Shotgun Protein Profile of
Human Adipose Tissue and
Its Changes in Relation to Systemic Amyloidoses
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Abstract
In systemic amyloidosis, accumulation
of misfolded proteins as
extracellular amyloid fibrils in tissues causes severe organ dysfunction,
but the molecular events of tissue damage related to amyloid deposition
are still largely unknown. Through the use of the MudPIT proteomic
approach, comprehensive protein profiles of human amyloid-affected
adipose tissue from patients and its control (non-amyloid-affected)
counterpart were acquired. Label-free comparison between patients
and controls made it possible to highlight differences related to
the presence of amyloid, by describing up- and down-represented proteins,
connected into interacting networks. In particular, extracellular
matrix (ECM), protein folding, lipid metabolism, and mitochondrial
functions were among the most affected structural/functional pathways.
The reported results, obtained with no a priori hypotheses, represent
a significant step forward in the clarification of the molecular mechanisms
involved in amyloidoses at tissue level and are the premise for understanding
protein misfolding diseases