Autism-Cancer Link Identified

by Dr. Meenakshy Varier on  March 11, 2017 at 6:06 PM Health Watch
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Highlights
  • SHANK protein prevents the ability of cancer cells to adhere and migrate to surrounding tissue.
  • But in autism there is the absence or gene mutations associated with SHANK proteins.
  • Gene mutations in SHANK, found in autistic patients, impair SHANKs ability to prevent the adherence of both neurons and breast cancer cells.
An unexpected link between cancer and autism has been discovered..
Autism-Cancer Link Identified
Autism-Cancer Link Identified

Researchers from Turku Centre for Biotechnology have observed that a protein called SHANK prevents the spread of breast cancer cells to the surrounding tissue by regulating the cell shape and adhesion in very different cell types.

It prevented the ability of cancer cells to adhere and migrate on their environment and invade into surrounding tissue.

The SHANK protein has been previously been intensively studied in several processes in the central nervous system, and it is known that its absence or gene mutations are related to autism.

The findings revealed that in autistic patients with gene mutations in SHANK, impairs the ability of SHANK to prevent the adherence of both neurons and breast cancer cells.

Rap1 proteins activate cell adhesion receptors called integrins.

In cell culture experiments, the researchers found that SHANK protein limits the ability of the protein called Rap1 to activate integrins.

But gene mutations of SHANK which impairs its ability, triggers increases Rap1 activity, cell spreading, migration and invasion in cancer.

The same mechanism that regulated cancer cell motility is applicable to the morphology and branching of neurites, known to be essential for normal brain function.

The research team is currently assessing the impact of SHANK proteins on cancer cells, especially on their proliferation.

The findings were published in Nature Cell Biology.

Reference

  1. Igor Barsukov et al. SHANK proteins limit integrin activation by directly interacting with Rap1 and R-Ras. Nature Cell Biology; (2017) doi:10.1038/ncb3487


Source: Medindia

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