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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

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A targeted proteomics approach to amyloidosis typing.

Matteo Conti¹, Irene Poppi¹, Thomas Matulli Cavedagna¹

¹Clinical Mass Spectrometry, Metropolitan Laboratory AUSL, Bologna, Italy.

Clinical Mass Spectrometry (Del Mar, Calif.)

|August 28, 2024

Summary

A new targeted proteomics method accurately identifies amyloidosis-causing proteins in tissues using mass spectrometry. This approach offers a sensitive and specific diagnostic tool for clinical research, aiding in personalized amyloidosis treatment.

Keywords:

Amyloidosis Cardiac muscle tissue Immunoglobulin light chains Mass spectrometry Protein typing Subcutaneous adipose tissue Targeted proteomics Transthyretin

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Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis

Published on: June 9, 2018

Area of Science:

Proteomics
Mass Spectrometry
Clinical Diagnostics

Background:

Amyloidosis is a severe condition caused by protein deposits in organs and tissues.
Accurate protein identification is crucial for diagnosis and personalized treatment.
Current advanced methods like LC-MS/MS are limited to specialized centers.

Purpose of the Study:

To develop a targeted proteomics approach for amyloid protein typing.
To enable analysis using low-resolution mass spectrometry without laser microdissection.
To determine frequently encountered amyloid proteins (immunoglobulin light chains, transthyretin) and tissue-specific reference proteins.

Main Methods:

Tissue samples were digested, reduced, alkylated, and trypsinized to create peptide mixtures.
Peptides were purified by SPE and separated by LC.
Proteotypic peptides were detected using Multiple Reaction Monitoring (MRM) transitions.

Main Results:

The method demonstrated high specificity and sensitivity for detecting amyloid protein peptides.
Limit of detection (LOD) values were in the picomole range for key amyloid proteins in different tissues.
Ratios of amyloid to tissue-specific proteins correlated with amyloid deposit presence.

Conclusions:

This targeted proteomics approach provides sensitive and specific discrimination of amyloidosis-affected tissues.
The method is suitable for clinical research applications.
It facilitates the identification of amyloid proteins for better patient management.