# Current Standards and Perspectives in Proteomics for Cardiac Amyloidosis

## TL;DR

This paper reviews how proteomics is used to diagnose cardiac amyloidosis and highlights the need for standardization to improve clinical reliability.

## Contribution

The paper provides insights and guidance on standardizing proteomics for amyloid typing in cardiac amyloidosis.

## Key findings

- Mass spectrometry-based proteomics is effective for identifying amyloidogenic proteins in cardiac amyloidosis.
- Proteomics is limited to specialized centers due to technical complexity and lack of standardization.
- Referral centers in the USA and Europe share experiences to improve clinical application of proteomics.

## Abstract

Amyloidosis is a heterogeneous group of protein misfolding
disorders
characterized by the deposition of amyloid fibrils in tissues, which
causes progressive organ dysfunction. Among the various forms, cardiac
involvement by transthyretin (ATTR) and immunoglobulin light chain
(AL) amyloidosis is particularly significant, as it is the main determinant
of prognosis and treatment. In clinical practice, tissue biopsy remains
crucial for diagnosing amyloidosis. Amyloid histological typing can
be performed using antibody-based methods such as immunohistochemistry
and immunoelectron microscopy. Mass spectrometry-based bottom-up proteomics
has emerged as a powerful alternative, offering precise identification
and quantification of amyloidogenic proteins. Despite being regarded
as an effective technique for amyloid typing, the application of proteomics
remains limited to specialized centers due to its technical complexity
and lack of standardization in clinical workflows. This paper describes
the current use of proteomics in patients with cardiac amyloidosis,
based on the experience of referral centers in the USA and Europe,
to provide guidance on improving the technique’s reliability
and to identify standard practices, challenges, and gaps in the clinical
application of amyloidosis typing.