Wyniki wyszukiwania - Biblioteka Nauki

1

Advances in understanding, diagnosis and targeting ATTR cardiomyopathy: a review

100%

Kulak M. , Lang M. , Waśniewski M. , Lange N.

European Journal of Translational and Clinical Medicine

|

2024

|

tom 7

|

nr 1

63-78

EN

Transthyretin amyloidosis (ATTR) manifests as wild-type (ATTRwt) and hereditary/mutant (ATTRv) forms and can lead to heart failure due to cardiac amyloidopathy. Diagnosing ATTR, particularly in asymptomatic carriers of pathogenic variants, remains challenging despite the advances. Complex and multi-aspect management involves a limited range of well-examined conventional therapies to address the heart failure and frequently coexisting arrhythmias and valvular issues. Disease-modifying treatment, RNA-based treatments, CRISPR-Cas9 gene editing and monoclonal antibodies targeting amyloid deposits are recent and promising innovations. This review explores the diagnostic intricacies, therapeutic dilemmas and emerging solutions in ATTR cardiomyopathy. The significance of early detection and precise, targeted approaches to enhance patient outcomes is underscored.

2

Aggregation-promoting conditions necessary to create the complexes by acylphosphatase from the hyperthermophile Sulfolobus solfataricus

100%

Banach M. , Wiśniowski Z. , Ptak M. , Roterman I.

Bio-Algorithms and Med-Systems

|

2019

|

tom Vol. 15, no. 2

art. no. 20190023

EN

The structural transition from the globular to the amyloid form of proteins requires aggregation-promoting conditions. The protein example of this category is acylphosphatase from the hyperthermophile Sulfolobus solfataricus. This protein represents a structure with a well-defined hydrophobic core. This is why the complexation (including oligomerization) of this protein is of low probability. The chain fragment participating in aggregation in comparison to the status with respect to the fuzzy oil drop model is discussed in this paper.

3

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

100%

Mladosievicova B. , Poljak Z. , El-Hassoun O. , Roziakova L. , Carter A.

OncoReview

|

2014

|

tom 4

|

nr 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.

4

3D Domain swapping, protein oligomerization, and amyloid formation.

75%

Jaskólski M.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 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.

5

Canine renal amyloidosis: a case report

75%

Szczepankiewicz B. , Paslawska U. , Grzegory M. , Jonkisz P. , Borecka P. , Marzec M. , Brzozowska M. , Nowak M.

Medycyna Weterynaryjna

|

2018

|

tom 74

|

nr 05

EN

Amyloidosis is a disease caused by the deposition of amorphous extracellular protein, leading to impaired kidney function. Canine and feline amyloidosis is associated with the deposition of AA protein. The disease is hereditary and is related to breed but not sex. Predisposed breeds include the Shar Pei dog and Abyssinian cat. Proteinuria resulting in hypoalbuminemia due to changes in renal glomeruli is the first clinical sign. In addition, a decreased appetite, anorexia, vomiting, lethargy, polyuria and polydipsia may be observed. In order to diagnose the disease, serum amyloid A levels may be measured. However, a definitive diagnosis is made on the basis of an intravital renal biopsy and the presence of amyloid in the histopathological examination. The main goal of treatment is to reduce inflammation and proteinuria. If nephrotic syndrome occurs, the prognosis is guarded to poor, and the majority of patients do not survive one year. The definitive diagnosis is based on the post-mortem examination, in which the presence of amyloid deposits is confirmed in the kidney tissue. We present the case of a 7-year-old female Shar Pei diagnosed with kidney amyloidosis, on the basis of which we have developed a prevention scheme for clinical practice.

6

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

|

2019

|

tom 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.

7

Structural basis of negative cooperativity in transthyretin

75%

Neumann P. , Cody V. , Wojtczak A.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 4

EN

A comparison of the AC and BD binding sites of transthyretin (TTR) was made in terms of the interatomic distances between the Ca atoms of equivalent amino acids, measured across the tetramer channel in each binding site. The comparison of the channel diameter for apo TTR from different sources revealed that in the unliganded transthyretin tetramers the distances between the A, D and H β-strands are consistently larger, while the distances between the G β-strands are smaller in one site than in the other. These differences might be described to have a 'wave' character. An analogous analysis performed for transthyretin complexes reveals that the shape of the plot is similar, although the amplitudes of the changes are smaller. The analysis leads us to a model of the changes in the binding sites caused by ligand binding. The sequence of events includes ligand binding in the first site, followed by a slight collapse of this site and concomitant opening of the second site, binding of the second molecule and collapse of the second site. The following opening of the first, already occupied site upon ligand binding in the second site is smaller because of the bridging interactions already formed by the first ligand. This explains the negative cooperativity (NC) effect observed for many ligands in transthyretin.

8

Limitations of electrocardiographic criteria of left ventricular hypertrophy in differentiation between hypertrophic cardiomyopathy, cardiac amyloidosis and Fabry disease

63%

Tometczak M. , Znamirowska J. , Topa J. , Pastor P. , Waksmundzki D. , Grzebinoga A. , Mizia-Stec K.

Annales Academiae Medicae Silesiensis

|

2023

|

nr 78

173-178

PL

WSTĘP: Przerost lewej komory (left ventricular hypertrophy – LVH) jest powszechną patologią i powinien być rozróżniany za pomocą metod inwazyjnych i nieinwazyjnych. Elektrokardiografia (electrocardiography – ECG) jest metodą pierwszego wyboru w klinicznej ocenie pacjentów z LVH. MATERIAŁ I METODY: Przeprowadzono retrospektywną analizę 77 pacjentów (wiek: 54.1 ± 16.3; 50,6% mężczyzn) z cechami przerostu serca w badaniu echokardiograficznym. Populację podzielono na trzy podgrupy: 60 pacjentów z kardiomiopatią przerostową (hypertrophic cardiomyopathy – HCM), 11 z amyloidozą serca (cardiac amyloidosis – CA) i 6 z chorobą Fabry’ego (Fabry disease – FD). Oceniono zapisy ECG oraz zweryfikowano obecność i częstość występowania ośmiu kryteriów LVH. WYNIKI: W badanej populacji kryteria LVH ECG były spełnione u 67,6% pacjentów z HCM, 53,8% z CA i 57,1% z FD. Analiza liczby kryteriów LVH ujawniła: żadnego kryterium nie spełniało 32,4% pacjentów z HCM, 46,2% z CA oraz 42,9% z FD; 1 kryterium spełniało 21,1% pacjentów z HCM, 46,2% z CA oraz 14,3% z FD; 2–4 kryteria stwierdzono u 33,8% pacjentów z HCM, 7,7% z CA oraz 42,9% z FD; 5–7 kryteriów występowało u 12,7% pacjentów z HCM i u żadnego pacjenta z CA i FD. Żaden pacjent nie spełniał ośmiu kryteriów. WNIOSKI: Elektrokardiograficzne kryteria LVH nie są swoistymi wykładnikami LVH. Różnice pomiędzy echokardiografią przezklatkową (transthoracic echocardiography – TTE) oraz zmianami elektrokardiograficznymi są charakterystyczne dla CA oraz FD, co może budzić podejrzenie wystąpienia tych chorób. Brak spełnionych kryteriów LVH w ECG nie wyklucza tych diagnoz.

EN

INTRODUCTION: Left ventricular hypertrophy (LVH) is a common pathology and should be differentiated using non-invasive and invasive methods. Electrocardiography (ECG) is the first choice method for the clinical evaluation of patients with LVH. MATERIAL AND METHODS: A retrospective analysis of 77 patients (pts; age: 54.1 ± 16.3; 50.6% men) with features of cardiac hypertrophy in an echocardiographic examination was performed. The population was divided into three subgroups: 60 pts with hypertrophic cardiomyopathy (HCM), 11 pts with cardiac amyloidosis (CA) and 6 pts with Fabry disease (FD). Multiple ECG records were evaluated and the presence and frequency of eight different LVH criteria were verified. RESULTS: Among the study population LVH criteria were present in 67.6% pts with HCM, 53.8% pts with CA and 57.1% pts with FD. Analysis of the number of LVH ECG criteria revealed: none of LVH ECG criteria: in 32.4% pts of HCM, in 46.2% pts with CA, in 42.9% pts with FD; 1 LVH ECG criterion in 21.1% pts with HCM, 46.2% pts with CA and 14.3% pts with FD; 2–4 criteria in 33.8% pts with HCM, 7.7% pts with CA and 42.9% pts with FD; 5–7 criteria in 12.7% pts with HCM and no pts with CA or FD. No patient fulfilled the eight LVH ECG criteria. CONCLUSIONS: Electrocardiographic LVH criteria are not sensitive indicators of LVH. The mismatch between transthoracic echocardiography (TTE) and ECG findings is characteristic for CA and FD that may raise the suspicion of these diseases. The lack of LVH ECG criteria do not exclude these diagnoses.

9

Amyloidogenic proteins and occurrence of different amyloidosis in different animal species

63%

Florczuk-Kolomyja P. , Kolomyja P. , Swiderek W. , Gruszczynska J.

Acta Scientiarum Polonorum. Zootechnica

|

2020

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tom 19

|

nr 3

10

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.

Acta Biochimica Polonica

|

2015

|

tom 62

|

nr 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).

11

3D domain swapping, protein oligomerization, and amyloid formation

63%

Jaskolski M.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 4

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 domain- 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.

12

Echocardiographic markers of left ventricular hypertrophy and concentric remodeling – limitations in diagnostics of cardiac amyloidosis, Fabry disease and hypertrophic cardiomyopathy

51%

Znamirowska J. , Tometczak M. , Topa J. , Pastor P. , Waksmundzki D. , Grzebinoga A. , Mizia-Stec K.

Annales Academiae Medicae Silesiensis

|

2024

|

nr 78

219-225

PL

WPROWADZENIE: Przerost lewej komory (left ventricular hypertrophy – LVH) jest istotną cechą powiązaną ze wzrostem ryzyka nagłej śmierci sercowej. Typowe przyczyny przerostu obejmujące amyloidozę serca (cardiac amyloidosis – CA), chorobę Fabry’ego (Fabry disease – FD) oraz kardiomiopatię przerostową (hypertrophic cardiomyopathy – HCM) wymagają specyficznego podejścia i rokują niepomyślnie. Echokardiografia przezklatkowa (transthoracic echocardiography – TTE) pozostaje wówczas podstawową metodą diagnostyczną. MATERIAŁ I METODY: Wykonano jednoośrodkową analizę retrospektywną obejmującą 86 pacjentów z przero-stem ściany lewej komory (left ventricular – LV) stwierdzonym w TTE. Kryteriami włączenia były grubość przegrody międzykomorowej (interventricular septum – IVS) powyżej 10 mm u mężczyzn i 9 mm u kobiet oraz potwierdzona diagnoza CA, FD lub HCM. Badana populacja została podzielona na trzy grupy w zależno-ści od końcowej diagnozy: CA (13 pacjentów), FD (7 pacjentów) oraz HCM (66 pacjentów). Analizowano in-deks masy lewej komory (LV mass index – LVMI), względną grubość ściany lewej komory (relative wall thickness – RWT) oraz typ przerostu. WYNIKI: LVMI powyżej normy obserwowano u 90,9% pacjentów z CA, wszystkich z FD, 89,5% z HCM. RWT powyżej normy obserwowano u 92,3% pacjentów z CA, 57,1% z FD, 92,4% z HCM. Przerost koncentryczny zdiagnozowano u 75% pacjentów z CA, 57,1% z FD, 84,2% z HCM; przerost ekscentryczny zaobserwowano u 8,3% pacjentów z CA, 42,9% z FD, 5,3% z HCM (p = 0,01). IVS/PWT powyżej normy stwierdzono u 23,1% pacjentów z CA, 28,6% z FD, 79,7% z HCM (p = 0,00001). WNIOSKI: Mimo iż przerost serca jest cechą typową, nie występuje u wszystkich osób z CA, FD, HCM. Do scharakteryzowania konkretnych chorób, jak CA, FD, HCM, wymagana jest dokładniejsza analiza obejmująca typ przerostu oraz remodeling lewego przedsionka. Na podstawie wyników przerost asymetryczny jest bardziej swoisty dla HCM.

EN

INTRODUCTION: Left ventricular hypertrophy (LVH) is a relevant sign associated with an increased risk of sudden death. The causes of LVH including cardiac amyloidosis (CA), Fabry disease (FD), hypertrophic cardiomyopathy (HCM) are associated with an inauspicious prognosis. Transthoracic echocardiography (TTE) remains the first-step baseline diagnostic method. MATERIAL AND METHODS: A retrospective one-center analysis of 86 patients (pts) with increased left ventricular (LV) wall thickness in TTE was performed. The inclusion criteria were interventricular septum (IVS) above 10 mm in males, 9 mm in females and the final diagnosis of CA, FD or HCM. The study population was divided into three subgroups: CA (13 pts), FD (7 pts), HCM (66 pts). The LV mass index (LVMI), relative wall thickness (RWT) and type of remodeling were analyzed. RESULTS: Increased LVMI occurred in 90.9% pts with CA, all with FD, 89.5% with HCM.RWT exceeded the normal range among 92.3% pts with CA, 57.1% with FD, 92.4% with HCM. Concentric hypertrophy was diagnosed in 75% pts with CA, 57.1% with FD, 84.2% with HCM and eccentric in 8.3% pts with CA, 42.9% with FD, 5.3% with HCM (p = 0.01). An abnormal IVS/PWT index was observed in 23.1% pts with CA, 28.6% with FD, 79.7% with HCM (p = 0.00001). CONCLUSIONS: Although cardiac hypertrophy is a typical sign, it does not occur in all subjects with CA, FD, HCM. More detailed analysis including the form of hypertrophy as well as left atrium remodeling are required to be characterized for specific diseases: CA, FD, HCM. Asymmetrical hypertrophy is more specific for HCM.

13

Tracheobronchial amyloidosis - bronchoscopic diagnosis and therapy of an uncommon disease: a case report

51%

Brill A. K. , Woelke K. , Schadlich R. , Weinz C. , Laier-Groeneveld G.

Journal of Physiology and Pharmacology. Supplement

|

2007

|

tom 58

|

nr 5

14

The transmissible brain amyloidoses: a comparison with the non transmissible brain amyloidoses of Alzheimer type

51%

Liberski P. P.

|

tom 53

|

nr 1

15

Amyloidosis and the acute phase response

51%

Sipe J. D.

Folia Histochemica et Cytobiologica

|

1992

|

tom 30

|

nr 4

16

Wplyw preparatow TFX-Polfa i lewamizolu na reaktywnosc immunologiczna swin w przebiegu amyloidogenezy

38%

Rotkiewicz Z.

Acta Academiae Agriculturae ac Technicae Olstenensis. Veterinaria

|

1995

|

tom 22,Suppl.B

1-59

PL

W przebiegu doświadczalnej amyloidozy u świń, wywołanej domięśniowym podawaniem kazeinianu sodu, określono wpływ lewamizolu i preparatu „TFX-Polfa" na reaktywność układu immunologicznego w zakresie nieswoistej i swoistej odporności komórkowej i humoralnej. Tę ostatnią indukowano żywą szczepionką wirusa chA. Z przeprowadzonych badań wynika, że w okresie przedamyloidowym następuje wzrost, a w fazie amyloidowej spadek wartości wszystkich badanych parametrów, tj. liczby limfocytów T i B, ich aktywności metabolicznej, aktywności fagocytarnej leukocytów, poziomu dopełniacza, lizozymu i przeciwciał seroneutralizujących wirus chA. Immunorekonstrukcyjny wpływ badanych immunostymulatorów był większy w drugiej fazie - amyloidowej i przejawiał się zmniejszeniem odkładania złogów amyloidu w narządach, co oznacza, że wymierna skuteczność preparatu „TFX-Polfa" była wyższa niż lewamizolu.

EN

The effect of levamisole and „TFX-Polfa" preparation on the immunological system reactivity concerning cellular and humoral immunity, specific and non-specific, was determined in the course of experimental amyloidosis induced by means of sodium caseinate injected intramuscularly. The humoral immunity was induced using attenuated ADV vaccine. The research results show that the values of all examined parameters, ie the number of T and В lymophocytes, their metabolic activity, phagocytic activity of leucocytes, the levels of complement, lysozyme and seroneutralising antibodies for ADV increased at the stage of pre-amyloidosis and decreased at that of amyloidosis. The immunoreconstructive effect of examined immunostimulators was bigger in the phase of amyloidosis and was revealed by decrease in deposit accumulation in the organs; the efficiency of „TFX-Polfa" preparation was higher than that of levamisole.