The role of Tumour Necrosis Factor in neuroinflammation associated with Parkinson's disease and targeted therapies.

Neurodegenerative disorders Parkinson's disease is a progressive neurodegenerative disorder associated with neuroinflammatory responses that lead to the neurodegeneration of the dopaminergic neurons. These neuroinflammatory mechanisms involve various cytokines produced by the activated glial cells. Tumour Necrosis factor α (TNF α) is one of the major mediators of the neuroinflammation associated with neurodegeneration. TNF α has a dual role of neuroprotection and neurotoxicity in the brain. The effective pathways of TNF involve various signalling pathways transduced by the receptors TNFR1 and TNFR2. Effective therapeutic strategies have been produced targeting the neurotoxic behaviour of the Tumour Necrosis Factor and the associated neurodegeneration which includes the use of Dominant Negative Tumour Necrosis Factor (DN-TNF) inhibitors like XENP 345 and XPro®1595 and peroxisome proliferator receptor gamma (PPAR-γ) agonists.

A Review on Tradescantia: Phytochemical Constituents, Biological Activities and Health-Promoting Effects.

Tradescantia is a genus of herbaceous and perennial plants belonging to the Commelinaceae family and organized into three infrageneric classifications and 12 sections. More than 80 species within the genus have been used for centuries for medicinal purposes. Phytochemical compounds (from various species of the genus) such as coumarins, alkaloids, saponins, flavonoids, phenolics, tannins, steroids and terpenoids have recently been characterized and described with antioxidant, cytotoxic, anti-inflammatory, anticancer or antimicrobial properties. The objective of this review is to describe the different aspects of the genus Tradescantia, including its botanical characteristics, traditional uses, phytochemical composition, biological activities, and safety aspects.

The effects of wireless electromagnetic fields on the activities of carbonic anhydrase and acetylcholinesterase enzymes in various tissues of rats.

The purpose of our study is to assist in understanding the effects of wireless electromagnetic waves on carbonic anhydrase (CA) and acetylcholinesterase (AChE) enzymes activities in the different tissues of the rats. For this purpose, two different groups each of which contains eight rats (n = 8) were formed as being control group and wireless electromagnetic wave-administered group. The rats were necropsied after 60 min from the injection of chemicals into the rats intraperitoneally. The different tissues of the rats were extracted. CA and AChE enzymes activities were measured for each tissue. All the experimental results were provided in mean ± S.D. Statistical significance was identified to be P < 0.05. It was observed that there were significant changes of enzyme activities in wireless-administered group in salivary gland, stomach, colon, liver, and striated muscle tissues.

Investigation of acetylcholinesterase and mammalian DNA topoisomerases, carbonic anhydrase inhibition profiles, and cytotoxic activity of novel bis(α-aminoalkyl)phosphinic acid derivatives against human breast cancer.

The aim of this study was to evaluate biologically active novel molecules having potentials to be drugs by their antitumor properties and by activities of apoptotic caspase and topoisomerase. Following syntheses of novel eight bis(α-aminoalkyl)phosphinic acid derivatives (4a-h) as a result of array of reactions, compounds were evaluated by cytotoxic effects in vitro on human breast cancer (MCF-7) and normal endothelial (HUVEC) cell lines. All phosphinic acid derivatives were effective for cytotoxicity on both MCF-7 and HUVEC lines, while 4c, 4e, and 4f compounds were found significantly more effective. For the evaluation of antitumor properties of compounds in a highly sensitive method, their effects on inhibiting topoisomerases I and II were investigated. Also, some of the bis(α-aminoalkyl)phosphinic acid derivatives (4a, 4e-h) showed nice inhibitory action against acetylcholinesterase and human carbonic anhydrase isoforms I and II.