ReviewCritical reviews in biochemistry and molecular biology
Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.
Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 110 citations in OpenAlex.
- Facial Weakness Revealing Rare Familial Polyneuropathy.Annals of neurology · 2026Article
- Finnish Variant of Gelsolin Amyloidosis in a South Indian Family: Clinical, Genetic, Ophthalmological, and Histopathological Findings.Annals of Indian Academy of Neurology · 2026Article
- A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026Review
- Gelsolin amyloidosis presenting with nephrotic syndrome: a case report and molecular insights.Frontiers in medicine · 2026Article
- Renal gelsolin amyloidosis as a rare cause of proteinuria: a case report and literature review.BMC nephrology · 2025Review
- VDAC1-interacting proteins: binding site mapping and their derived peptides induce apoptosis and multifaceted cellular effects.Apoptosis : an international journal on programmed cell death · 2025Article
- Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- First Reported Case of Dual Hereditary Gelsolin and Transthyretin Wild-Type Cardiac Amyloidosis in a Man in his late 40s.Mayo Clinic proceedings. Innovations, quality & outcomes · 2025Article
- A novel heterozygous mutation in the gelsolin gene causes Finnish gelsolin amyloidosis associated with nephropathy and thrombotic microangiopathy.Archives of medical science : AMS · 2025Article
- Evidence for SbioRxiv : the preprint server for biology · 2024Article
- Advancing Renal Amyloidosis Care: The Role of Modern Diagnostic Techniques with the Potential of Enhancing Patient Outcomes.International journal of molecular sciences · 2024Review
- Dynamic Reconstruction Using Bilateral Lengthening Temporalis Myoplasty for Facial Palsies in Patients with Hereditary Skin Laxity.Plastic and reconstructive surgery. Global open · 2024Article
- Viruses and amyloids - a vicious liaison.Prion · 2023Review
- Accurate and Efficient SAXS/SANS Implementation Including Solvation Layer Effects Suitable for Molecular Simulations.Journal of chemical theory and computation · 2023Article
- Clinical considerations in early-onset cerebral amyloid angiopathy.Brain : a journal of neurology · 2023Review
- Familial amyloidosis of the Finnish type: clinical and neurophysiological features of two index cases.BMJ case reports · 2022Article
- Report of two pedigrees with heterozygous HTRA1 variants-related cerebral small vessel disease and literature review.Molecular genetics & genomic medicine · 2022Review
- Sequence grammar underlying the unfolding and phase separation of globular proteins.Molecular cell · 2022Article
- Cluster-Assembled Nanoporous Super-Hydrophilic Smart Surfaces for On-Target Capturing and Processing of Biological Samples for Multi-Dimensional MALDI-MS.Molecules (Basel, Switzerland) · 2022Article
- Hearing problems in patients with hereditary gelsolin amyloidosis.Orphanet journal of rare diseases · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein misassembly into aggregate structures, including cross-β-sheet amyloid fibrils, is linked to diseases characterized by the degeneration of post-mitotic tissue. While amyloid fibril deposition in the extracellular space certainly disrupts cellular and tissue architecture late in the course of amyloid diseases, strong genetic, pathological and pharmacologic evidence suggests that the process of amyloid fibril formation itself, known as amyloidogenesis, likely causes these maladies. It seems that the formation of oligomeric aggregates during the amyloidogenesis process causes the proteotoxicity and cytotoxicity characteristic of these disorders. Herein, we review what is known about the genetics, biochemistry and pathology of familial amyloidosis of Finnish type (FAF) or gelsolin amyloidosis. Briefly, autosomal dominant D187N or D187Y mutations compromise Ca(2+) binding in domain 2 of gelsolin, allowing domain 2 to sample unfolded conformations. When domain 2 is unfolded, gelsolin is subject to aberrant furin endoproteolysis as it passes through the Golgi on its way to the extracellular space. The resulting C-terminal 68 kDa fragment (C68) is susceptible to extracellular endoproteolytic events, possibly mediated by a matrix metalloprotease, affording 8 and 5 kDa amyloidogenic fragments of gelsolin. These amyloidogenic fragments deposit systemically, causing a variety of symptoms including corneal lattice dystrophy and neurodegeneration. The first murine model of the disease recapitulates the aberrant processing of mutant plasma gelsolin, amyloid deposition, and the degenerative phenotype. We use what we have learned from our biochemical studies, as well as insight from mouse and human pathology to propose therapeutic strategies that may halt the progression of FAF.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.