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Micronutrients in the Prevention and Improvement of the Standard Therapy for Alzheimer’s Disease
Published in Kedar N. Prasad, Micronutrients in Health and Disease, 2019
Neuroglobin (Ngb) is O2-binding heme protein related to hemoglobin and myoglobin. It is widely and specifically located in neurons of central and peripheral nervous system of vertebrates. It reversibly binds with oxygen with a high affinity. Expression of Ngb increases in response to neuronal hypoxia and protect neurons caused by hypoxia in vitro and in vivo.254–256 It also protects the brain from experimental stroke in vivo.257 Age-dependent loss of Ngb was found in rat cerebral neocortex, hippocampus, caudate-putamen, and cerebellum.258,259
Pterostilbene fluorescent probes as potential tools for targeting neurodegeneration in biological applications
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2022
Lidia Ciccone, Susanna Nencetti, Maria Marino, Chiara Battocchio, Giovanna Iucci, Iole Venditti, Martina Marsotto, Emiliano Montalesi, Simone Socci, Beatrice Bargagna, Elisabetta Orlandini
The lack of any toxics effects of Ptb fluorescent derivatives (1, 2) raised the question if these compounds still maintain some of neuro-protective effects ascribed to their precursor50,51. The discovery that high levels of neuroglobin (NGB), an endogenous neuroprotective globin, are active against several brain injuries, including neurodegeneration, hypoxia, ischaemia, toxicity, and nutrient deprivation prompted us to evaluate the effect of different concentrations of Ptb and their fluorescent derivatives in SH-SY5Y cells. Res 1 µM, which increased NGB levels in neuronal derived cells reducing globin levels in breast cancer cells52, was used as positive control. As expected, Res increased NGB levels by 58% ± 0.6, Ptb 10 µM shows the same efficacy than Res (1 µM) although it is less effective increasing NGB levels by 30% ± 0.4. The compound 1 maintained the same efficacy than Res, with a value higher with respect to its precursor (Ptb), whereas the compound 2 reduced NGB levels under the control value. As a whole, these data, for the first time, indicate that Ptb neuroprotective effects, like Res, could be mediated by the accumulation of NGB suggesting that both polyphenols could share the same signalling pathways. Moreover, only Ptb functionalised on phenolic ring with benzofurazan (compound 1) maintained the same efficacy of its precursor in enhancing NGB levels, while Ptb derivative containing rhodamine B-isothiocyanate (compound 2) significantly reduced NGB levels under the control values, Figure 6.
Regulatory effect of neuroglobin in the recovery of spinal cord injury
Published in The Journal of Spinal Cord Medicine, 2019
Ji-Lin Dai, Yun Lin, Yong-Jian Yuan, Shi-Tong Xing, Yi Xu, Qiang-Hua Zhang, Ji-Kang Min
The neuroglobin is a globin protein involves in the oxygen homeostasis of a cellular system in animals. It is a hemoprotein found in the cerebrospinal fluid (CSF), retinal cells, central nervous system (CNS), peripheral nervous system (PNS) and endocrine tissues.1 Furthermore, it is found in jellyfish, acoel and in the astrocytes of rodent brain under the diseased condition, and seal brain under physiological condition.2–4 Neuroglobin bind with oxygen with more affinity compared to hemoglobin and protects the brain by providing oxygen under ischemic and hypoxic conditions. Neuroglobin has been reported as a neuroprotective agent and resistant to cerebral ischemia in transgenic mice,5 and reduces oxidative stress and improves mitochondrial function under hypoxic condition.6 Neuroglobin has been overexpressed to protect brain following mechanical injury,7 and it has been used to treat reactive oxygen species (ROS) related disorders.6 Brittain1 have reported that the neuroglobin is actively participating in the mitochondrial release of cytochrome c and, thereby apoptosis pathway.
Remote ischaemic preconditioning may prolong permissible period of hypothermic circulatory arrest in a porcine model*
Published in Scandinavian Cardiovascular Journal, 2019
Caius Mustonen, Hannu-Pekka Honkanen, Tuomas Anttila, Johanna Herajärvi, Fredrik Yannopoulos, Tuomas Mäkelä, Timo Kaakinen, Vesa Anttila, Tatu Juvonen
The main finding of this study is that RIPC tends to affect CMRO2. Cellular and molecular mechanisms of RIPC have been studied intensively by our research group as well as others [12,13]. We have previously shown that RIPC preserves cerebral oxygen tension during HCA [9]. This finding suggests that RIPC might enhance suppression of CMRO2 and thereby increase the permissible period of HCA. One of the potential mediators in this process is neuroglobin. It regulates release and stabilization of classical molecules that are associated with oxygen metabolism and survival of neurons such as HIF-1α, nuclear factor erythroid 2-related factor 2, and cytochrome c [13,14].