Investigation of the effects of cephalosporin antibiotics on glutathione S-transferase activity in different tissues of rats in vivo conditions in order to drug development research

Abstract

Glutathione S-transferases are multifunctional enzymes for the cellular defense against xenobiotics and provide protection for organism. In this study, the inhibition effects of some antibiotics were investigated against GST obtained from albino-rats kidney, liver, and heart tissues. Ninety-six albino-rats were randomly divided into 16 groups (n:6). The first four groups were control groups that were administrated blank enjection and decapitated at 1-7 h. The other groups were administrated the antibiotics. In all tissues, GST activity was increased in antibiotics groups at 1st and 3rd hours compared to control groups, while it began to fall at 5th and 7th hours (p < .05). In kidney tissues, it was lower than the same control group the cefuroxime and cefoperazone groups at 7th hours (p < .05). In addition, almost all antibiotic groups of kidney tissues had higher GST activity at all hours than those of control groups, but it was higher only at 5th hours in heart tissues (p < .05).

Tannic acid as a natural antioxidant compound: Discovery of a potent metabolic enzyme inhibitor for a new therapeutic approach in diabetes and Alzheimer's disease

“…Indeed, the important role of cholinesterase enzymes in neural transmission makes them the primary target of a large number of cholinesterase-inhibiting toxins and drugs, which are beneficial for agriculture and new drugs that need to be prepared, although there is less interest in the new toxins like tacrine, donepezil, rivastigmine, and galantamine, four cholinesterase inhibitor molecules that are recorded for the therapy of AD. [44][45][46][47][48] Indeed, the galantamine molecule is an allosterically potentiating ligand of nicotinic ACh receptors. By making the remaining nicotinic ACh receptors more sensitive to ACh, this drug may induce a stronger response.…”

“…Based on the anticholinergic system, acetylcholinesterase inhibitor compounds have been developed to enhance or sustain the acetylcholine levels. Indeed, the important role of cholinesterase enzymes in neural transmission makes them the primary target of a large number of cholinesterase‐inhibiting toxins and drugs, which are beneficial for agriculture and new drugs that need to be prepared, although there is less interest in the new toxins like tacrine, donepezil, rivastigmine, and galantamine, four cholinesterase inhibitor molecules that are recorded for the therapy of AD . Indeed, the galantamine molecule is an allosterically potentiating ligand of nicotinic ACh receptors.…”

Broad-Spectrum Antibiotic Use and Disease Progression in Early-Stage Melanoma Patients: A Retrospective Cohort Study

“…Certain antibiotics, such as cephalosporins, sulfonamides, tetracyclines, and fluoroquinolones, have been shown to possess antineoplastic properties [29]. Cephalosporins increased the activity of the glutathione S-convertase enzyme-a detoxifying enzyme that is involved in the protection against oxidative stress and DNA damage and is the first line of defense against carcinogens-in the liver and kidney in rat models [43][44][45]. Sulfonamides arrested the division of melanoma cells at the G0 and G1 phases in mice models, inhibiting tumor growth [46].…”

In silicoandin vitroinvestigations on the protein–protein interactions of glutathione S-transferases with mitogen-activated protein kinase 8 and apoptosis signal-regulating kinase 1

“…Cytosolic glutathione S-transferase (GST) enzymes are involved in multiple cellular processes, in addition to catalysing glutathione conjugation reactions that eliminate endogenous and exogenous toxic compounds, especially electrophiles (Adler et al, 1999;G€ ulc¸in, Scozzafava, Supuran, Akıncıo glu, et al, 2016;Hayes & Pulford, 1995;Hayes et al, 2005;Taslimi et al, 2020;Temel et al, 2018). Members of the cytosolic GST family share sequence similarity among themselves and with members of the mitochondrial GST family (Gulçin et al, 2018;Nebert & Vasiliou, 2004;T€ urkan et al, 2020). Structurewise, Cytosolic GST enzymes comprise two important domains and two critical binding sites: the N-terminal thioredoxin-like domain is responsible for glutathione binding, i.e.…”