Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detection of immunoglobulin light chain amyloidosis

Hoshii, Yoshinobu; Setoguchi, Mihoko; Iwata, Takako; Ueda, Junko; Cui, Dan; Kawano, Hiroyuki; Gondo, Toshikazu; Takahashi, Mutsuo; Ishihara, Tokuhiro

doi:10.1046/j.1440-1827.2001.01198.x

Cited by 70 publications

(50 citation statements)

References 26 publications

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“…The degree of amyloidosis was divided into three categories and evaluated semiquantitatively [12,13] [15], anti-AA [16] and anti-TTR (115-124) [17] antibodies were applied to the sections as primary antibodies for 30 min at room temperature. The sections were then incubated with EnVision+ (Dako) as the secondary antibody for 30 min at room temperature.…”

Section: Congo Red and Immunohistochemical Analysismentioning

confidence: 99%

High prevalence of wild-type transthyretin deposition in patients with idiopathic carpal tunnel syndrome: a common cause of carpal tunnel syndrome in the elderly

et al. 2011

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SummaryCarpal tunnel syndrome is the most common type of entrapment neuropathy. However, the cause of carpal tunnel syndrome remains unclear in most cases. Senile systemic amyloidosis, induced by wild-type transthyretin deposition, is a prevalent aging-related disorder and often accompanied by carpal tunnel syndrome. In this study, we measured the frequency of unrecognized wild-type transthyretin deposition in idiopathic carpal tunnel syndrome patients.One-hundred and twenty-three patients with carpal tunnel syndrome, including 100 idiopathic patients, treated by carpal tunnel release surgery were analyzed. Tenosynovial tissues obtained at surgery were analyzed by Congo red and immunohistochemical staining. If staining for transthyretin was positive, the entire TTR gene was analyzed by direct DNA sequencing. We also analyzed tenosynovial tissues from 32 autopsy cases as controls. Thirty-four (34.0%) patients with idiopathic carpal tunnel syndrome showed amyloid deposition in the tenosynovial tissue, and all amyloid showed specific immunolabelling with anti-transthyretin antibody. Direct DNA sequencing of the entire TTR gene did not reveal any mutations, indicating that all amyloid deposits were derived form wild-type transthyretin. Statistical analysis using logistic regression showed that the prevalence of transthyretin deposition in the idiopathic carpal tunnel syndrome group was significantly higher than that in controls (odds ratio 15.8, 95% CI 3.3-75.7), and age and male gender were independent risk factors for transthyretin amyloid deposition. Our results demonstrate that wild-type transthyretin deposition is a common cause of carpal tunnel syndrome in elderly men. It is likely that many patients develop carpal tunnel syndrome as an initial symptom of senile systemic amyloidosis.4

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Section: Congo Red and Immunohistochemical Analysismentioning

confidence: 99%

High prevalence of wild-type transthyretin deposition in patients with idiopathic carpal tunnel syndrome: a common cause of carpal tunnel syndrome in the elderly

et al. 2011

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“…To make a correct diagnosis, proven amyloid deposition in biopsy specimens is an initial step and immunohistochemical staining with antibodies to diverse amyloid fibril proteins is necessary for the classification of the different forms of amyloidosis (7). Additionally, gene analysis of amyloid precursor proteins is required in hereditary amyloidosis (8) (Fig.…”

Section: Classification Of Amyloidosismentioning

confidence: 99%

Cardiac Amyloidosis: Heterogenous Pathogenic Backgrounds

Ikeda

2004

Intern. Med.

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Cardiac amyloidosis is a fatal disorder which develops on the basis of the different pathologic conditions in systemic amyloidosis: the most common underlying disease is immunoglobulin light chain-derived primary amyloidosis and the next is transthyretin-related hereditary amyloidosis; the latter disorder, typically represented by familial amyloid polyneuropathy, was long regarded as an endemic disease. However, this disorder has now been shown to involve a highly variable clinical picture due to a large number of transthyretin gene mutations, and many patients with diverse ancestors suffer from severe cardiac amyloidosis. Additionally, senile systemic amyloidosis is now noted as a cause of cardiac dysfunction in elderly individuals. Echocardiogram and myocardial technetium-99m-pyrophosphate scintigraphy can provide characteristic findings. Immunohistochemistry on tissue amyloid, biochemical analysis of serum and urine proteins, and DNA sequencing are usually employed to determine the disease-related amyloid fibril protein.Although systemic amyloidosis has become treatable, the prognosis of each patient who received up-to-date and effective, but nevertheless stressful, therapy depends on the severity of cardiac involvement by amyloid deposition.

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“…It has been previously reported that in some cases, the monoclonal deposition of IgG κ in glomeruli can be masked [15]. Although Hoshii et al generated new antibodies against the immunoglobulin light chain constant and variable region in AL amyloid [16,17], this technique is difficult to use in routine pathological studies. However, the use of the LCMS/MS proteomic analysis can compensate for these limitations in the detection of amyloid protein that occur when using these routine pathological techniques.…”

Section: Discussionmentioning

confidence: 99%

Optimal conditions and the advantages of using laser microdissection and liquid chromatography tandem mass spectrometry for diagnosing renal amyloidosis

et al. 2018

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Background Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has recently been utilized to accurately detect the amyloid proteins of renal amyloidosis. The present study investigated the optimal procedures for analyzing samples by LCMS/MS, and the advantage of using this technique to diagnosis renal amyloidosis. Methods To detect amyloid proteins, laser microdissected glomeruli from AL (n = 13) or AA (n = 10) renal amyloidosis patients were digested and analyzed by LCMS/MS. To determine the best procedures for analyzing samples by LCMS/MS, we examined the suitability of tissue samples, frozen or formalin-fixed paraffin-embedded (FFPE), the number of dissected glomeruli required for analysis (2, 10, or 50 glomeruli), and the amount of trypsin with or without dithiothreitol (DTT). We additionally compared the detection of amyloid proteins between immunostaining and LCMS/MS. Results Examining 10 dissected glomeruli from FFPE sections digested with trypsin 3 µL (0.1 mg/mL) without DDT made it possible to detect amyloid protein in all 10 AA and in 10 out of 12 AL amyloidosis cases. All AA amyloidosis cases were diagnosed using immunohistochemistry for amyloid A. With immunostaining, however, there were several inconclusive immunoglobulin and/or their light chain staining noted in the AA or AL amyloidosis cases. Even so, LCMS/MS was able to accurately detect amyloid protein in renal amyloidosis. Conclusion The use of 10 laser microdissected glomeruli (170,000-220,000 µm 2 ) with amyloid deposition from FFPE sections digested with trypsin 3 µL (0.1 mg/mL) allowed the accurate detection of amyloid protein in AA and AL amyloidosis.

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Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detection of immunoglobulin light chain amyloidosis

Cited by 70 publications

References 26 publications

High prevalence of wild-type transthyretin deposition in patients with idiopathic carpal tunnel syndrome: a common cause of carpal tunnel syndrome in the elderly

High prevalence of wild-type transthyretin deposition in patients with idiopathic carpal tunnel syndrome: a common cause of carpal tunnel syndrome in the elderly

Cardiac Amyloidosis: Heterogenous Pathogenic Backgrounds

Optimal conditions and the advantages of using laser microdissection and liquid chromatography tandem mass spectrometry for diagnosing renal amyloidosis

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