Usefulness of labial salivary gland biopsy in familial amyloid polyneuropathy Portuguese type

Amaral, Barbas do; Coelho, Teresa; Sousa, Alda; Guimarães, António

doi:10.3109/13506120903421850

Cited by 61 publications

(39 citation statements)

References 21 publications

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“…As expected (40), amyloid fibrils in the salivary gland were localized around glandular acini as revealed by thioflavin T fluorescence (Fig. 2C top left panel, white arrows, and fig.…”

Section: Resultssupporting

confidence: 84%

“…( C ) Probe B-1-Biotin labeling of salivary gland biopsies of a FAP patient (n=2; left panel) and a non-FAP control (n=2; right panel). Arrows indicate regions with amyloid fibrils (around the glandular acini in the patient sample (40)), stained by thioflavin T (ThT; top row) and the anti-TTR antibody (anti-TTR-Alexa594; third row) not labeled by probe B-1-Biotin (B-1-Alexa594; second row). Asterisks indicate regions inside the glandular acini that are labeled by B-1-Biotin in both the patient and the control samples.…”

Section: Figmentioning

confidence: 99%

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Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients

et al. 2017

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Increasing evidence supports the hypothesis that soluble misfolded protein assemblies contribute to the degeneration of post-mitotic tissue in amyloid diseases. However, there is a dearth of reliable non-antibody based probes for selectively detecting oligomeric aggregate structures circulating in plasma or deposited in tissues, making it difficult to scrutinize this hypothesis in patients. Hence, understanding the structure-proteotoxicity relationships driving amyloid diseases remains challenging, hampering the development of early diagnostic and novel treatment strategies. Here, we report peptide-based probes that selectively label misfolded transthyretin (TTR) oligomers circulating in the plasma of TTR hereditary amyloidosis patients exhibiting a predominant neuropathic phenotype. These probes revealed that there are much fewer misfolded TTR oligomers in healthy controls, in asymptomatic carriers of mutations linked to amyloid polyneuropathy, and in patients with TTR-associated cardiomyopathies. The absence of misfolded TTR oligomers in the plasma of cardiomyopathy patients suggests that the tissue tropism observed in the TTR amyloidoses is structure based. Misfolded oligomers decrease in TTR amyloid polyneuropathy patients treated with disease-modifying therapies (tafamidis or liver transplant-mediated gene therapy). In a subset of TTR amyloid polyneuropathy patients, the probes also detected a circulating TTR fragment that disappeared after tafamidis treatment. Proteomic analysis of the isolated TTR oligomers revealed a specific patient associated-signature comprised of proteins that likely associate with the circulating TTR oligomers. Quantification of plasma oligomer concentrations using peptide probes could become an early diagnostic strategy, a response-to-therapy biomarker, and a useful tool for understanding structure-proteotoxicity relationships in the TTR amyloidoses.

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“…As expected (40), amyloid fibrils in the salivary gland were localized around glandular acini as revealed by thioflavin T fluorescence (Fig. 2C top left panel, white arrows, and fig.…”

Section: Resultssupporting

confidence: 84%

Section: Figmentioning

confidence: 99%

Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients

et al. 2017

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“…The diagnostic sensitivity of fat pad examination is high (70%-80% overall) [59] and acquisition of this tissue by fine needle biopsy is substantially innocuous, rapid and inexpensive. If clinical suspicion stands despite a negative fat pad biopsy, examination of minor labial salivary glands [61,62] can be considered the preferred second step (being positive in > 50% of patients with negative fat pad) [61]. This procedure has also high sensitivity for detecting amyloid deposits in subjects with molecular diagnosis of variant TTR [62].…”

Section: Detection Of Amyloid Deposits In Tissuesmentioning

confidence: 99%

Biochemical markers in early diagnosis and management of systemic amyloidoses

Lavatelli

Albertini

Fonzo

et al. 2014

Clinical Chemistry and Laboratory Medicine (CCLM)

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Systemic amyloid diseases are characterized by widespread protein deposition as amyloid fibrils. Precise diagnostic framing is the prerequisite for a correct management of patients. This complex process is achieved through a series of steps, which include detection of the tissue amyloid deposits, identification of the amyloid type, demonstration of the amyloidogenic precursor, and evaluation of organ dysfunction/damage. Laboratory medicine plays a central role in the diagnosis and management of systemic amyloidoses, through the quantification of the amyloidogenic precursor and evaluation of end-organ damage using biomarkers.

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“…Moreover, the high degree of deposits was present in the first stage of FAP: 1.5 years in the first patient and 6 months in the second. 6 For these reasons, we suggest nasal mucosa as a suitable site for tissue biopsy in patients with suspected hereditary TTR amyloidosis.…”

Section: Discussionmentioning

confidence: 99%

Nasal mucosa: A new site for tissue biopsy to diagnose hereditary TTR amyloidosis

Munar-Qués¹,

Solé

Martínez-Nadal

et al. 2014

Medicina Clínica

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Usefulness of labial salivary gland biopsy in familial amyloid polyneuropathy Portuguese type

Cited by 61 publications

References 21 publications

Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients

Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients

Biochemical markers in early diagnosis and management of systemic amyloidoses

Nasal mucosa: A new site for tissue biopsy to diagnose hereditary TTR amyloidosis

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