Due to the intrinsic alterations of cellular metabolism, de novo genetic mutations, and extrinsic factors in the tumor microenvironment, cancer cells are constantly under stress, and they retort to this stress by inducing the expression levels of chaperones. Chaperones or heat-shock proteins (HSPs) are a large family of highly conserved and constitutively expressed proteins, traditionally known to be involved in protein folding, protein trafficking, and assembly/disassembly of oligomeric structures. Under stress conditions, they facilitate correct folding and prevent toxic protein aggregation. However, severe and chronic stress activates chaperones-facilitated proteomic alterations that generate adaptive and pro-survival signals. Emerging studies have started to appreciate the role of chaperones in the intricate regulation of the fine balance between the protective and destructive cellular responses within the tumor microenvironment. We intend to bring such emerging ideas together in one platform focusing on the role of chaperones in the tumor microenvironment.
Empirical studies have provided the evidence to support the critical requirement of chaperones for tumor neoangiogenesis and discussed the importance of their inhibition, for instance, GRP78 in Glioblastoma, to dually suppresses tumor growth and angiogenesis. The role of chaperones in the microenvironment have now well extended beyond the endothelial cells. There is enough data suggesting that chaperones promote the uptake of antigens by antigen-presenting cells while simultaneously triggering the activation of T lymphocytes. Not only immunological response, but chaperones also participate in tumor invasion and metastatic signaling cascades and thus contribute to the poor survival rates among patients. Considering the importance of the molecular chaperones in the tumor microenvironment, we want to dedicate the upcoming Research Topic in Frontiers in Molecular Bioscience, to summarize the structural and functional characteristics of chaperones and discuss their roles in the tumor microenvironment.
The Research Topic will cover, but is not limited to, the following:
• The role of chaperones and chaperome in the context of the tumor and tumor microenvironment
• How do the chaperones, cochaperones, and their connectivity (or protein-protein interactions) alter during tumorigenesis
• What novel tools, techniques, and reagents are available to dissect the functions of chaperones in the tumor microenvironment
• How can we therapeutically target them to modulate tumor microenvironment in favor of tumor regression and what are the challenges we might have to experience
Due to the intrinsic alterations of cellular metabolism, de novo genetic mutations, and extrinsic factors in the tumor microenvironment, cancer cells are constantly under stress, and they retort to this stress by inducing the expression levels of chaperones. Chaperones or heat-shock proteins (HSPs) are a large family of highly conserved and constitutively expressed proteins, traditionally known to be involved in protein folding, protein trafficking, and assembly/disassembly of oligomeric structures. Under stress conditions, they facilitate correct folding and prevent toxic protein aggregation. However, severe and chronic stress activates chaperones-facilitated proteomic alterations that generate adaptive and pro-survival signals. Emerging studies have started to appreciate the role of chaperones in the intricate regulation of the fine balance between the protective and destructive cellular responses within the tumor microenvironment. We intend to bring such emerging ideas together in one platform focusing on the role of chaperones in the tumor microenvironment.
Empirical studies have provided the evidence to support the critical requirement of chaperones for tumor neoangiogenesis and discussed the importance of their inhibition, for instance, GRP78 in Glioblastoma, to dually suppresses tumor growth and angiogenesis. The role of chaperones in the microenvironment have now well extended beyond the endothelial cells. There is enough data suggesting that chaperones promote the uptake of antigens by antigen-presenting cells while simultaneously triggering the activation of T lymphocytes. Not only immunological response, but chaperones also participate in tumor invasion and metastatic signaling cascades and thus contribute to the poor survival rates among patients. Considering the importance of the molecular chaperones in the tumor microenvironment, we want to dedicate the upcoming Research Topic in Frontiers in Molecular Bioscience, to summarize the structural and functional characteristics of chaperones and discuss their roles in the tumor microenvironment.
The Research Topic will cover, but is not limited to, the following:
• The role of chaperones and chaperome in the context of the tumor and tumor microenvironment
• How do the chaperones, cochaperones, and their connectivity (or protein-protein interactions) alter during tumorigenesis
• What novel tools, techniques, and reagents are available to dissect the functions of chaperones in the tumor microenvironment
• How can we therapeutically target them to modulate tumor microenvironment in favor of tumor regression and what are the challenges we might have to experience
