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Canine renal amyloidosis: a case report

100%

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

Medycyna Weterynaryjna

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2018

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tom 74

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nr 05

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.

2

Structural basis of negative cooperativity in transthyretin

100%

Neumann P., Cody V., Wojtczak A.

Acta Biochimica Polonica

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2001

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tom 48

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nr 4

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.

3

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Amyloidogenic proteins and occurrence of different amyloidosis in different animal species

84%

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

Acta Scientiarum Polonorum. Zootechnica

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2020

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tom 19

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nr 3

4

3D domain swapping, protein oligomerization, and amyloid formation

84%

Jaskolski M.

Acta Biochimica Polonica

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2001

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tom 48

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nr 4

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.

5

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

67%

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

Journal of Physiology and Pharmacology. Supplement

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2007

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tom 58

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nr 5

6

Amyloidosis and the acute phase response

67%

Sipe J. D.

Folia Histochemica et Cytobiologica

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1992

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tom 30

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nr 4

7

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

67%

Liberski P. P.

Acta Neurobiologiae Experimentalis

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1993

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tom 53

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nr 1

8

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

51%

Rotkiewicz Z.

Acta Academiae Agriculturae ac Technicae Olstenensis. Veterinaria

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1995

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tom 22,Suppl.B

1-59

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.

Ograniczanie wyników

Canine renal amyloidosis: a case report

Structural basis of negative cooperativity in transthyretin

Amyloidogenic proteins and occurrence of different amyloidosis in different animal species

3D domain swapping, protein oligomerization, and amyloid formation

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

Amyloidosis and the acute phase response

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

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