Effects of commonly prescribed nonsteroidal anti-inflammatory drugs on thyroid hormone measurements

Bishnoi, Alka; Carlson, Harold E.; Gruber, Barry L.; Kaufman, Lee D.; Bock, Jay L.; Lidonnici, Kenneth

doi:10.1016/0002-9343(94)90148-1

Cited by 42 publications

(28 citation statements)

References 14 publications

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“…Diclofenac competes for T 3 and T 4 binding sites in serum at the cel lsurfaces (Bishnoi et al, 1994). But in the present study, ciprofloxacin did not compete for T 3 and T 4 but it induces the gland to secrete both the hormones to maximum and was dosage dependent.…”

Section: Discussion Effect On Serum Thyrotropin and Thyroid Hormocontrasting

confidence: 75%

Ciprofloxacin induced hormonal changes in the thyroid gland of rats and Anti-oxidant vitamin A, C and E as rescue agents

Vanithakumari¹

2013

IOSR-JPBS

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Section: Discussion Effect On Serum Thyrotropin and Thyroid Hormocontrasting

confidence: 75%

Ciprofloxacin induced hormonal changes in the thyroid gland of rats and Anti-oxidant vitamin A, C and E as rescue agents

Vanithakumari¹

2013

IOSR-JPBS

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“…Furthermore, diclofenac exposure in male O. latipes fish showed that concentrations as low as 1 µg/L can increase the gene expression for VTG in the liver, thereby showing estrogenic effects (Hong et al, 2007). Furthermore, assessment of patients using diclofenac as an NSAID has shown a reduction in serum T 3 levels ( Table 2; Bishnoi et al, 1994), which is the more active thyroid hormone responsible for growth, development and metabolism in the body. The other NSAID that has also been found in South African waters, naproxen, has also …”

Section: Endocrine Disruption Of Detected Pharmaceutical Contaminantsmentioning

confidence: 99%

“…been shown to cause a reduction in serum T 3 levels in patients taking this medication (Bishnoi et al, 1994). However, according to our knowledge, little is known about the endocrinedisrupting activity of naproxen pollution into the environment, and the effects of this compound on non-target organisms.…”

mentioning

confidence: 99%

Review: <i>Pharmaceutical and personal care products (PPCPs) as endocrine disrupting contaminants (EDCs) in South African surface waters</i>

Archer

Wolfaardt

Wyk

2017

WSA

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Globally, water resources are under constant threat of being polluted by a diverse range of man-made chemicals, and South Africa is no exception. These contaminants can have detrimental effects on both human and wildlife health. It is increasingly evident that several chemicals may modulate endocrine system pathways in vertebrate species, and these are collectively referred to as endocrine disrupting contaminants (EDCs). Although the endocrine-disrupting effect of water pollutants has been mainly linked to agricultural pesticides and industrial effluents, other pollutants such as pharmaceuticals and personal care products (PPCPs) are largely unnoticed, but also pose a potentially significant threat. Here we present for the first time in a South African context, a summarised list of PPCPs and other EDCs detected to date within South African water systems, as well as their possible endocrine-disrupting effect in-vitro and in-vivo. This review addresses other factors which should be investigated in future studies, including endocrine disruption, PPCP metabolites, environmental toxicology, and antibiotic resistance. The challenges of removing EDCs and other pollutants at South African wastewater treatment works (WWTWs) are also highlighted. The need for focused research involving both in-vitro and in-vivo studies to detect PPCPs in water systems, and to delineate adverse outcome pathways (AOPs) of priority PPCPs to aid in environmental impact assessment (EIA), are discussed.

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“…In addition, a plant-derived naphthoquinone, shikonin (PubChem CID: 479503), which did not show interaction with either the fatty acid module or the thyroid hormone related module based on the current dataset, was reported to bind to both NR-LBD-TR domain contained receptors (PubChem AID: 1479) and PES domain contained receptors, including cyclooxygenase-1 and -2 (COX1 and COX2) [53] (dashed line in green in Figure 6). Furthermore, it has also been reported that NSAIDs indeed compete with thyroid hormone binding in vivo [54,55]. Similarly, based on the observed connection between the two neighboring modules (CA module and fatty acid module) due to celecoxib (PubChem CID: 2662), a selective COX2 inhibitor with nanomolar activity against the carbonic anhydrase [56], we successfully verified a hidden interaction of alpha-CA-I-II-III-XIII domain with indomethacin, a ligand of the PES domain [57,58].…”

Section: Resultsmentioning

confidence: 99%

Characterizing protein domain associations by Small-molecule ligand binding

Li¹,

Cheng²,

Wang³

et al. 2012

J Proteome Sci Comput Biol

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Background Protein domains are evolutionarily conserved building blocks for protein structure and function, which are conventionally identified based on protein sequence or structure similarity. Small molecule binding domains are of great importance for the recognition of small molecules in biological systems and drug development. Many small molecules, including drugs, have been increasingly identified to bind to multiple targets, leading to promiscuous interactions with protein domains. Thus, a large scale characterization of the protein domains and their associations with respect to small-molecule binding is of particular interest to system biology research, drug target identification, as well as drug repurposing. Methods We compiled a collection of 13,822 physical interactions of small molecules and protein domains derived from the Protein Data Bank (PDB) structures. Based on the chemical similarity of these small molecules, we characterized pairwise associations of the protein domains and further investigated their global associations from a network point of view. Results We found that protein domains, despite lack of similarity in sequence and structure, were comprehensively associated through binding the same or similar small-molecule ligands. Moreover, we identified modules in the domain network that consisted of closely related protein domains by sharing similar biochemical mechanisms, being involved in relevant biological pathways, or being regulated by the same cognate cofactors. Conclusions A novel protein domain relationship was identified in the context of small-molecule binding, which is complementary to those identified by traditional sequence-based or structure-based approaches. The protein domain network constructed in the present study provides a novel perspective for chemogenomic study and network pharmacology, as well as target identification for drug repurposing.

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Effects of commonly prescribed nonsteroidal anti-inflammatory drugs on thyroid hormone measurements

Cited by 42 publications

References 14 publications

Ciprofloxacin induced hormonal changes in the thyroid gland of rats and Anti-oxidant vitamin A, C and E as rescue agents

Ciprofloxacin induced hormonal changes in the thyroid gland of rats and Anti-oxidant vitamin A, C and E as rescue agents

Review: <i>Pharmaceutical and personal care products (PPCPs) as endocrine disrupting contaminants (EDCs) in South African surface waters</i>

Characterizing protein domain associations by Small-molecule ligand binding

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