Wyniki wyszukiwania

1

Expression of the type 1 metalloproteinase in the rat hippocampus after the intracerebroventricular injection of beta-amyloid peptide (25-35)

100%

Ierusalimsky V. N., Kuleshova E. P., Balaban P. M.

Acta Neurobiologiae Experimentalis

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2013

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tom 73

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nr 4

The expression of matrix metalloproteinase of the first type was studied in frontal sections of the adult rat brain one month after a single intracerebroventricular injection of P-amyloid peptide (25-35), which is known to be a well-known model of the development of Alzheimer's disease. Brain sections were stained immunocytochemically to detect MMP-1 expression, and histologically to reveal the state of hippocampal neurons. Administration of P-amyloid peptide induced a significant degeneration of cells in the dorsal hippocampus. This was demonstrated by a significant decrease in the total number of cells and by the appearance of acidophilic neurons of altered (often triangular) shape. Altered cells were most often found in the hippocampal field CA3, and in a smaller quantity in the CA1 field. MMP-1-like immunoreactivity was found in the same hippocampal areas, the staining being restricted to the cells of altered shape (staining of somata and primary neurites). The data suggest possible involvement of the type 1 metalloproteinase in the development of Alzheimer's disease.

2

Increase of cerebral blood flow in rats after human beta-amyloid peptide infusion

100%

Pluta R., Oseka M., Januszewski S., Misicka A., Lipkowski A. W., Barcikowska M., Kozniewska E.

Folia Morphologica

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1996

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tom 55

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nr 4

3

Targeting BACE with small inhibitory nucleic acids - a future for Alzheimer's disease therapy?

100%

Nawrot B.

Acta Biochimica Polonica

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2004

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tom 51

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nr 2

ß-Secretase, a ß-site amyloid precursor protein (APP) cleaving enzyme (BACE), participates in the secretion of ß-amyloid peptides (Aß), the major components of the toxic amyloid plaques found in the brains of patients with Alzheimer's disease (AD). According to the amyloid hypothesis, accumulation of Aß is the primary influence driving AD pathogenesis. Lowering of Aß secretion can be achieved by decreasing BACE activity rather than by down-regulation of the APP substrate protein. Therefore, ß-secretase is a primary target for anti-amyloid therapeutic drug design. Several approaches have been undertaken to find an effective inhibitor of human ß-secretase activity, mostly in the field of peptidomimetic, non-cleavable substrate analogues. This review describes strategies targeting BACE mRNA recognition and its down-regulation based on the antisense action of small inhibitory nucleic acids (siNAs). These include antisense oligonucleotides, catalytic nucleic acids — ribozymes and deoxyribozymes — as well as small interfering RNAs (siRNAs). While antisense oligonucleotides were first used to identify an aspartyl protease with S-secretase activity, all the strategies now demonstrate that siNAs are able to inhibit BACE gene expression in a sequence-specific manner, measured both at the level of its mRNA and at the level of protein. Moreover, knock-down of BACE reduces the intra- and extracellular population of Aß40 and Aß42 peptides. An anti-amyloid effect of siNAs is observed in a wide spectrum of cell lines as well as in primary cortical neurons. Thus targeting BACE with small inhibitory nucleic acids may be beneficial for the treatment of Alzheimer’s disease and for future drug design.

4

A promising rat model of Alzheimer's disease-like neuropathology

100%

Pluta R., Misicka A., Barcikowska M., Januszewski S., Lipkowski A. W.

Folia Morphologica

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1996

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tom 55

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nr 4

5

In vitro studies of activation of phagocytic cells by bioactive peptides

84%

Stoika R. S., Lutsik M. D., Barska M. L., Tsyrulnyk A. A., Kashchak N. I.

Journal of Physiology and Pharmacology

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2002

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tom 53

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nr 4,1

The effect of formyl chemotactic peptide (fCTP, fMet-Leu-Phe), ß-amyloid peptides (ß-AP, 1-42, 1-16 and 25-35), and bradykinin (BK) on functional activity of phagocytic cells has been investigated. Wheat germ agglutinin (WGA) was also used as a model membrane binding agent of polypeptide nature. Murine monocyte- macrophage cell line J774.2 and normal human blood polymorphonuclear (PMN) cells were used as target phagocytic cells. Their activity was quantitatively estimated by measuring phagocytosis of killed yeast cells. ß-AP (1-41) maximally stimulated phagocytosis at 0.1 µg/ml, BK - at 1.0 µg/ml, and fCTP - at 2.0 µg/ml. ß-AP (1-16) and ß-AP (25-35) were inactive in used test-systems. Phagocytosis-inducing activity of ß-AP (1-42) and BK reached maximal levels in 2 h and decreased after 4-6 h of incubation. Phagocytosis numbers were compared with the indicators of phagocytic cell activation, such as absorption of neutral red dye, glucose utilization, production of super-oxide anion (NBT-test) and nitrite accumulation (indicator of NO production). NBT-test, which may be related to the killing ability of phagocytic cells towards the ingested objects, was positive only in stimulated PMN leukocytes, while the nitrite accumulation was detected only in stimulated macrophages. Nitrite accumulation in macrophages was markedly induced by lipopolysaccharide and to a lower extent by 0.5 µg/ml ß-AP (1-42). In high dose (5.0 µg/ml) ß-AP suppressed nitrite accumulation in macrophages stimulated by lipopolysaccharide. Other studied peptides were inactive in inducing nitrite accumulation. Transforming growth factor type ß suppressed phagocytic activity of PMN cells activated by ß-AP or WGA. The anti-inflammatory drugs (indomethacin and L-lysine aescinate) inhibited ß-AP (1- 42)-induced phagocytosis. The interrelations between the regulatory pathways of BK, ß-AP and fCTP are discussed.

6

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Gamma-secretase complex in plant cells

67%

Skrzypczak T., Smolarkiewicz M., Wojtaszek P.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 3

7

Aging and beta-amyloid peptides decrease cholinergic receptor-mediated calcium increase in brain cortex synaptoneurosomes

67%

Samochocki M.

Acta Neurobiologiae Experimentalis

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1998

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tom 58

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nr 1

8

Alzheimer's beta-amyloid peptide as a source of neurotoxic free radicals: the role of structural effects

59%

Pogocki D.

Acta Neurobiologiae Experimentalis

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2003

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tom 63

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nr 2

Ograniczanie wyników

Expression of the type 1 metalloproteinase in the rat hippocampus after the intracerebroventricular injection of beta-amyloid peptide (25-35)

Increase of cerebral blood flow in rats after human beta-amyloid peptide infusion

Targeting BACE with small inhibitory nucleic acids - a future for Alzheimer's disease therapy?

A promising rat model of Alzheimer's disease-like neuropathology

In vitro studies of activation of phagocytic cells by bioactive peptides

Gamma-secretase complex in plant cells

Aging and beta-amyloid peptides decrease cholinergic receptor-mediated calcium increase in brain cortex synaptoneurosomes

Alzheimer's beta-amyloid peptide as a source of neurotoxic free radicals: the role of structural effects