**Author Listing - Lead/ Submitting Author (we will be communicating with this individual): Name, Institution, City and State where the work was done. Co-authors will be added in a separate section.**
Dario Di Silvestre
Institute for Biomedical Technologies – National Research Council, F.lli Cervi 93, 20054 Segrate (MI), Italy

**Main Body of the Abstract**
Systemic amyloidosis are diseases characterized by misfolding of circulating proteins, which are progressively accumulated at the extracellular level. Deposition in the form of insoluble amyloid beta-sheet fibrils can occur in various tissues and organs, including the heart, kidney and lung [1]. In addition to structural distortions caused by large amounts of amyloid deposits, aberrant interactions of prefibrillar aggregates contribute to cell death and organ dysfunction. Analyzing tissues and organs at a holistic level is critical to shed light on the molecular and histological alterations induced by amyloid aggregates in affected tissues. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system-wide. To fill this gap, we evaluated proteome changes in heart tissues from AL λ and ATTR patients and Controls [2]. Protein profiles and differentially abundant proteins (DAPs) were further processed by data-derived systems biology approaches based on protein-protein interaction and protein co-expression network models. In addition to provide new insights on functional modules most affected by amyloid deposition, the correlation between the network's structure and function was exploited to identify topologically relevant proteins, called hubs, as key proteins in amyloidosis-related processes [3]. These findings contribute to the puzzle of the pathophysiological mechanisms and key players that characterize the heart tissue of patients affected by AL and ATTR amyloidosis. Furthermore, they support the integration of -omics profiles and network models as a promising strategy to generate new knowledge for developing more effective diagnostic methods and therapies.
1.NEngl JMed 349(6):583-596
2.Amyloid 30(1):96-108
3.Cells 12(5):69



**Author Listing - Lead/ Submitting Author (we will be communicating with this individual): Name, Institution, City and State where the work was done. Co-authors will be added in a separate section.**
Dario Di Silvestre
Institute for Biomedical Technologies – National Research Council, F.lli Cervi 93, 20054 Segrate (MI), Italy

**Main Body of the Abstract**
Systemic amyloidosis are diseases characterized by misfolding of circulating proteins, which are progressively accumulated at the extracellular level. Deposition in the form of insoluble amyloid beta-sheet fibrils can occur in various tissues and organs, including the heart, kidney and lung [**1**]. In addition to structural distortions caused by large amounts of amyloid deposits, aberrant interactions of prefibrillar aggregates contribute to cell death and organ dysfunction. Analyzing tissues and organs at a holistic level is critical to shed light on the molecular and histological alterations induced by amyloid aggregates in affected tissues. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system-wide. To fill this gap, we evaluated proteome changes in heart tissues from AL _λ_ and ATTR patients and Controls [**2**]. Protein profiles and differentially abundant proteins (DAPs) were further processed by data-derived systems biology approaches based on protein-protein interaction and protein co-expression network models. In addition to provide new insights on functional modules most affected by amyloid deposition, the correlation between the network's structure and function was exploited to identify topologically relevant proteins, called hubs, as key proteins in amyloidosis-related processes [**3**]. These findings contribute to the puzzle of the pathophysiological mechanisms and key players that characterize the heart tissue of patients affected by AL and ATTR amyloidosis. Furthermore, they support the integration of -omics profiles and network models as a promising strategy to generate new knowledge for developing more effective diagnostic methods and therapies.
1.NEngl JMed 349(6):583-596
2.Amyloid 30(1):96-108
3.Cells 12(5):69



Omics data-derived systems biology to shed light on molecular mechanisms characterizing the heart tissue of ALλ and ATTR amyloidosis patients PB113 (#290)

We invite you to attend the XIX International Symposium on Amyloidosis to be held in Rochester, MN.

This symposium is organized as a hybrid meeting (with the focus on in-person) held from Sunday, May 26 through Thursday, May 30, 2024.

Together with the ISA Board and members of Mayo Clinic, a very attractive scientific hybrid program is being planned. The program will cover a variety of types of systemic amyloidosis: ATTR (hereditary and wild-type), AL (light-chain), AA and less frequent forms. There will be key lectures, specific symposia including those company sponsored, oral presentations and poster sessions of accepted abstracts.

COURSE DESCRIPTION
This program will provide a comprehensive review of state-of-the-art education in systemic amyloidosis: basic science, pathophysiology, diagnosis, current and emerging treatments. Scientific presentations will include competitive oral and poster abstracts. The rapid evolution of scientific discovery and expanding treatment options has created tremendous interest in the field and this meeting will fill and important gap in educating scientists and clinicians.