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Cardiac amyloidosis: a hidden cause of cardiovascular complications in oncology practice

100%
Mladosievicova B., Poljak Z., El-Hassoun O., Roziakova L., Carter A.
OncoReview
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2014
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vol. 4
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issue 4
A137-A143
EN
Amyloidosis is rare, but known cause of heart failure, cardiomyopathy, coronary artery disease, disorders of cardiac conduction system and valvular damage. Disease often remains undetected until it reaches an advanced stage. Currently, we distinguish several types of amyloidosis. Cardiac amyloidosis may be caused by cancer, chronic inflammation, genetic factors and by aging related processes. Overproduction of amyloidogenic proteins by tumor cells has a key role in the pathogenesis of immunoglobulin light chain amyloidosis. Cardiovascular complications in patients with amyloidosis can be induced by insoluble deposits of misfolded proteins or by direct toxic effects of amyloidogenic molecules on cardiomyocytes and endothelial cells. In this review we focus mainly on pathophysiological mechanisms of cardiac amyloidosis, classification of cardiac amyloidosis types and their cardiovascular manifestations.
2
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Head and neck amyloidosis – a report on five cases

75%
Orłowska A., Mastalerek J., Jaskólska M., Rzepakowska A., Grzybowski J., Gotlib T., Niemczyk K.
Polski Przegląd Otorynolaryngologiczny
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2019
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vol. 8(2)
32-37
EN
Background: Amyloidosis is a group of diseases caused by the extracellular accumulation of insoluble fibers called amyloid in the tissues and organs. They have a secondary beta-sheet structure, which makes them resistant to proteolysis. In histological examination amyloid deposits stain with Congo red and show an apple-green birefringence in polarized light. Amyloid deposits disturb the function of organs and cause clinical symptoms. Their formation or accumulation in the system may be acquired or inherited. Due to the location of amyloid deposits we distinguish systemic and localized amyloidosis with the formation of tumors (usually from light chains). Case reports: 5 cases of amyloidosis in the head and neck region are presented in this paper. The locations of the amyloid deposits were as follows: larynx, nasopharynx, sublingual and submandibular gland and the tongue. The initial clinical presentation correlated with location of amyloid tumour in our patients. Two patients had history of local recurrence of the disease. Surgical resection and histopathological examination were performed. Sections stained with Congo red confirmed the diagnosis of amyloidosis. Three patients had potential conditions predisposing to amyloidosis: previous radiotherapy, chronic inflammation due to hepatitis C virus infection and graft versus host disease. Conclusion: Amyloidosis should be considered as the cause of symptoms in pathologies of the head and neck region. The diagnosis requires a histopathological examination. The systemic form of the disease must be ruled out in all patients with head and neck amyloidosis. In localized amyloidosis the surgical resection of the lesions is the procedure of choice, however the organ’s functionality should be taken into account.
3
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3D Domain swapping, protein oligomerization, and amyloid formation.

75%
Jaskólski M.
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2001
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vol. 48
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issue 4
807-827
EN
In 3D domain swapping, first described by Eisenberg, a structural element of a monomeric protein is replaced by the same element from another subunit. This process requires partial unfolding of the closed monomers that is then followed by adhesion and reconstruction of the original fold but from elements contributed by different subunits. If the interactions are reciprocal, a closed-ended dimer will be formed, but the same phenomenon has been suggested as a mechanism for the formation of open-ended polymers as well, such as those believed to exist in amyloid fibrils. There has been a rapid progress in the study of 3D domain swapping. Oligomers higher than dimers have been found, the monomer-dimer equilibrium could be controlled by mutations in the hinge element of the chain, a single protein has been shown to form more than one domain-swapped structure, and recently, the possibility of simultaneous exchange of two structural domains by a single molecule has been demonstrated. This last discovery has an important bearing on the possibility that 3D domain swapping might be indeed an amyloidogenic mechanism. Along the same lines is the discovery that a protein of proven amyloidogenic properties, human cystatin C, is capable of 3D domain swapping that leads to oligomerization. The structure of do-main-swapped human cystatin C dimers explains why a naturally occurring mutant of this protein has a much higher propensity for aggregation, and also suggests how this same mechanism of 3D domain swapping could lead to an open-ended polymer that would be consistent with the cross-β structure, which is believed to be at the heart of the molecular architecture of amyloid fibrils.
4
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Identification of proteins associated with amyloidosis by polarity index method

63%
Polanco C., Samaniego J., Uversky V., Castañón-González J., Buhse T., Leopold-Sordo M., Madero-Arteaga A., Morales-Reyes A., Tavera-Sierra L., González-Bernal J., Arias-Estrada M.
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2015
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vol. 62
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issue 1
41-55
EN
There is a natural protein form, insoluble and resistant to proteolysis, adopted by many proteins independently of their amino acid sequences via specific misfolding-aggregation process. This dynamic process occurs in parallel with or as an alternative to physiologic folding, generating toxic protein aggregates that are deposited and accumulated in various organs and tissues. These proteinaceous deposits typically represent bundles of β-sheet-enriched fibrillar species known as the amyloid fibrils that are responsible for serious pathological conditions, including but not limited to neurodegenerative diseases, grouped under the term amyloidoses. The proteins that might adopt this fibrillar conformation are some globular proteins and natively unfolded (or intrinsically disordered) proteins. Our work shows that intrinsically disordered and intrinsically ordered proteins can be reliably identified, discriminated, and differentiated by analyzing their polarity profiles generated using a computational tool known as the polarity index method (Polanco & Samaniego, 2009; Polanco et al., 2012; 2013; 2013a; 2014; 2014a; 2014b; 2014c; 2014d). We also show that proteins expressed in neurons can be differentiated from proteins in these two groups based on their polarity profiles, and also that this computational tool can be used to identify proteins associated with amyloidoses. The efficiency of the proposed method is high (i.e. 70%) as evidenced by the analysis of peptides and proteins in the APD2 database (2012), AVPpred database (2013), and CPPsite database (2013), the set of selective antibacterial peptides from del Rio et al. (2001), the sets of natively unfolded and natively folded proteins from Oldfield et al. (2005), the set of human revised proteins expressed in neurons, and non-human revised proteins expressed in neurons, from the Uniprot database (2014), and also the set of amyloidogenic proteins from the AmyPDB database (2014).
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