| Autor: |
Delrue C; Department of Nephrology, Ghent University Hospital, 9000 Ghent, Belgium., Dendooven A; Department of Pathology, Ghent University Hospital, 9000 Ghent, Belgium.; Faculty of Medicine, University of Antwerp, 2610 Wilrijk, Belgium., Vandendriessche A; Department of Pathology, Ghent University Hospital, 9000 Ghent, Belgium., Speeckaert R; Department of Dermatology, Ghent University Hospital, 9000 Ghent, Belgium., De Bruyne S; Department of Laboratory Medicine, Ghent University Hospital, 9000 Ghent, Belgium., Speeckaert MM; Department of Nephrology, Ghent University Hospital, 9000 Ghent, Belgium.; Research Foundation-Flanders (FWO), 1000 Brussels, Belgium. |
| Abstrakt: |
Renal amyloidosis is a set of complex disorders characterized by the deposition of amyloid proteins in the kidneys, which causes gradual organ damage and potential kidney failure. Recent developments in diagnostic methods, particularly mass spectrometry and proteome profiling, have greatly improved the accuracy of amyloid typing, which is critical for disease management. These technologies provide extensive insights into the specific proteins involved, allowing for more targeted treatment approaches and better patient results. Despite these advances, problems remain, owing to the heterogeneous composition of amyloid proteins and the varying efficacy of treatments based on amyloid type. Access to sophisticated diagnostics and therapy varies greatly, highlighting the global difference in renal amyloidosis management. Future research is needed to investigate next-generation sequencing and gene-editing technologies, like clustered regularly interspaced short palindromic repeats (CRISPR), which promise more profound insights into the genetic basis of amyloidosis. |
