Wyniki wyszukiwania

1

Quantification of selected elements in ovarian tumours and their potentials as a tissue classifier

100%

Chmura L., Grzelak M., Czyzycki M., Wrobel P., Brzyszczyk M., Jach R., Adamek D., Lankosz M.

Journal of Physiology and Pharmacology

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2017

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tom 68

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nr 5

2

Inhibition of serum amyloid A protein amyloid formation

84%

Sosnowska M., Jankowska E.

Acta Neurobiologiae Experimentalis

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2013

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tom 73

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nr 1

The acute-phase protein serum amyloid A (SAA) is present in the bloodstream at the concentration below 1 µM under physiological conditions, but its level increases significantly during the acute-phase response following infection or inflammatory condition. A consequence of the long-term elevated SAA concentration is deposition of normally soluble serum amyloid A in the form of insoluble fibrils, impairing tissue structure and function. These deposits cause development of a secondary type amyloidosis, called amyloid A protein (AA) amyloidosis, which results in a death of thousands of people per annum around the world. The ability of SAA to form amyloids seems to be connected with the N-terminal portion of the molecule. The capacity of the synthetic peptides derived from the N-terminal sequence of human or mice SAA to form fibrils in vitro proves that the most amyloidogenic region is embedded within the protein’s first 15 amino acids. We decided therefore to use peptides consisting of 11–15 amino acids and the sequence derived from the N-terminus of the parent aggregating protein as a research tool for investigation of the molecular recognition and self-assembly mechanisms that promote the formation of SAA amyloid fibrils deposits. In this study, we tested the hypothesis that non-aggregating very short peptides derived from SAA sequence would interact with the analogous region in the protein molecule or its aggregation-prone N-terminal fragment, and block its assembly into oligomers and amyloid fibrils. We designed and synthesized a peptide with the sequence 1RSFFS5, derived from the human SAA primary structure, and then tested it as a potential inhibitor of the aggregation process of SAA protein. The hypothesis about the role of aromatic interactions in amyloid fibril formation led us to test another peptide: 17LVFF20, which is derived from the sequence of Aβ. We tested propensity of the N-terminal segment (1–15) of mice SAA for amyloid fibrils formation, incubating it either alone or together with the potential inhibitors. Thioflavin T (ThT) fluorescence test was used to detect amyloid fibrils formation. These tests confirmed that the designed peptides are able to diminish propensity of the aggregation-prone SAA peptides to form amyloid fibrils. There are currently no effective medical treatment of diseases associated with the systemic amyloidosis. We believe that results of the presented project open up new possibilities in designing compounds that are able to prevent formation of amyloid deposits and could be a starting point for the design of peptidomimetic molecules more suitable as potential drugs. The work was supported by grant NCN nr 2011/03/N/NZ5/01460 and grant BMN No 538-8440-1042-12.

3

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The structure of secretory tissue of the stigma and septal nectaries as well as nectar secretion of flowers of Hosta fortunei Baker L. H. Bailey (Funkiaceae)

67%

Chwil M.

Acta Agrobotanica

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2009

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tom 62

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nr 1

A study of Hosta fortunei Baker L. H. Bailey (Funkiaceae) flowers was conducted in the years 2007 – 2008. The flower life span and flowering duration as well as the nectar production rate were determined. The structure of the tissues of the stigma and nectary was investigated using stereoscopic, light and scanning electron microscopy (SEM). The plants flowered over a period of five weeks. Flowers of H. fortunei lived two days, on the average. Developed a pistil with an elongated ovary terminating in a discal stigma. On the surface of the stigma, unicellular glandular trichomes grew densely, composed of a stalk with a length of 113 – 213 μm and a head which was characterised by a large diameter range of 54 – 96 μm. The cuticle on the apical surface of a part of the trichomes was smooth, whereas it was striated on the stalk. Their protoplast was characterised by dense cytoplasm and weak vacuolisation. In the head of the trichomes fatty substances were accumulated. Septal nectaries occurred in the ovary of the superior pistil. Nectar was exuded onto the surface through three openings, situated in the upper part of the ovary of the pistil. At these places, epidermal cells formed a smooth or slightly wrinkled cuticle. The outer walls of the cells of the epidermis covering the duct accumulating nectar were thick. The glandular tissue of the nectary was made up of 2 layers of different-shaped, thin-walled cells and a deeply stained protoplast. They contained dense cytoplasm and a large, frequently lobate nucleus. At the final stage of secretion, fine vacuoles were observed in the cytoplasm of the glandular cells. Nectar secretion was abundant. In its initial stage, secretion droplets, increasing during the activity of the glandular tissue, were observed on the epidermis surface around the nectar openings. The weight of nectar from 10 flowers was 92.41 mg. The sugar concentration in the nectar was within a range of 23% – 30%, with an average value of 26%. Sugar yield was 23.83 mg/from 10 flowers.

4

The distribution and structure of cclerenchyma in the pericarp of Ranunculus sceleratus L.

67%

Trzaski L.

Acta Biologica Silesiana

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1993

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tom 24

62-72

5

Wyznaczanie minimalnej liczby komorek do analizy geometrycznych parametrow struktury tkanki bulwy ziemniaka

67%

Konstankiewicz K., Garncarz M., Krol A., Pawlak K.

Acta Agrophysica

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2003

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tom 02

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nr 3[97]

579-587

6

Wlasciwosci mechaniczne tkanki jablka w odniesieniu do jej struktury

59%

Jakubczyk E., Lewicki P. P.

Acta Agrophysica

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2003

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tom 02

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nr 3[97]

549-557

Ograniczanie wyników

2 Acta Agrophysica

1 Acta Agrobotanica

1 Acta Biologica Silesiana

1 Acta Neurobiologiae Experimentalis

1 Journal of Physiology and Pharmacology

1 Adamek D.

1 Brzyszczyk M.

1 Chmura L.

1 Chwil M.

1 Czyzycki M.

1 Garncarz M.

1 Grzelak M.

1 Jach R.

1 Jakubczyk E.

1 Jankowska E.

1 Konstankiewicz K.

1 Krol A.

1 Lankosz M.

1 Lewicki P. P.

1 Pawlak K.

1 Sosnowska M.

1 Trzaski L.

1 Wrobel P.

1 2017

1 2013

1 2009