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In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study
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In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study
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Journal Article
In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study
2016
Overview
Light chain (AL) amyloidosis, caused by deposition of amyloidogenic immunoglobulin light chains (LCs), is the most common systemic form in industrialized countries. Still open questions, and premises for developing targeted therapies, concern the mechanisms of amyloid formation
in vivo
and the bases of organ targeting and dysfunction. Investigating amyloid material in its natural environment is crucial to obtain new insights on the molecular features of fibrillar deposits at individual level. To this aim, we used Fourier transform infrared (FTIR) microspectroscopy for studying
in situ
unfixed tissues (heart and subcutaneous abdominal fat) from patients affected by AL amyloidosis. We compared the infrared response of affected tissues with that of
ex vivo
and
in vitro
fibrils obtained from the pathogenic LC derived from one patient, as well as with that of non amyloid-affected tissues. We demonstrated that the IR marker band of intermolecular β-sheets, typical of protein aggregates, can be detected
in situ
in LC amyloid-affected tissues, and that FTIR microspectroscopy allows exploring the inter- and intra-sample heterogeneity. We extended the infrared analysis to the characterization of other biomolecules embedded within the amyloid deposits, finding an IR pattern that discloses a possible role of lipids, collagen and glycosaminoglycans in amyloid deposition
in vivo
.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Amyloidogenic Proteins - chemistry
/ Amyloidogenic Proteins - metabolism
/ Biopsy
/ Body fat
/ Female
/ Heart
/ Humanities and Social Sciences
/ Humans
/ Immunoglobulin Light Chains - chemistry
/ Immunoglobulin Light Chains - metabolism
/ Immunoglobulin Light-chain Amyloidosis - metabolism
/ Immunoglobulin Light-chain Amyloidosis - pathology
/ Kidneys
/ Lipids
/ Male
/ Plaque, Amyloid - metabolism
/ Protein Aggregation, Pathological - metabolism
/ Protein Conformation, beta-Strand
/ Proteins
/ Science
/ Spectroscopy, Fourier Transform Infrared
/ Tissues
