If one person is corrupted, he will try to corrupt other people also. But what amazing thing is even protein follow the same pattern.
A new study led by the researchers at the UT Southwestern Medical Center found a way by which cells invites the corrupted protein inside which can lead to neurodegenerative disease by turning normal protein into corrupted ones.
Alzheimer’s and Parkinson Disease which are the neurodegenerative diseases linked to misfolding and accumulation of particular protein which in turn can induce the default in other protein also.
These particular proteins at fault are the disease-associated proteins tau, alpha-synuclein and amyloid-beta which must bind to heparin sulfate proteoglycan (HSPGS), a sugar-protein present on the cell surface. This binding leads to cell bringing corrupted protein inside.
Tau protein is mostly present in the neuron of the central nervous system and its function is to stabilize the microtubules.
HSPGS have different size and structure with different patterns of sugar and sugar can also have different sulfur moieties i.e. different sulfur-containing groups.
Hence the researcher examined that how the different sulfate moieties can affect binding and uptake of corrupted protein into the cell.
She found that there was an only a specific pattern and modified HSPG which was allowing misfolded Tau protein to enter into the cell. On the other hand, the other 2 protein i.e. alpha-synuclein and amyloid-beta were entering due to particular specific moieties.
After that researcher identified the particular sulfation patterns creating enzyme in HSPG and removed it. The result was no misfolded tau protein was able to enter into the cell.
This happened because as the sulfation pattern and HPSG decoration changed meaning misfolded tau no longer knew the molecular password.
The next step of this research is to find whether the process is same in the brain as it is in cultured brain cells.
In the light of this study, researchers hope to find a therapy to stop uptake of corrupted protein i.e. stopping misfolded tau protein to enter.
“There’s something very remarkable about how efficiently a cell will take up these aggregates, bring them inside and use them to make more,” Diamond said. “This knowledge has important implications for our understanding how neurodegenerative diseases get worse over time. Because we have identified specific enzymes that can be inhibited to block this process, this could lead to new therapies.”