Marked and Rapid Regression of Hepatic Amyloid Deposition in a Patient with Systemic Light Chain (AL) Amyloidosis after High-dose Melphalan Therapy with Stem Cell Transplantation

Katoh, Nagaaki; Matsushima, Akira; Kurozumi, Masahiro; Matsuda, Masayuki; Ikeda, Shu‐ichi

doi:10.2169/internalmedicine.53.2065

Cited by 11 publications

(7 citation statements)

References 23 publications

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“…Asian and European patients with Aα-chain amyloidosis do not show remarkable differences with respect to clinical manifestations; however, the most prevalent genetic variant E526V in European patients may not be common in Asian patients. Recently, several effective therapies have been established for treating different types of systemic amyloidosis; however, the therapeutic strategy for treating each type of amyloidosis is different [ 13 , 17 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 ] ( Table 2 ), highlighting the importance of the correct diagnosis of the disease at an early stage. Moreover, the possibility of Aα-chain amyloidosis should always be considered in sporadic cases of amyloid nephropathy, even in Asian countries.…”

Section: Discussionmentioning

confidence: 99%

Hereditary Fibrinogen Aα-Chain Amyloidosis in Asia: Clinical and Molecular Characteristics

Yazaki

Yoshinaga

Sekijima

et al. 2018

IJMS

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Hereditary fibrinogen Aα-chain amyloidosis (Aα-chain amyloidosis) is a type of autosomal dominant systemic amyloidosis caused by mutations in fibrinogen Aα-chain gene (FGA). Patients with Aα-chain amyloidosis have been mainly reported in Western countries but have been rarely reported in Asia, with only five patients with Aα-chain amyloidosis being reported in Korea, China, and Japan. Clinically, the most prominent manifestation in Asian patients with Aα-chain amyloidosis is progressive nephropathy caused by excessive amyloid deposition in the glomeruli, which is similar to that observed in patients with Aα-chain amyloidosis in Western countries. In molecular features in Asian Aα-chain amyloidosis, the most common variant, E526V, was found in only one Chinese kindred, and other four kindred each had a different variant, which have not been identified in other countries. These variants are located in the C-terminal region (amino acid residues 517–555) of mature Aα-chain, which was similar to that observed in patients with Aα-chain amyloidosis in other countries. The precise number of Asian patients with Aα-chain amyloidosis is unclear. However, patients with Aα-chain amyloidosis do exist in Asian countries, and the majority of these patients may be diagnosed with other types of systemic amyloidosis.

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Section: Discussionmentioning

confidence: 99%

Hereditary Fibrinogen Aα-Chain Amyloidosis in Asia: Clinical and Molecular Characteristics

Yazaki

Yoshinaga

Sekijima

et al. 2018

IJMS

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“…However, most of them may have been misdiagnosed with other types of systemic amyloidosis. Recently, several effective therapies have been established, especially for AL amyloidosis or AA amyloidosis (27)(28)(29). In AApoAI amyloidosis, organ transplantation, including that of the kidney, liver, or heart, has been performed as a promising therapy (30).…”

Section: Discussionmentioning

confidence: 99%

Giant Hepatomegaly with Spleno-testicular Enlargement in a Patient with Apolipoprotein A-I Amyloidosis: An Uncommon Type of Amyloidosis in Japan

et al. 2021

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Hereditary systemic amyloidosis aside from transthyretin-related familial amyloid polyneuropathy is quite uncommon in Japan. We herein report a sporadic case of hereditary apolipoprotein A-I (apoAI) amyloidosis. The patient was a 43-year-old Japanese man who exhibited marked hepatomegaly with spleno-testicular enlargement. While he was initially thought to have primary AL amyloidosis, a proteomics analysis revealed that the amyloid was composed of variant apoAI with an E34K variant. To date, only one patient with apoAI amyloidosis has been reported in Japan. However, our study suggests that more patients may be present in Japan, and the majority may have been diagnosed with other types of amyloidosis due to its clinical similarity.

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“…The formation of amyloid fibrils is a dynamic process, with monomers and oligomers being rapidly exchanged for each other depending on various factors that include pH, temperature, and co-solvents [ 34 ]. According to studies of serial biopsy specimens obtained from AL, ATTR, and AA amyloidosis patients, even mature amyloid fibril masses disappear when successful disease-modifying therapies are provided [ 35 , 36 , 37 ]. Electron microscope studies have demonstrated the appearance of dotty or globular structures 4 to 5 nm in diameter and the subsequent formation of short protofibrils 30 to 100 nm in length during an incubation of Aβ in vitro [ 38 ].…”

Section: Initiation Of Protein Aggregationmentioning

confidence: 99%

Significance of Oligomeric and Fibrillar Species in Amyloidosis: Insights into Pathophysiology and Treatment

et al. 2021

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Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or whether, amyloid fibrils contribute to tissue damage in amyloidosis has been the topic of debate. In vitro studies have demonstrated the appearance of small globular oligomeric species during the incubation of amyloid beta peptide (Aβ). Nerve biopsy specimens from patients with systemic amyloidosis have suggested that globular structures similar to Aβ oligomers were generated from amorphous electron-dense materials and later developed into mature amyloid fibrils. Schwann cells adjacent to amyloid fibrils become atrophic and degenerative, suggesting that the direct tissue damage induced by amyloid fibrils plays an important role in systemic amyloidosis. In contrast, there is increasing evidence that oligomers, rather than amyloid fibrils, are responsible for cell death in neurodegenerative diseases, particularly Alzheimer’s disease. Disease-modifying therapies based on the pathophysiology of amyloidosis have now become available. Aducanumab, a human monoclonal antibody against the aggregated form of Aβ, was recently approved for Alzheimer’s disease, and other monoclonal antibodies, including gantenerumab, solanezumab, and lecanemab, could also be up for approval. As many other agents for amyloidosis will be developed in the future, studies to develop sensitive clinical scales for identifying improvement and markers that can act as surrogates for clinical scales should be conducted.

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Marked and Rapid Regression of Hepatic Amyloid Deposition in a Patient with Systemic Light Chain (AL) Amyloidosis after High-dose Melphalan Therapy with Stem Cell Transplantation

Cited by 11 publications

References 23 publications

Hereditary Fibrinogen Aα-Chain Amyloidosis in Asia: Clinical and Molecular Characteristics

Hereditary Fibrinogen Aα-Chain Amyloidosis in Asia: Clinical and Molecular Characteristics

Giant Hepatomegaly with Spleno-testicular Enlargement in a Patient with Apolipoprotein A-I Amyloidosis: An Uncommon Type of Amyloidosis in Japan

Significance of Oligomeric and Fibrillar Species in Amyloidosis: Insights into Pathophysiology and Treatment

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