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Inflammatory disorders of the larynx
Published in Declan Costello, Guri Sandhu, Practical Laryngology, 2015
The mainstay of diagnosis is obtaining a biopsy from an affected site. Amyloidosis displays a pathognomonic apple green birefringence on microscopy under polarised light after being stained with Congo red dye.14 Other investigations should focus around excluding other system involvement. A serum amyloid P component scan is one such test, whereby radiolabelled protein is injected into patients to locate areas of amyloid deposition.
Mechanisms of Fibril Formation and Cellular Response
Published in Martha Skinner, John L. Berk, Lawreen H. Connors, David C. Seldin, XIth International Symposium on Amyloidosis, 2007
Martha Skinner, John L. Berk, Lawreen H. Connors, David C. Seldin
Serum amyloid P component (SAP) binds to amyloid deposits. 123I-labeled SAP is used in scintigraphy to detect amyloid and to determine the extent and distribution of amyloid deposits in systemic amyloidosis (1-3). Objective of the study was to assess the diagnostic accuracy and prognostic value of a simple parameter describing 123I-SAP body retention in systemic and localized amyloidosis.
Scintigraphy at Different Time Intervals after Administration of 123I Labelled Serum Amyloid P Component (SAP) in Patients with Amyloidosis
Published in Gilles Grateau, Robert A. Kyle, Martha Skinner, Amyloid and Amyloidosis, 2004
B.P.C. Hazenberg, P.L. Jager, D.A. Piers, P.C. Limburg, M.N. de Hooge, M.H. van Rijswijk
AA amyloidosis is sometimes seen in longstanding arthritis. Early detection is important for prognosis. Scintigraphy with 123I labelled serum amyloid P component (SAP) may be helpful to detect amyloidosis in patients suspected to have amyloidosis (1).
A case of asymmetric insulin-derived localised amyloid deposition associated with long-acting insulin analog administration
Published in Amyloid, 2022
Keiji Hirai, Shigeki Imamura, Aizan Hirai, Naoka Umemoto, Hisashi Oshiro, Fuyuki Kametani, Nagaaki Katoh, Masahide Yazaki, Susumu Ookawara, Yoshiyuki Morishita
Insulin-derived amyloidosis is a rare complication of insulin therapy that occurs in long-term insulin users at sites of repeated insulin injection [1]. It is observed as a hard subcutaneous mass that has higher radiodensity than the surrounding subcutaneous adipose tissue [2]. Insulin-derived amyloid can be demonstrated by amyloid staining and immunostaining using anti-insulin antibody [1]. It has been reported that other amyloid precursor proteins such as apolipoproteins A-I, A-IV, E, and serum amyloid P-component are associated with insulin-derived amyloid [3]. In our case, the radiodensity of the mass was indeed higher than that of the surrounding adipose tissue and the specimen was positive for Congo red and anti-insulin antibody immunohistochemistry staining. Peptides consistent with insulin, apolipoproteins A-I, A-IV, E, and serum amyloid P-component were detected in the amyloid deposition area. These findings of our case are consistent with those of previous reports [1–3].
The discovery of protein biomarkers in pre-eclampsia: the promising role of mass spectrometry
Published in Biomarkers, 2018
Of note, conflicting results of the level of some altered proteins have been reported by different studies. Blankley et al. (Blankley et al. 2009) revealed higher level of serum amyloid P-component in the plasma of pre-eclamptic women compared to controls, while Liu et al. (Liu et al. 2011) observed lower level of the same protein in a similar study. Generally, disagreement in the literature might be due to various reasons such as different patient populations and selection criteria, patients’ heterogeneity, and the diverse methodologies and workflow followed in sample processing and analysis.
Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies
Published in Amyloid, 2021
Jonathan Schönfelder, Peter Benedikt Pfeiffer, Tejaswini Pradhan, Johan Bijzet, Bouke P. C. Hazenberg, Stefan O. Schönland, Ute Hegenbart, Bernd Reif, Christian Haupt, Marcus Fändrich
To interrogate the possible molecular basis of this effect we analysed the possible contributions of serum amyloid P component (SAP). Similar to previous analyses which showed that ex vivo fibrils can contain SAP [17], we find significant amounts of SAP in our ex vivo fibrils, and specifically in ATTR amyloid fibrils (Figure 1). Western Blot-based quantifications of SAP in samples containing 200 µg/mL fibril protein revealed SAP concentration of 38.2 ± 1.5 µg/mL for the three samples of ATTR amyloid fibrils and of 3.4 ± 2.3 µg/mL for the four samples of human AA and AL amyloidosis (Figure S4).