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Methods in Enzymology 2006Scintigraphic imaging of radioiodinated serum amyloid P-component is a proven method for the clinical detection of peripheral amyloid deposits (Hawkins et al., 1990).... (Review)
Review
Scintigraphic imaging of radioiodinated serum amyloid P-component is a proven method for the clinical detection of peripheral amyloid deposits (Hawkins et al., 1990). However, the inability to perform comparably high-resolution studies in experimental animal models of amyloid disease has impacted not only basic studies into the pathogenesis of amyloidosis but also in the preclinical in vivo evaluation of potential anti-amyloid therapeutic agents. We have developed microimaging technologies, implemented novel computational methods, and established protocols to generate high-resolution images of amyloid deposits in mice. (125)I-labeled serum amyloid P component (SAP) and an amyloid-fibril reactive murine monoclonal antibody (designated 11-1F4) have been used successfully to acquire high-resolution single photon emission computed tomographic (SPECT) images that, when fused with x-ray computed tomographic (CT) data, have provided precise anatomical localization of secondary (AA) and primary (AL) amyloid deposits in mouse models of these diseases. This chapter will provide detailed protocols for the radioiodination and purification of amyloidophilic proteins and the generation of mouse models of AA and AL amyloidosis. A brief description of the available hardware and the parameters used to acquire high-resolution microSPECT and CT images is presented, and the tools used to perform image reconstruction and visualization that permit the analysis and presentation of image data are discussed. Finally, we provide established methods for measuring organ- and tissue-specific activities with which to corroborate the microSPECT and CT images.
Topics: Amyloid; Amyloidosis; Animals; Humans; Iodine Radioisotopes; Mice; Mice, Transgenic; Serum Amyloid P-Component; Tomography, Emission-Computed, Single-Photon
PubMed: 17046658
DOI: 10.1016/S0076-6879(06)12011-X -
The FEBS Journal Dec 2005Alzheimer's disease and Creutzfeldt-Jakob disease are the best-known examples of a group of diseases known as the amyloidoses. They are characterized by the... (Review)
Review
Alzheimer's disease and Creutzfeldt-Jakob disease are the best-known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the rational design of drugs to inhibit or reverse amyloid formation. Structural models have been built using information from a wide variety of techniques, including X-ray diffraction, electron microscopy, solid state NMR and EPR. Recent advances have been made in understanding the architecture of the amyloid fibril. Here, we describe and compare postulated structural models for the mature amyloid fibril and discuss how the ordered structure of amyloid contributes to its stability.
Topics: Alzheimer Disease; Amyloid; Amyloidosis; Creutzfeldt-Jakob Syndrome; Humans; Models, Molecular; Molecular Structure; Protein Conformation; X-Ray Diffraction
PubMed: 16302960
DOI: 10.1111/j.1742-4658.2005.05025.x -
Molecules (Basel, Switzerland) Nov 2021Renal amyloidosis typically manifests albuminuria, nephrotic-range proteinuria, and ultimately progresses to end-stage renal failure if diagnosed late. Different types...
Renal amyloidosis typically manifests albuminuria, nephrotic-range proteinuria, and ultimately progresses to end-stage renal failure if diagnosed late. Different types of renal amyloidosis have completely different treatments and outcomes. Therefore, amyloidosis typing is essential for disease prognosis, genetic counseling and treatment. Thirty-six distinct proteins currently known to cause amyloidosis that have been described as amyloidogenic precursors, immunohistochemistry (IHC) or immunofluorescence (IF), can be challenging for amyloidosis typing especially in rare or hereditary amyloidosis in clinical practice. We made a pilot study that optimized the proteomics pre-processing procedures for trace renal amyloidosis formalin-fixed paraffin-embedded (FFPE) tissue samples, combined with statistical and bioinformatics analysis to screen out the amyloidosis-related proteins to accurately type or subtype renal amyloidosis in order to achieve individual treatment. A sensitive, specific and reliable FFPE-based proteomics analysis for trace sample manipulation was developed for amyloidosis typing. Our results not only underlined the great promise of traditional proteomics and bioinformatics analysis using FFPE tissues for amyloidosis typing, but also proved that retrospective diagnosis and analysis of previous cases laid a solid foundation for personalized treatment.
Topics: Amyloidosis; Base Sequence; Case-Control Studies; Formaldehyde; Humans; Kidney; Mass Spectrometry; Muramidase; Paraffin Embedding; Pilot Projects; Proteomics; Tissue Fixation
PubMed: 34885818
DOI: 10.3390/molecules26237234 -
The British Journal of Ophthalmology Jul 1970
Topics: Amyloidosis; Biopsy; Chondroma; Conjunctiva; Diagnosis, Differential; Exophthalmos; Eye Diseases; Humans; Male; Middle Aged; Orbit
PubMed: 5433348
DOI: 10.1136/bjo.54.7.445 -
Ear, Nose, & Throat Journal Sep 2021Amyloidosis is a heterogeneous group of diseases characterized by the extracellular deposition of insoluble proteins whose pathogenesis is not yet fully understood. The...
Amyloidosis is a heterogeneous group of diseases characterized by the extracellular deposition of insoluble proteins whose pathogenesis is not yet fully understood. The deposition of amyloid proteins can be systemic or localized, idiopathic or related to systemic diseases, mostly multiple myeloma or chronic inflammatory diseases. Localized head and neck amyloidosis is a rare entity, mainly involving the larynx. Given the rarity of the disease and the absence of a lasting follow-up protocol, there is no standard treatment defined for localized amyloidosis. We report a rare case of localized nasopharyngeal amyloidosis, treated with complete transoral resection and confirmed by histological examination.
Topics: Aged, 80 and over; Amyloidosis; Female; Humans; Medical Illustration; Nasopharyngeal Diseases; Nasopharynx
PubMed: 32228034
DOI: 10.1177/0145561320914432 -
Journal of Clinical Pathology Aug 1972Amyloid goitre is a rare manifestation of amyloidosis; about 50 cases have been recorded and this paper adds a further six cases, the first to be described from Uganda....
Amyloid goitre is a rare manifestation of amyloidosis; about 50 cases have been recorded and this paper adds a further six cases, the first to be described from Uganda. The condition has to be distinguished from the more common types of goitre, and histological differentiation from medullary carcinoma may be difficult with small biopsies. Irrespective of an underlying cause, the distribution of amyloidosis in Uganda resembles the classical secondary type, and the findings in 81 cases confirm this. The age of onset of the primary type is earlier than seen elsewhere and it is possible that these variations result from immune depression following malnutrition or endemic infectious diseases.
Topics: Adult; Age Factors; Aged; Amyloidosis; Autopsy; Biopsy; Carcinoma; Diagnosis, Differential; Female; Foreign Bodies; Goiter; Histocytochemistry; Humans; Infections; Male; Middle Aged; Nutrition Disorders; Thyroid Gland; Thyroidectomy; Uganda
PubMed: 5076803
DOI: 10.1136/jcp.25.8.683 -
European Heart Journal. Cardiovascular... Aug 2023Myocardial longitudinal strain (LS) by two-dimensional (2D) speckle-tracking echocardiography has a diagnostic and prognostic role in cardiac amyloidosis (CA)....
AIMS
Myocardial longitudinal strain (LS) by two-dimensional (2D) speckle-tracking echocardiography has a diagnostic and prognostic role in cardiac amyloidosis (CA). Typically, the apical segments of the left ventricle (LV) are less affected by LS abnormalities, a finding called relative apical sparing (RELAPS). Whether a variable burden of CA might explain the RELAPS remains unknown.We aimed to evaluate the extent, distribution, and deposition pattern of amyloid in autopsy hearts of CA patients and to correlate the histopathology findings with 2D echocardiography.
METHODS AND RESULTS
This is a retrospective study of whole heart specimens of CA patients who died and underwent autopsy and 2D echocardiography. Amyloid burden quantification was assessed by histomorphometry in each segment at different LV levels. The LS analysis results were compared with the amyloid burden and the base-to-apex distribution.Histopathology investigation of 27 hearts with CA [immunoglobulin light chains (AL) 17 cases and transthyretin (ATTR) 10 cases] demonstrated an amyloid base-to-apex gradient. In 11 CA patients with 2D echocardiography, analysis of LS and histological amyloid burden allowed to identify different patterns: RELAPS (8 cases, 73%), with (2) or without (6) amyloid gradient, normal or mildly reduced LS with diffuse low amyloid (2, 18%), and severely reduced LS with diffuse high amyloid (1, 9%).
CONCLUSION
The typical RELAPS pattern at echocardiography is not always explained by a base-to-apex gradient of amyloid burden at histopathology, suggesting that RELAPS might be an epiphenomenon of complex interactions among amyloid infiltration, myocardial structure, and adaptation.
Topics: Humans; Retrospective Studies; Cardiomyopathies; Amyloidosis; Myocardium; Echocardiography
PubMed: 37191052
DOI: 10.1093/ehjci/jead107 -
Medicine Dec 2022Amyloidosis is a group of benign lesions characterized by extracellular deposition of amyloid proteins. Amyloidosis lesions can occur in various organs of the body, but... (Review)
Review
RATIONALE
Amyloidosis is a group of benign lesions characterized by extracellular deposition of amyloid proteins. Amyloidosis lesions can occur in various organs of the body, but rarely in the urinary system. Amyloidosis in the bladder trigone is extremely rare.
PATIENT CONCERNS
An 80-year-old female patient presented with painless whole-course gross hematuria with reddish urine and no blood clots, accompanied by right lumbar discomfort.
DIAGNOSIS
Based on the patient's medical history and cystoscopy findings, the relevant literature was reviewed and a preoperative diagnosis of bladder tumor was made, although bladder amyloidosis was not excluded. Postoperative pathology ultimately revealed bladder amyloidosis.
INTERVENTIONS
The patient underwent resection of bladder tumor and ureteral stent implantation. Postoperatively, the patient was maintained on antibiotics and oral colchicine treatment.
OUTCOMES
Two months after surgery the patient reported that the gross hematuria had disappeared, and that the right lumbar discomfort was significantly relieved.Cystoscopy showed no obvious recurrence in the operative area, but magnetic resonance imaging (MRI) suggested recurrence. The patient refused partial cystectomy, and the ureteral stent was removed.
LESSON
The clinical manifestations of bladder amyloidosis are nonspecific, and under cystoscopy can be easily confused with bladder tumors. Accurate diagnosis of bladder amyloidosis relies on histopathology. Transurethral resection of bladder tumors or partial cystectomy is an option for surgical treatment; the latter should be performed if the ureteral opening is involved.
Topics: Female; Humans; Aged, 80 and over; Urinary Bladder; Urinary Bladder Diseases; Hematuria; Neoplasm Recurrence, Local; Amyloidosis; Urinary Bladder Neoplasms
PubMed: 36626417
DOI: 10.1097/MD.0000000000032179 -
Middle East African Journal of... 2013To describe six cases of anterior orbital and adnexal amyloidosis and to report on proteomic analysis to characterize the nature of amyloid in archived biopsies in two...
PURPOSE
To describe six cases of anterior orbital and adnexal amyloidosis and to report on proteomic analysis to characterize the nature of amyloid in archived biopsies in two cases.
MATERIALS AND METHODS
The clinical features, radiological findings, pathology, and outcome of six patients with anterior orbit and adnexal amyloidosis were retrieved from the medical records. The biochemical nature of the amyloid was determined using liquid chromatography/mass spectroscopy archived paraffin-embedded tissue in two cases.
RESULTS
Of the six cases, three had unilateral localized anterior orbit and lacrimal gland involvement. Four of the six patients were female with an average duration of 12.8 years from the time of onset to presentation eyelid infiltration by amyloid caused ptosis in five cases. CT scan in patients with lacrimal gland involvement (n = 3) demonstrated calcified deformable anterior orbital masses and on pathological exmaintionamyloid and calcific deposits replaced the lacrimal gland acini. Ptosis repair was performed in three patients with good outcomes. One patient required repeated debulking of the mass and one patient had recurrenct disease. Proteomic analysis revealed polyclonal IgG-associated amyloid deposition in one patient and AL kappa amyloid in the second patient.
CONCLUSION
Amyloidosis of the anterior orbit and lacrimal gland can present with a wide spectrum of findings with good outcomes after surgical excision. The nature of amyloid material can be precisely determined in archival pathology blocks using diagnostic proteomic analysis.
Topics: Adult; Aged; Amyloid; Amyloidosis; Biopsy; Chromatography, Liquid; Conjunctival Diseases; Female; Humans; Lacrimal Apparatus Diseases; Male; Middle Aged; Orbital Diseases; Proteomics; Tandem Mass Spectrometry; Tomography, X-Ray Computed
PubMed: 24014979
DOI: 10.4103/0974-9233.114789 -
The American Journal of Pathology Dec 1984The senile amyloidoses comprise a heterogeneous group of disorders with deposition of amyloid in a variety of tissues. Most of these amyloidoses are localized to one...
The senile amyloidoses comprise a heterogeneous group of disorders with deposition of amyloid in a variety of tissues. Most of these amyloidoses are localized to one tissue. It has been shown previously that the amyloid fibrils in one form of senile amyloidosis affecting the heart contains a prealbumin-related protein, ASc1. It is shown in this paper by immunohistochemical study using a specific anti-protein ASc1 antiserum that this type of amyloidosis, previously called senile cardiac amyloidosis, is a systemic disease with amyloid deposits in many organs. The designation senile systemic amyloidosis is proposed for this disease, which differs from other systemic amyloidoses in distribution of amyloid deposits.
Topics: Aged; Aging; Amyloid; Amyloidosis; Digestive System; Endocrine Glands; Female; Heart Ventricles; Histocytochemistry; Humans; Kidney; Lung; Male; Serum Amyloid A Protein
PubMed: 6507586
DOI: No ID Found