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International Journal of Molecular... Mar 2023Cardiac amyloidosis is an uncommon restrictive cardiomyopathy featuring an unregulated amyloid protein deposition that impairs organic function. Early cardiac... (Review)
Review
Cardiac amyloidosis is an uncommon restrictive cardiomyopathy featuring an unregulated amyloid protein deposition that impairs organic function. Early cardiac amyloidosis diagnosis is generally delayed by indistinguishable clinical findings of more frequent hypertrophic diseases. Furthermore, amyloidosis is divided into various groups, according to a generally accepted taxonomy, based on the proteins that make up the amyloid deposits; a careful differentiation between the various forms of amyloidosis is necessary to undertake an adequate therapeutic treatment. Thus, cardiac amyloidosis is thought to be underdiagnosed, which delays necessary therapeutic procedures, diminishing quality of life and impairing clinical prognosis. The diagnostic work-up for cardiac amyloidosis begins with the identification of clinical features, electrocardiographic and imaging findings suggestive or compatible with cardiac amyloidosis, and often requires the histological demonstration of amyloid deposition. One approach to overcome the difficulty of an early diagnosis is the use of automated diagnostic algorithms. Machine learning enables the automatic extraction of salient information from "raw data" without the need for pre-processing methods based on the a priori knowledge of the human operator. This review attempts to assess the various diagnostic approaches and artificial intelligence computational techniques in the detection of cardiac amyloidosis.
Topics: Humans; Artificial Intelligence; Quality of Life; Amyloidosis; Amyloid; Machine Learning; Cardiomyopathies
PubMed: 36982754
DOI: 10.3390/ijms24065680 -
The Journal of International Medical... Dec 2022Amyloidosis is a disease caused by amyloid deposition in tissues or organs. According to the extent of the lesion, it can be divided into systemic amyloidosis and...
Amyloidosis is a disease caused by amyloid deposition in tissues or organs. According to the extent of the lesion, it can be divided into systemic amyloidosis and localized amyloidosis. Amyloidosis originating in the larynx accounts for approximately 0.5% to 1.0% of benign lesions of the larynx; such lesions are relatively rare and mostly localized. Nasopharyngeal amyloidosis combined with laryngeal amyloidosis is even rarer. We herein present a case involving a patient with amyloidosis in the nasopharynx and larynx who presented with a foreign body sensation and hoarseness in the pharynx. Electronic fiber laryngoscopy revealed a smooth neoplasm in the left nasopharynx and left vocal cord. The patient underwent surgical treatment, and the postoperative pathologic examination results suggested amyloidosis. Special staining performed using Congo red and crystal violet was positive, confirming amyloidosis. The patient recovered after surgery, and no recurrence was present at the 3- and 6-month follow-ups.
Topics: Humans; Larynx; Amyloidosis; Laryngeal Diseases; Immunoglobulin Light-chain Amyloidosis; Nasopharynx
PubMed: 36539964
DOI: 10.1177/03000605221144151 -
Medicina Oral, Patologia Oral Y Cirugia... Jul 2023Amyloidosis is a disease characterized by the progressive deposition of abnormal proteins that can occur in any organ. In the oral cavity, the tongue is the most common...
BACKGROUND
Amyloidosis is a disease characterized by the progressive deposition of abnormal proteins that can occur in any organ. In the oral cavity, the tongue is the most common affected site, usually causing macroglossia. Biopsy is essential for the diagnosis and the occurrence of its systemic form is mandatory to be investigated. This systematic review evaluated the existing information in the literature on Amyloidosis in the oral cavity to allow a more comprehensive and updated analysis of its clinicopathological characteristics, as well as to explore the main forms of treatment and prognostic factors.
MATERIAL AND METHODS
Electronic searches were undertaken in five databases supplemented by manual scrutiny.
RESULTS
A total of 111 studies were included with 158 individuals.
CONCLUSIONS
The disease had a higher prevalence in women, the tongue was the most affected site, as well as the systemic form of the disease. The worst prognosis was for cases of systemic amyloidosis associated with multiple myeloma.
Topics: Humans; Female; Amyloidosis; Macroglossia; Multiple Myeloma; Tongue Diseases; Tongue
PubMed: 37330968
DOI: 10.4317/medoral.25761 -
Journal of the American College of... Jun 2018Prognosis in light-chain (AL) and transthyretin (ATTR) amyloidosis is influenced by cardiac involvement. ATTR amyloidosis has better prognosis than AL amyloidosis...
BACKGROUND
Prognosis in light-chain (AL) and transthyretin (ATTR) amyloidosis is influenced by cardiac involvement. ATTR amyloidosis has better prognosis than AL amyloidosis despite more amyloid infiltration, suggesting additional mechanisms of damage in AL amyloidosis.
OBJECTIVES
The aim of the study was to assess the presence and prognostic significance of myocardial edema in patients with amyloidosis.
METHODS
The study recruited 286 patients: 100 with systemic AL amyloidosis, 163 with cardiac ATTR amyloidosis, 12 with suspected cardiac ATTR amyloidosis (grade 1 on Tc-3,3-diphosphono-1,2-propanodicarboxylic acid), 11 asymptomatic individuals with amyloidogenic TTR gene mutations, and 30 healthy volunteers. All subjects underwent cardiovascular magnetic resonance with T1 and T2 mapping and 16 underwent endomyocardial biopsy.
RESULTS
Myocardial T2 was increased in amyloidosis with the degree of elevation being highest in untreated AL patients (untreated AL amyloidosis 56.6 ± 5.1 ms; treated AL amyloidosis 53.6 ± 3.9 ms; ATTR amyloidosis 54.2 ± 4.1 ms; each p < 0.01 compared with control subjects: 48.9 ± 2.0 ms). Left ventricular (LV) mass and extracellular volume fraction were higher in ATTR amyloidosis compared with AL amyloidosis while LV ejection fraction was lower (p < 0.001). Histological evidence of edema was present in 87.5% of biopsy samples ranging from 5% to 40% myocardial involvement. Using Cox regression models, myocardial T2 predicted death in AL amyloidosis (hazard ratio: 1.48; 95% confidence interval: 1.20 to 1.82) and remained significant after adjusting for extracellular volume fraction and N-terminal pro-B-type natriuretic peptide (hazard ratio: 1.32; 95% confidence interval: 1.05 to 1.67).
CONCLUSIONS
Myocardial edema is present in cardiac amyloidosis by histology and cardiovascular magnetic resonance T2 mapping. T2 is higher in untreated AL amyloidosis compared with treated AL and ATTR amyloidosis, and is a predictor of prognosis in AL amyloidosis. This suggests mechanisms additional to amyloid infiltration contributing to mortality in amyloidosis.
Topics: Adult; Aged; Aged, 80 and over; Amyloidosis; Cardiomyopathies; Edema; Female; Humans; London; Magnetic Resonance Imaging; Male; Middle Aged; Myocardium; Prealbumin
PubMed: 29929616
DOI: 10.1016/j.jacc.2018.03.536 -
Journal of Ultrasound Sep 2023Cardiac involvement from amyloidosis is of growing interest in the overall literature. Despite cardiac amyloidosis (CA) has been considered for a long time a rare... (Review)
Review
Cardiac involvement from amyloidosis is of growing interest in the overall literature. Despite cardiac amyloidosis (CA) has been considered for a long time a rare disease, the diagnostic awareness is increasing mainly thanks to the improvement of diagnostic softwares and of imaging techniques such as cardiac magnetic resonance (CMR). Some authors have observed an increase of prevalence rate of CA; moreover it's often underestimated because clinical manifestations are aspecific. The interstitial infiltration of the left ventricle has been extensively studied, while the involvement of the right ventricle (RV) has been less investigated. Involvement of the RV, even in the absence of pulmonary hypertension or clearly left ventricle infiltration, plays an important role as prognostic factor and is useful to achieve an early diagnosis. Therefore, the use of fast and low-cost diagnostic methods such as ultrasound strain of the right ventricle could be used to recognize cardiac amyloidosis early. Herein the importance of evaluating the right ventricular involvement, which can predict the most severe course of the disease also without overt clinical manifestations. The role of imaging, in particular of echocardiography, CMR, and scintigraphy is here reported.
Topics: Humans; Amyloidosis; Heart; Prognosis; Echocardiography; Disease Progression
PubMed: 37162729
DOI: 10.1007/s40477-023-00789-1 -
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 -
JACC. Cardiovascular Imaging Feb 2010
Topics: Amyloidosis; Biomarkers; Biopsy; Cardiomyopathies; Contrast Media; Early Diagnosis; Gadolinium DTPA; Humans; Magnetic Resonance Imaging, Cine; Myocardium; Predictive Value of Tests; Prognosis; Severity of Illness Index; Ultrasonography
PubMed: 20159643
DOI: 10.1016/j.jcmg.2009.10.013 -
The American Journal of Managed Care Jun 2017Hereditary transthyretin-mediated (hATTR) amyloidosis is a progressive disease characterized by deposition of amyloid fibrils in various organs and tissues of the body.... (Review)
Review
Hereditary transthyretin-mediated (hATTR) amyloidosis is a progressive disease characterized by deposition of amyloid fibrils in various organs and tissues of the body. There are a wide variety of clinical presentations for this multisystemic disorder, so it is often misdiagnosed or subject to delayed diagnosis. Although the exact prevalence is difficult to determine, existing estimates suggest a worldwide prevalence of 50,000 individuals, with varying phenotypic presentations of disease. Due to the heterogeneous nature of its presentation, incorrect or delayed diagnosis can severely impact quality of life for these patients. hATTR amyloidosis can lead to significant disability and mortality. After an accurate diagnosis of hATTR amyloidosis is established, new patients should undergo appropriate therapy as soon as possible. Current treatment options for hATTR amyloidosis are limited, but orthotopic liver transplant serves as an established option for patients with early-stage disease. Consequently, there is a need for new, effective, and safe therapies.
Topics: Amyloidosis, Familial; Cost of Illness; Humans
PubMed: 28978215
DOI: No ID Found -
Clinical Cardiology Aug 1998Primary amyloidosis, systemic senile amyloidosis, isolated atrial amyloidosis, and transthyretin isoleucine 122 amyloidosis frequently involve the heart. Amyloid fibrils... (Review)
Review
Primary amyloidosis, systemic senile amyloidosis, isolated atrial amyloidosis, and transthyretin isoleucine 122 amyloidosis frequently involve the heart. Amyloid fibrils infiltrate the myocardium, impairing ventricular contraction and relaxation. The clinical manifestations of cardiac infiltration in these disorders are protean, though congestive heart failure and arrhythmias are most common. Treatment of cardiac amyloidosis is directed at the underlying cause and at relief of symptoms. Heart transplantation is not a viable treatment option for patients with primary amyloidosis; its role in the other amyloidoses has not been established. The prognosis of patients with cardiac amyloidosis varies and is largely determined by the underlying disorder responsible for amyloid infiltration.
Topics: Aged; Amyloid; Amyloidosis; Cardiomyopathies; Humans; Myocardium
PubMed: 9702380
DOI: 10.1002/clc.4960210804 -
Molecules (Basel, Switzerland) Aug 2021Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or... (Review)
Review
Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or whether, amyloid fibrils contribute to tissue damage in amyloidosis has been the topic of debate. In vitro studies have demonstrated the appearance of small globular oligomeric species during the incubation of amyloid beta peptide (Aβ). Nerve biopsy specimens from patients with systemic amyloidosis have suggested that globular structures similar to Aβ oligomers were generated from amorphous electron-dense materials and later developed into mature amyloid fibrils. Schwann cells adjacent to amyloid fibrils become atrophic and degenerative, suggesting that the direct tissue damage induced by amyloid fibrils plays an important role in systemic amyloidosis. In contrast, there is increasing evidence that oligomers, rather than amyloid fibrils, are responsible for cell death in neurodegenerative diseases, particularly Alzheimer's disease. Disease-modifying therapies based on the pathophysiology of amyloidosis have now become available. Aducanumab, a human monoclonal antibody against the aggregated form of Aβ, was recently approved for Alzheimer's disease, and other monoclonal antibodies, including gantenerumab, solanezumab, and lecanemab, could also be up for approval. As many other agents for amyloidosis will be developed in the future, studies to develop sensitive clinical scales for identifying improvement and markers that can act as surrogates for clinical scales should be conducted.
Topics: Amyloid; Amyloidosis; Animals; Humans; Organ Specificity; Protein Aggregates; Schwann Cells
PubMed: 34443678
DOI: 10.3390/molecules26165091