Cancer Cells Can Be Turned Off by Stimulating Formation of Amyloid Bodies

Highlights

Cancer involves new growth formation and spread of cancer cells to distant sites.
Inducing proteins involved in cancer progression to remain stored as amyloid bodies, renders cancer cells inactive.
Growth and spread of cancer can be prevented as long as the proteins remain as amyloid bodies.
This may have potential therapeutic applications in the future.

Cancer cells could be made dormant or inactive by causing the proteins involved in its growth and spread, to be stored within the cells as amyloid bodies. This forms the basis of a study by researchers at Sylvester Comprehensive Cancer Center at the University of Miami Miller School of Medicine.

Outline of the Study

Scientists Study Structurally Modified Proteins
Cells regulate protein functions in a wide variety of ways, including by modifying the structure of the protein.

‘Inducing proteins involved in cancer progression to stay stored as amyloid bodies, renders cancer cells dormant, and could have possible therapeutic applications.’

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Amyloid bodies have been implicated in the pathogenesis of neurological diseases such as Alzheimer's and Parkinson's disease. However, their involvement in the growth and spread of cancer remain largely unknown. The findings of this study open up a new avenue in the therapy of various types of cancers by employing the insight and evidence gained in the field of neuroscience to tumor biology.

Molecular Processes Involved in Amyloid Protein Formation

Two processes have been identified within cells, one promoting amyloid protein formation,

and the other causing breakdown of the amyloid protein structure.

"The amyloid state of protein organization is typically associated with debilitating human neuropathies and rarely observed in physiology," said Stephen Lee, Ph.D., director of the Tumor Biology Program at Sylvester, professor of biochemistry and molecular biology at the Miller School, and corresponding author of the study. "Yet, we found that a large number of proteins are stored as amyloid bodies in cancer cells that are dormant. The heat shock chaperone pathway can disaggregate the amyloid bodies and turn the dormant cancer cells into active, progressing cancer cells."

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The researchers also discovered that ribosomal intergenic noncoding RNA controlled the process of amyloid formation in cancer cells, making it a potential target for drug discovery and development. "If we can stop the amyloid bodies from disaggregating in cancer cells, the hope is that they will remain dormant indefinitely," said Lee. "In addition, we may also be able to turn active cancer cells into dormant ones by encouraging them to store the proteins as amyloid bodies."

Amyloidogenesis has been shown to help cells remain viable during prolonged periods of extracellular stress, underscoring the protective nature of the process, not just in cancer cells.

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About Amyloid Structure of Protein

Misfolding of proteins disrupts critical cellular processes, leading to a wide range of diseases. One such misfolding is the aggregation of proteins from their soluble forms to insoluble fibrils, taking the form of β-pleated sheets referred to as amyloid. Once formed, these fibrils can virtually not be destroyed. This explains the severe and progressive neurodegenerative effects they produce in Alzheimer’s and Parkinson’s disease.

Intensive research is ongoing to develop treatments targeting amyloidogenesis in various diseases, including cancer.

Scope of the Study Findings

The most important takeaway from this study would be its potential therapeutic application in various forms of cancer.

"Following this approach, we wouldn't necessarily rid the body of cancer cells, but we would keep them inactive - shut off, if you will - and not allow them to become active again," said Lee. "I am optimistic this could become a novel way of treating cancer. There are already drugs on the market, and others are being studied, that target the ribosomal intergenic noncoding RNA as well as the heat shock chaperone pathway."

Source-Medindia