What if we could tackle the
cause of Alzheimer’s and
Parkinson’s Disease?
Neurodegeneration
A hallmark of neurodegenerative diseases such as Alzheimer’s and Parkinson’s Disease, as well as rarer diseases such as Huntington’s Disease and Amyotrophic Lateral Sclerosis (ALS), is the appearance of cytotoxic, misfolded proteins. For example, it has long been known that the protein a-synuclein and the large aggregates of a-synuclein known as Lewy Bodies have been correlated with Parkinson’s Disease disease progression.
While functional a-synuclein is important for healthy brain function, excessive protein causes oligomers and aggregation, leading to neurotoxicity and the characteristic deadly symptoms of PD.
It’s likely that a-synuclein aggregation is caused by lysosomal misprocessing and that this dysfunction is in turn associated with dysfunctional autophagy
This hypothesis is underpinned by strong genetic evidence.
By restoring autophagy in such diseased cells we can remove the misfolded protein, such as a-synuclein, and restore lysosome function, something we have already demonstrated in cells derived from Parkinson’s DIsease patients and early onset Alzheimer’s patients.
iPS-derived GBA-mutated Parkinson’s Disease patient neurons exhibit reduced autophagy levels
Blue = DAPI (nuclei); Red = DQ-BSA (measure of lysosomal degradative activity)
The autophagy deficit in GBA patient neurons is rescued by TRPML1 activator SAM001
Parkinson’s Disease GBA patient neurons show increased α-synuclein aggregates
Green = aggregated a-synuclein (pS129 antibody)
Significant reduction in a-synuclein levels in patient neurons on treatment with Samsara’s TRPML1 activator, SAM001
iPS-derived GBA-mutated Parkinson’s Disease patient neurons exhibit reduced autophagy levels
Blue = DAPI (nuclei); Red = DQ-BSA (measure of lysosomal degradative activity)
The autophagy deficit in GBA patient neurons is rescued by TRPML1 activator SAM001
Parkinson’s Disease GBA patient neurons show increased α-synuclein aggregates
Green = aggregated a-synuclein (pS129 antibody)
Significant reduction in a-synuclein levels in patient neurons on treatment with Samsara’s TRPML1 activator, SAM001
Samsara compounds restore autophagy and reverse the pathological accumulation of a-synuclein in dopaminergic neurons derived from a patient with the GBA mutation of Parkinson’s Disease
The Lysoseeker™ Platform
A unique approach for discovering new autophagy therapeutics.
Neurodegeneration
What if we could tackle the cause of Alzheimer’s and Parkinson’s Disease?
Rare Monogenic Disease
What if we could offer real hope for serious rare genetic diseases?
Our Pipeline
Samsara is leveraging its knowledge of new autophagy biology.
Samsara Therapeutics adds eminent neurologist Professor Dame Pamela Shaw to its scientific advisory board to help accelerate ALS/MND treatment development
Samsara Therapeutics, the autophagy biotech company, has appointed eminent neurologist and world-leading researcher in Amyotrophic Lateral Sclerosis (ALS)/Motor Neuron Disease (MND) Professor Dame Pamela Shaw to its scientific advisory board.
Samsara Therapeutics Parkinson’s drug receives funding boost from The Michael J. Fox Foundation
Samsara Therapeutics announced today that it has received a grant from The Michael J. Fox Foundation for Parkinson’s Research (MJFF) to further its research into a promising Parkinson’s disease drug.
Samsara Therapeutics unveils promising autophagy drug candidate, offering new hope for people with Parkinson’s and motor neurone disease
Samsara Therapeutics is first in the race to find a viable, potent autophagy inducing drug, with the potential to give us longer and healthier lives.
Meet the Neuro Team – Modelling Neurodegeneration in a Dish
We caught up with Senior Scientists Gabriela Vilema Enríquez and Matthew Williamson on their work within the neuroscience team at Samsara.
© 2021 Samsara Therapeutics | Legal Information | Privacy
© 2021 Samsara Therapeutics
Legal Information | Privacy