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Marine Fungi-Derived Secondary Metabolites: Potential as Future Drugs for Health Care
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Health Benefits of Secondary Phytocompounds from Plant and Marine Sources, 2021
Syed Shams Ul Hassan, Hui-Zi Jin, Abdur Rauf, Saud Bawazeer, Hafiz Ansar Rasul Suleria
Four diterpene glycosides (Virescenosides R1 (image 101 in Figure 8.9), Virescenosides R2 (image 102 in Figure 8.9), Virescenosides R3 (image 103 in Figure 8.9) and Virescenosides R4 (image 104 in Figure 8.9)) were isolated from the marine endophytic fungus Acremonium striatisporum that was obtained from sea cucumber holothurian Eupentacta fraudatrix. All four compounds were studied for enzymatic actions and inhibition of non-specific esterase activity in mouse lymphocytes. These compounds were applied at concentration of 100 mg/mL and these displayed inhibition of esterase activity of 56, 58, 36, and 40%, respectively [1].
Biomaterial, Host, and Microbial Interactions
Published in Mary Anne S. Melo, Designing Bioactive Polymeric Materials for Restorative Dentistry, 2020
Several bacterial species that have been identified and characterized to have esterase activities include Bacillus, Pseudomonas, Streptomyces, Enterococcus, and Streptococcus (Bourbia et al. 2013; Huang, Siqueira et al. 2018; Marashdeh et al. 2018; Sayali et al. 2013). Of interest are cariogenic bacteria, such as Streptococcus mutans. Not only has S. mutans been implicated as a major etiological agent for dental caries (Aas et al. 2008), but it has also been shown that they can hydrolyze resin composite materials and adhesives (Bourbia et al. 2013). Since cariogenic bacteria comprise a majority of the biofilm at the marginal interface (Buchmann et al. 1990), bacterial esterases are considered another contributor to the biodegradation of the resin-dentin interface and failure of the restoration (Kermanshahi et al. 2010; Huang, Siqueira et al. 2018; Spencer et al. 2010).
Histiocytosis and Lipid Storage Diseases
Published in Harold R. Schumacher, William A. Rock, Sanford A. Stass, Handbook of Hematologic Pathology, 2019
Salwa Shabbir Sheikh, David F. Garvin
Wolman’s disease is a rare disorder, clinically very similar to Niemann-Pick disease, in which death may occur in infancy. Enzyme acid esterase is severely deficient, resulting in accumulation of triglycerides and cholesterol esters in many tissues. X-rays show punctate calcification of the adrenal glands. Foam cells are seen in the bone marrow and almost any other tissue or organ. The changes in the CNS are usually confined to the endothelial cells and are not prominent in the neurons.
Design, synthesis and biological evaluation of novel N-phosphorylated and O-phosphorylated tacrine derivatives as potential drugs against Alzheimer’s disease
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2022
Maja Przybyłowska, Krystyna Dzierzbicka, Szymon Kowalski, Sebastian Demkowicz, Mateusz Daśko, Iwona Inkielewicz-Stepniak
We established profile of esterases inhibition for all of 14 synthesised compounds. We described an inhibitory potency by calculated IC50 values (Table 6). Tacrine was used as a reference compound. Both of enzyme, which we used in our investigation, AChE and BChE, come from the electric eel and equine serum respectively. However, they are commonly used instead of human enzymes because of high sequence identity 43. The most inhibitory activity against AChE had compounds 6, 8, 9 and 11–13, where derivatives 6 and 11 showed similar activity to tacrine and the rest of mentioned analogs exhibited IC50 values in the range of 6.11–16.34 nM. IC50 value calculated for a tacrine was equal to 35.12 nM and for the strongest analog 8 was 6.11 nM, what means it is almost 6 times more potent.
Complement system network in cell physiology and in human diseases
Published in International Reviews of Immunology, 2021
Roberta Romano, Giuliana Giardino, Emilia Cirillo, Rosaria Prencipe, Claudio Pignata
Hereditary deficiency of C1-esterase inhibitor is a rare disorder, affecting approximately 1 in 50–100,000 individuals [53]. Three types have been described so far: type I is caused by inadequate production of the protein, while type II is due to dysfunctional production of the enzyme (C1-INH), both caused by mutations in the SERPING1 gene, located on the chromosome 11. They are both inherited in an autosomal dominant manner, but de novo mutations have also been described. In type III, currently regarded as “unknown” hereditary angioedema, no genetic alteration has been identified [54]. This form is characterized by a later age of onset, between the second and the third decade of life and it appears to be more frequent in females, usually worsening during pregnancy. The consumption of C1-esterase inhibitor may lead to an acquired form of angioedema in the context of lymphoproliferative or autoimmune diseases [55].
Is genetic variability in carboxylesterase-1 and carboxylesterase-2 drug metabolism an important component of personalized medicine?
Published in Xenobiotica, 2020
S. Casey Laizure, Robert B Parker
Esterases are considered promiscuous enzymes with broad substrate specificity (Hatfield et al., 2016). This has been commonly interpreted to mean that carboxylesterase substrate-drugs are susceptible to hydrolysis by multiple esterases. In both the literature and in the FDA-approved labeling information it is common to refer to the metabolism of carboxylesterase-substrate drugs by “esterases” (Entresto-PPI, 2018; Plavix-PPI, 2010; Pradaxa-PPI, 2015) implying that drugs undergoing hydrolysis are susceptible to multiple enzymes. This would greatly diminish the importance of variability in enzyme activity on carboxylesterase-substrate drug disposition such as that due to genetic polymorphisms. If no single enzymatic pathway predominates, then alterations in the activity of a single enzyme would be unlikely to significantly affect drug disposition. However, with few exceptions the evidence shows that for most substrate-drugs hydrolysis occurs predominantly through a single metabolic pathway as illustrated by dimethyl fumarate hydrolysis, which is almost exclusively catalyzed by CES1.