bioRxiv Science⌕ Search

Biology subjects

Westermark, P.

Publications and source records attributed to Westermark, P..

2 recordsLinked to original sources

Single-Cell Resolution of Cellular Damage Illuminates Disease Progression

Degenerative diseases feature progressive accumulation of cellular damage, leading to impaired organ function. Capturing such gradual decline of individual cells in vivo remains challenging. Here, we present a universal framework for quantifying damage at single-cell resolution, to uncover molecular trajectories of degeneration. This method enables the detection of progressive damage within cell populations under physiological and pathological conditions. We developed the Podocyte Damage Score (PDS) and Hepatocyte Damage Score (HDS) to monitor deterioration in kidney glomerulosclerosis and liver steatosis. The application of these scores to murine and human datasets quantified cellular damage across disease models and distinguished varying degrees of damage even in unperturbed samples. The PDS revealed circadian gene expression dysregulation as a consequence of podocyte injury, while the HDS identified a threshold of hepatocyte damage leading to senescence and metabolic dysfunction. The approach provides a scalable tool for decoding disease progression and identifying therapeutic targets across degenerative disorders.

bioinformatics↗

Cryo-EM structure of an amyloid fibril from systemic amyloidosis

Systemic AA amyloidosis is a worldwide occurring disease of humans and animals that arises from the misfolding of serum amyloid A protein. To provide insights into the molecular basis of this disease we used electron cryo-microscopy and determined the structure of an ex vivo amyloid fibril purified from AA amyloidotic mice at 3.0 [A] resolution. The fibril consists of C-terminally truncated serum amyloid A protein arranged into a compactly folded all-{beta} conformation. The structure identifies the protein N-terminus as central for the assembly of this fibril and provides a mechanism for its prion-like replication. Our data further explain how amino acid substitutions within the tightly packed fibril core can lead to amyloid resistance in vivo.

biophysics↗