-2. Hydrogen atoms are not shown for clarity. Polar and nonpolar interactions are colored coded and details are provided in text.
Mentions: It should be noted that in vivo, the positional isomers of NOSH-ASA may form a number of metabolites as suggested in Fig. 5. Among them, proposed metabolites 1–5 are capable of exhibiting COX inhibition on their own. Furthermore, depending on the dose, frequency and routes of administration, a fraction of intact NOSH-aspirin derivatives can interact and inhibit the COX enzymes (Fig.6).

Bottom Line: We also analyzed the effect of these compounds on proliferation and apoptosis in HT-29 cells.The reduction of cell growth appeared to be mediated through inhibition of proliferation, and induction of apoptosis.These results suggest that the three positional isomers of NOSH-aspirin have the same biological actions, but that o-NOSH-ASA displayed the strongest anti-neoplastic potential.

View Article: PubMed Central - PubMed

Affiliation: Department of Physiology, Pharmacology and Neuroscience, Sophie Davis School of Biomedical Education, City University of New York Medical School, New York, NY 10031, United States.

No MeSH data available.


Related in: MedlinePlus