RESUMO
Heat-shock proteins (HSPs), also known as stress proteins, are ubiquitously present in all forms of life. They play pivotal roles in protein folding and unfolding, the formation of multiprotein complexes, the transportation and sorting of proteins into their designated subcellular compartments, the regulation of the cell cycle, and signalling processes. These HSPs encompass HSP27, HSP40, HSP70, HSP60, and HSP90, each contributing to various cellular functions. In the context of cancer, HSPs exert influence by either inhibiting or activating diverse signalling pathways, thereby impacting growth, differentiation, and cell division. This article offers an extensive exploration of the functions of HSPs within the realms of pharmacology and cancer biology. HSPs are believed to play substantial roles in the mechanisms underlying the initiation and progression of cancer. They hold promise as valuable clinical markers for cancer diagnosis, potential targets for therapeutic interventions, and indicators of disease progression. In times of cellular stress, HSPs function as molecular chaperones, safeguarding the structural and functional integrity of proteins and aiding in their proper folding. Moreover, HSPs play a crucial role in cancer growth, by regulating processes such as angiogenesis, cell proliferation, migration, invasion, and metastasis.
RESUMO
Recent research has focused mostly on understanding and combating the neurodegenerative mechanisms and symptoms of Parkinson's disease (PD). Moreover, developing novel therapeutic targets to halt the progression of PD remains a key focus for researchers. As yet, no agents have been found to have unambiguous evidence of disease-modifying actions in PD. The primary objective of this review is to summarize the promising targets that have recently been uncovered which include histamine 4 receptors, beta2 adrenergic receptor, phosphodiesterase 4, sphingosine-1-phosphate receptor subtype 1, angiotensin receptors, high-mobility group box 1, rabphilin-3A, purinergic 2Y type 12 receptor, colony-stimulating factor-1 receptor, transient receptor potential vanilloid 4, alanine-serine-cysteine transporter 2, G protein-coupled oestrogen receptor, a mitochondrial antiviral signalling protein, glucocerebrosidase, indolamine-2,3-dioxygenase-1, soluble epoxy hydroxylase and dual specificity phosphatase 6. We have also reviewed the molecular signalling cascades of those novel targets which cause the initiation and progression of PD and gathered some emerging disease-modifying agents that could slow the progression of PD. These approaches will assist in the discovery of novel target molecules, for curing disease symptoms and may provide a glimmer of hope for the treatment of PD. As of now, there is no drug available that will completely prevent the progression of PD by inhibiting the pathogenesis involved in PD, and thus, the newer targets and their inhibitors or activators are the major focus for researchers to suppress PD symptomatology. And the major limitations of these targets are the lack of clinical data and less number pre-clinical data, as we have majorly discussed the different targets which all have well reported for other disease pathogenesis. Thus, finding the disease-drug interactions, the molecular mechanisms, and the major side effects will be major challenges for the researchers.
