Investigating the Pathogenic Role of N-glycosylation in AL Amyloidosis: Molecular Bases, Diagnosis, and Treatment

Recruiting now

Conditions studied: AL Amyloidosis, MGUS, Multiple Myeloma, Monoclonal Gammopathies

In brief

Immunoglobulin light chain (AL) amyloidosis is caused by a typically small, minimally proliferating bone marrow plasma cell clone secreting a patient-unique, unstable, aggregation-prone, toxic light chain (LC). The amyloidogenicity of LCs is encrypted in their sequence, yet molecular determinants of LC pathogenicity remain obscure. N-glycosylation has been long suspected to be a determinant of LC amyloidogenicity based on anecdotal reports of individual AL patients with a clonal LC displaying this post-translational modification. It is hypothesized that N-glycosylation fundamentally contributes to determining the amyloidogenicity of immunoglobulin LCs in a subset of patients with AL and might influence its clinical phenotype. It is further proposed that the synthesis and secretion of unstable LCs that also have to be N-glycosylated might reverberate on the biology of the plasma cell clone, possibly modulating the sensitivity toward different drugs and might represent itself a therapeutic target. The objective of our study is now to elucidate the molecular role of LC N-glycosylation in AL amyloidosis, exploit it for risk assessment, and define its potential impact on the biology of the underlying plasma cell clone and its drug sensitivity.

Key facts

Study ID
NCT07448779
Run by
Fondazione IRCCS Policlinico San Matteo di Pavia
People needed
100
Starts
2025-11-17
Expected to finish
2027-05-30
Last updated by the study team
2026-03-04

Who can join

Age: 18 and older, up to 99. Sex: any. Healthy volunteers: not accepted.

You may qualify if…

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Where it is running

Full record on ClinicalTrials.gov

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