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Synthetic and Natural Inhibitors of Mortalin for Cancer Therapy. | LitMetric

AI Article Synopsis

  • Upregulation of Mortalin, a stress chaperone, is linked to serious cancer processes like tumor development, aggressiveness, metastasis, and drug resistance.
  • Research shows that higher Mortalin levels help cancer cells grow, spread, and avoid cell death, which are common traits in cancers.
  • Mortalin is a promising target for cancer treatments, and various inhibitors (like peptides, small RNAs, and compounds) are being explored for their potential to combat cancer.

Article Abstract

Upregulation of stress chaperone Mortalin has been closely linked to the malignant transformation of cells, tumorigenesis, the progression of tumors to highly aggressive stages, metastasis, drug resistance, and relapse. Various in vitro and in vivo assays have provided evidence of the critical role of Mortalin upregulation in promoting cancer cell characteristics, including proliferation, migration, invasion, and the inhibition of apoptosis, a consistent feature of most cancers. Given its critical role in several steps in oncogenesis and multi-modes of action, Mortalin presents a promising target for cancer therapy. Consequently, Mortalin inhibitors are emerging as potential anti-cancer drugs. In this review, we discuss various inhibitors of Mortalin (peptides, small RNAs, natural and synthetic compounds, and antibodies), elucidating their anti-cancer potentials.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11506508PMC
http://dx.doi.org/10.3390/cancers16203470DOI Listing

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Synthetic and Natural Inhibitors of Mortalin for Cancer Therapy.

Cancers (Basel)

October 2024

Department of Computational Biology, Indraprastha Institute of Information Technology (IIIT) Delhi, Okhla Industrial Estate, Phase III, New Delhi 110020, India.

Article Synopsis
  • Upregulation of Mortalin, a stress chaperone, is linked to serious cancer processes like tumor development, aggressiveness, metastasis, and drug resistance.
  • Research shows that higher Mortalin levels help cancer cells grow, spread, and avoid cell death, which are common traits in cancers.
  • Mortalin is a promising target for cancer treatments, and various inhibitors (like peptides, small RNAs, and compounds) are being explored for their potential to combat cancer.
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Mortalin, a member of the Hsp70 family of proteins, is commonly enriched in many types of cancers. It promotes carcinogenesis and metastasis in multiple ways of which the inactivation of the tumor suppressor activity of p53 has been firmly established. The downregulation of mortalin and/or disruption of mortalin-p53 interactions by small molecules has earlier been shown to activate p53 function yielding growth arrest/apoptosis in cancer cells.

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Melittin, a peptide from bee venom, was found to be able to interact with many proteins, including calmodulin target proteins and ion-transporting P-type ATPases. It is assumed that melittin mimics a protein module involved in protein-protein interactions within cells. Previously, a Na^(+)/K^(+)-ATPase containing the α1 isoform of the catalytic subunit was found to co-precipitate with a protein with a molecular weight of about 70 κDa that interacts with antibodies against melittin by cross immunoprecipitation.

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Functional inactivation of wild-type p53 is a major trait of cancerous cells. In many cases, such inactivation occurs by either gene mutations or due to overexpression of p53 binding partners. This review focuses on an overexpressed p53 binding partner called mortalin, a mitochondrial heat shock protein that sequesters both wild-type and mutant p53 in malignant cells due to changes in subcellular localization.

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The BCL-2 family protein BCL-RAMBO, also known as BCL2-like 13, anchors at the outer mitochondrial membrane and regulates apoptosis, mitochondrial fragmentation, and mitophagy. However, the mechanisms underlying the proapoptotic role of BCL-RAMBO remain unclear. In the present study, we demonstrated that BCL-RAMBO interacted with glucose-regulated protein 75 (GRP75), also known as heat shock protein family A member 9, and mortalin using co-immunoprecipitation and glutathione S-transferase-based pull-down assays.

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