The review analyzes current clinical studies on the use of therapeutic hypothermia as a neuroprotective method for treatment of brain damage. This method yields good outcomes in patients with acute brain injuries and chronic critical conditions. There has been shown the interest of researchers in studying the preventive potential of therapeutic hypothermia in secondary neuronal damage. There has been described participation of new molecules producing positive effect on tissues and cells of the central nervous system - proteins and hormones of cold stress - in the mechanisms of neuroprotection in the brain. The prospects of using targeted temperature management in treatment of brain damage are considered.

The advancements in biotechnology over time have led to an increase in the demand of pure, soluble and functionally active proteins. Recombinant protein production has thus been employed to obtain high expression of purified proteins in bulk. E. coli is considered as the most desirable host for recombinant protein production due to its inexpensive and fast cultivation, simple nutritional requirements and known genetics. Despite all these benefits, recombinant protein production often comes with drawbacks, such as, the most common being the formation of inclusion bodies due to improper protein folding. Consequently, this can lead to the loss of the structure-function relationship of a protein. Apart from various strategies, one major strategy to resolve this issue is the use of molecular chaperones that act as folding modulators for proteins. Molecular chaperones assist newly synthesized, aggregated or misfolded proteins to fold into their native conformations. Chaperones have been widely used to improve the expression of various proteins which are otherwise difficult to produce in E. coli. Here, we discuss the structure, function, and role of major E. coli molecular chaperones in recombinant technology such as trigger factor, GroEL, DnaK and ClpB.

Hemoglobin (Hb) synthesis is a complex, well-coordinated process that requires molecular chaperones. These intervene in different steps: regulating epigenetic mechanisms necessary for the adequate expression of the α- and β-globin clusters, binding the nascent peptides and helping them acquire their native structure, preventing oxidative damage by free globin chains and preventing the cleavage of essential erythroid transcription factors. This study analyzed the distribution of the single nucleotide polymorphism (SNP) rs4296276 in intron 1 of the α-globin chaperone α Hb-stabilizing protein (AHSP) in the Argentinean population. The risk allele was found in thalassemia patients who exhibited more severe phenotypes than expected. Future studies may help establish the role of these chaperones as modifiers in pathological states with globin chain imbalance, such as thalassemia.

Plants are sessile in nature, but are capable to evade from high level concentration of heavy metals like Cd, Hg, Cu, through various metabolic pathways. Some of the pathways regulate normal metabolism in plants, whereas others are required for for their survival under metal toxicity. Different plant proteins act as transporters to transfer metal from one organelle to the other and further eliminate it out from the plants. Initially, exposure of heavy metals/metalloids to plants lead to over expression of proteins which in turn stimulate other stress-related genes. Further, they activate signalling mechanism like MAPK cascade, Cd-Calmodulin signalling pathway, and oxidation signalling pathway that lead to generation of ROS (reactive oxygen species). Once these ROS (highly unstable) are formed, they generate free radicals which react with macromolecules like proteins and DNA. This has negative impact on plant growth and leads to ageing and, eventually, cell death. The uncontrolled, destructive processes damage plants physiologically and ultimately lead to oxidative stress. Activation of antioxidant enzymes like SOD (superoxide dismutase) and CAT (catalase) allows plants to cope under oxidative stress conditions. Among plant proteins, some of the antioxidant enzymes like glutathione, and APX (ascorbate peroxidase) play defensive roles against abiotic stress in plants. Chaperones help in protein folding to maintain protein stability under stress conditions. With this background, the present review gives a brief account of the functions, localization and expression pattern of plant proteins against metal/metalloid toxicity. Moreover, the aim of this review is also to summarize the cutting edge research of plant protein and metal interfaces and their future prospects.

As sessile organisms, plants are exposed to persistently changing stresses and have to be able to interpret and respond to them. The stresses, drought, salinity, chemicals, cold and hot temperatures, and various pathogen attacks have interconnected effects on plants, resulting in the disruption of protein homeostasis. Maintenance of proteins in their functional native conformations and preventing aggregation of non-native proteins are important for cell survival under stress. Heat shock proteins (HSPs) functioning as molecular chaperones are the key components responsible for protein folding, assembly, translocation, and degradation under stress conditions and in many normal cellular processes. Plants respond to pathogen invasion using two different innate immune responses mediated by pattern recognition receptors (PRRs) or resistance (R) proteins. HSPs play an indispensable role as molecular chaperones in the quality control of plasma membrane-resident PRRs and intracellular R proteins against potential invaders. Here, we specifically discuss the functional involvement of cytosolic and endoplasmic reticulum (ER) HSPs/chaperones in plant immunity to obtain an integrated understanding of the immune responses in plant cells.

The development of α-synuclein immunoreactive aggregates in selectively vulnerable neuronal types of the human central, peripheral, and enteric nervous systems is crucial for the pathogenesis of sporadic Parkinson\'s disease. The presence of these lesions persists into the end phase of the disease, a process that is not subject to remission. The initial induction of α-synuclein misfolding and subsequent aggregation probably occurs in the olfactory bulb and/or the enteric nervous system. Each of these sites is exposed to potentially hostile environmental factors. Once formed, the aggregates appear to be capable of propagating trans-synaptically from nerve cell to nerve cell in a virtually self-promoting pathological process. A regional distribution pattern of aggregated α-synuclein emerges that entails the involvement of only a few types of susceptible and axonally interconnected projection neurons within the human nervous system. One major route of disease progression may originate in the enteric nervous system and retrogradely reach the dorsal motor nucleus of the vagal nerve in the lower brainstem. From there, the disease process proceeds chiefly in a caudo-rostral direction through visceromotor and somatomotor brainstem centres to the midbrain, forebrain, and cerebral cortex. Spinal cord centres may become involved by means of descending projections from involved lower brainstem nuclei as well as by sympathetic projections connecting the enteric nervous system with postganglionic peripheral ganglia and preganglionic nuclei of the spinal cord. The development of experimental cellular and animal models is helping to explain the mechanisms of how abnormal α-synuclein can undergo aggregation and how transmission along axonal connectivities can occur, thereby encouraging the initiation of potential disease-modifying therapeutic strategies for sporadic Parkinson\'s disease.