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.
Ami, D., Lavatelli, F., Rognoni, P., Palladini, G., Raimondi, S., Giorgetti, S., et al. (2016). In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study. SCIENTIFIC REPORTS, 6 [10.1038/srep29096].
Citazione: | Ami, D., Lavatelli, F., Rognoni, P., Palladini, G., Raimondi, S., Giorgetti, S., et al. (2016). In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study. SCIENTIFIC REPORTS, 6 [10.1038/srep29096]. | |
Tipo: | Articolo in rivista - Articolo scientifico | |
Carattere della pubblicazione: | Scientifica | |
Presenza di un coautore afferente ad Istituzioni straniere: | No | |
Titolo: | In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study | |
Autori: | Ami, D; Lavatelli, F; Rognoni, P; Palladini, G; Raimondi, S; Giorgetti, S; Monti, L; Doglia, S; Natalello, A; Merlini, G | |
Autori: | NATALELLO, ANTONINO (Penultimo) | |
Data di pubblicazione: | 2016 | |
Lingua: | English | |
Rivista: | SCIENTIFIC REPORTS | |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1038/srep29096 | |
Appare nelle tipologie: | 01 - Articolo su rivista |
File in questo prodotto:
File | Descrizione | Tipologia | Licenza | |
---|---|---|---|---|
srep29096_In situ characterization.pdf | Articolo principale | Publisher's version | Open Access Visualizza/Apri | |
41598_2016_BFsrep29096_MOESM32_ESMIn situ characterization.pdf | dati supplementari | Publisher's version | Open Access Visualizza/Apri |