Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 10

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  actin
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1
Content available remote

Actin in human colon adenocarcinoma cells with different metastatic potential.

100%
Nowak D., Krawczenko A., Duś D., Malicka-Błaszkiewicz M.
Acta Biochimica Polonica
|
2002
|
vol. 49
|
issue 4
823-828
EN
Four human colon adenocarcinoma cell line variants with different metastatic potential were used to examine whether a correlation exists between actin level, state of actin polymerization and invasiveness of tumour cells. Monomeric (G), total (T) and filamentous (F) actin were determined in the cytosolic fraction of these cells. A statistically significant decrease in G actin level and increase in the state of actin polymerization (measured by F:G actin ratio) were found in the cytosol of three cell variants with higher metastatic potential and invasiveness (EB3, 3LNLN, 5W) compared with the parental cell line (LS180). Our experimental data lead to the conclusion that there is a correlation between the metastatic capacity of human colon adenocarcinoma cells and the state of actin polymerization.
2
Content available remote

Identification of actin from hepatoma Morris 5123 cells

100%
Nowak D., Kochman A., Malicka-Błaszkiewicz M.
Acta Biochimica Polonica
|
1999
|
vol. 46
|
issue 4
949-959
EN
The hepatoma Morris 5123 tumor growth is accompanied by changes in actin content and polymerization (Malicka-Błaszkiewicz et al. (1995) Mat. Med. Pol., 27, 115-118;  Nowak et al. (1995) J. Exp. Cancer Res. 14, 37-40). Presently actin isoforms from cytosol and  cytoskeleton fractions were separated by SDS/PAGE and identified with antibodies directed against different actin isoforms. Actin isolated from the cytosol by affinity chromatography on DNase I bound to agarose shows the presence of only one protein spot on 2D gel electrophoresis corresponding to the mobility of the rabbit α skeletal muscle actin (M^r 43000) and isoelectric point equal to 5.3. It interacts only with monoclonal anti β actin isoform antibodies, posing the question of differential affinity of actin isoforms to DNase I.
3
Content available remote

Gelsolin in human colon adenocarcinoma cells with different metastatic potential

100%
Litwin M., Mazur A., Nowak D., Mannherz H., Malicka-Błaszkiewicz M.
Acta Biochimica Polonica
|
2009
|
vol. 56
|
issue 4
739-743
EN
Gelsolin, one of a major actin-binding proteins, is involved in the regulation of actin cytoskeleton organization by its severing and capping activity towards actin filaments. Human colon adenocarcinoma cell line LS180 and its selected variants of different metastatic potential were used to check for a correlation between gelsolin level, its subcellular localization and the invasive capacity of cells. Based on immunoblotting experiments, a decreased level of gelsolin was detected in the most invasive 5W subline when compared to the parental cell line LS180. The intracellular distribution of actin filaments and gelsolin in colon adenocarcinoma cells was examined by confocal microscopy. In the 5W subline, unlike in the other examined cells, gelsolin was colocalized with filamentous actin at the cell periphery. In summary, in human colon adenocarcinoma cells, gelsolin level and its subcellular distribution seem to correlate with their metastatic potential.
4
Content available remote

The effect of methotrexate on actin and invasiveness of hepatoma Morris 5123 cells in culture.

100%
Otrocka M., Verschueren H., Malicka-Błaszkiewicz M.
Acta Biochimica Polonica
|
2001
|
vol. 48
|
issue 4
1051-1060
EN
Monomeric (G), total (T) and filamentous (F) actin and the state of actin polymerisation (F:G) were determined and actin filaments were visualized in hepatoma Morris 5123 cells cultured in the presence of methotrexate (MTX) at various concentration. The exposure of the cells to this drug resulted in a decrease of total and polymerised actin in cytoplasm and in some changes in actin filament organization. This coincided with a decrease of the cells' ability to migrate through Matrigel coated filters and with inhibition of tumour formation after reimplantation of the methotrexate treated cells to experimental rats.
5
Content available remote

Is MLC phosphorylation essential for the recovery from ROCK inhibition in glioma C6 cells?

88%
Korczyński J., Sobierajska K., Krzemiński P., Wasik A., Wypych D., Pomorski P., Kłopocka W.
Acta Biochimica Polonica
|
2011
|
vol. 58
|
issue 1
125-130
EN
Inhibition of Rho-associated protein kinase (ROCK) activity in glioma C6 cells induces changes in actin cytoskeleton organization and cell morphology similar to those observed in other types of cells with inhibited RhoA/ROCK signaling pathway. We show that phosphorylation of myosin light chains (MLC) induced by P2Y2 receptor stimulation in cells with blocked ROCK correlates in time with actin cytoskeleton reorganization, F-actin redistribution and stress fibers assembly followed by recovery of normal cell morphology. Presented results indicate that myosin light-chain kinase (MLCK) is responsible for the observed phosphorylation of MLC. We also found that the changes induced by P2Y2 stimulation in actin cytoskeleton dynamics and morphology of cells with inhibited ROCK, but not in the level of phosphorylated MLC, depend on the presence of calcium in the cell environment.
6
Publication available in full text mode
Content available

Immunophenotypic characteristics and karyotype analysis of bone marrow-derived mesenchymal stem cells of rabbits duringin vitro cultivation

75%
Mazurkevych A., Kharkevych Y., Jakubczak A., Gryzinska M., Malyuk M., Bezdieniezhnykh N., Starodub L.
Polish Journal of Veterinary Sciences
|
2017
|
issue 4
7
Content available remote

Designing primers potentially specific to Entamoeba gingivalis genes

75%
Abramek J.
Current Issues in Pharmacy and Medical Sciences
|
2015
|
vol. 28
|
issue 3
159-163
EN
Entamoeba gingivalis normally exists in the human oral cavity, namely in the gums, and brings about some specific diseases. However, it can also trigger some more serious illnesses. Among these are infections of the genital tract, acute osteomyelitis of the mandible and pulmonary abscess. Entamoeba gingivalis identification by light microscopy is difficult, hence polymerase chain reaction (PCR) is used. The contemporary primers for PCR are complement to 18S rRNA. This article informs the reader of the process that was involved in designing new primers for three genes which were thought to be present on the Entamoeba gingivalis genome, but their sequences were unknown. The newly obtained sequences of primers have better properties for identification purposes, compared to these which are currently used.
8
Publication available in full text mode
Content available

Modyfikacje potranslacyjne aktyny

63%
Rędowicz M.
Kosmos
|
2018
|
vol. 67
|
issue 1
43-55
PL
Aktyna, komponent cytoszkieletu komórek eukariotycznych, to jedno z białek najistotniejszych dla funkcjonowania organizmów i najlepiej zachowanych w toku ewolucji. Ta globularna cząsteczka o masie cząsteczkowej około 42,3 kDa występuje zarówno w formie monomerycznej, jak i spolimeryzowanej (filamenty), a zdolność do dynamicznej reorganizacji aktyny jest niezbędna dla życia komórki. Przejście pomiędzy obiema formami jest możliwe dzięki precyzyjnej w czasie i przestrzeni, dynamicznej regulacji organizacji aktyny przez szereg białek wiążących się zarówno z monomerami, jak i filamentami aktyny. Istotnym czynnikiem wpływającym na stopień spolimeryzowania aktyny są także liczne modyfikacje potranslacyjne tego białka. Niniejszy artykuł przeglądowy jest poświęcony omówieniu tego obszernego i wciąż mało poznanego zagadnienia, a w szczególności opisowi jakim modyfikacjom ulega aktyna i w jaki sposób modyfikacje te wpływają na strukturę i funkcje tego wyjątkowego białka.
EN
Actin, a constituent of the cytoskeleton of eukaryotic cells, is one of the most important as well as best evolutionary conserved proteins. This globular protein with molecular mass of ~42.3 kDa exists in the cell both in the monomeric and filamentous form, and ability to undergo dynamic reorganization of these two forms is absolutely crucial for cell survival. The monomer-filament transition, precisely controlled in time and space, is possible due to interaction of actin with a panoply of proteins binding to either monomeric or filamentous actin. Yet another factor is affecting actin organization, namely numerous posttranslational modifications. This review article is devoted to presentation of this broad and still unrecognized topic with emphasis on description of the type of actin modifications and how they affect actin structure and function.
9
Publication available in full text mode
Content available

Filamenty cienkie i mikrofilamenty - funkcjonalne kompleksy aktyny z tropomiozyną

63%
Moraczewska J.
Kosmos
|
2018
|
vol. 67
|
issue 1
31-41
PL
Aktyna jest uniwersalnym białkiem o strukturze dobrze zachowanej w toku ewolucji. W komórkach aktyna istnieje w równowadze pomiędzy formą monomeryczną i filamentową. Pomimo zachowanej w toku ewolucji struktury, aktyna pełni zdumiewająco wiele różnorodnych funkcji. Jest to możliwe dzięki zdolności aktyny do oddziaływania z wieloma białkami, wśród których znajdują się motory miozynowe oraz białka regulujące dynamiczną polimeryzację i depolimeryzację aktyny. Nadrzędnymi regulatorami filamentów aktynowych są tropomiozyny, rodzina superhelikalnych białek, które polimeryzują wzdłuż filamentowej aktyny, dzięki czemu stabilizują filamenty zapobiegając ich depolimeryzacji oraz kontrolują dostęp i aktywność białek wiążących aktynę. Tropomiozyny działają jako "stróże" filamentu, którzy kontrolują oddziaływania aktyny, co prowadzi do segregacji białek wiążących aktynę do swoistych przedziałów komórkowych gdzie białka te realizują określone funkcje komórkowe. W artykule zostały omówione zależne od tropomiozyny mechanizmy regulacji oddziaływań aktyny z niektórymi miozynami oraz z Arp2/3 i kofiliną - białkami, które inicjują rozgałęzianie, polimeryzację i depolimeryzację filamentów aktynowych.
EN
Actin is a universal protein highly conserved in evolution. In cells, actin exists in equilibrium between a monomeric and filamentous form. In spite of a conservative structure, actin plays amazingly versatile functions. This is possible due to its interactions with numerous actin-binding proteins, among them with myosin motors and proteins regulating dynamic polymerization and depolymeriation of actin. Tropomyosins, superhelical proteins, which polymerize along the filament and stabilize actin by preventing its depolymerization, are superior actin filament regulators. Tropomyosins control the access and activity of various actin-binding proteins. Tropomyosins act thus as actin “gate-keepers” which control actin interactions leading to the segregation of actin-binding proteins into specific cell compartments where they perform specific cellular functions. This article discusses tropomyosin-dependent mechanisms of regulation of actin interactions with some myosins as well as Arp2/3 and cofilin - the proteins, which initiate branching, polymerization and depolymerization of actin filaments.
10
Publication available in full text mode
Content available

Aktyna i miozyny w jądrze komórkowym

51%
Nowak J., Rędowicz M.
Kosmos
|
2018
|
vol. 67
|
issue 1
75-93
PL
Aktyna i miozyna to białka kojarzone przede wszystkim z ich kluczową rolą w generacji skurczu mięśni. Natomiast poza izoformami charakterystycznymi dla mięśni są również izoformy aktyny i miozyny, które występują we wszystkich typach komórek i tkanek (patrz artykuł Suszek i współaut. w tym zeszycie KOSMOSU). Badania prowadzone w ostatnich dwóch dekadach wykazały niezbicie, że zarówno aktyna (i szereg białek wiążących aktynę) oraz liczne miozyny (przedstawiciele rodzin I, II, V, VI, XVI i XVIII) lokalizują się w jądrze komórkowym gdzie są zaangażowane w procesy transkrypcji i naprawy DNA, transport w nukleoplazmie oraz import i eksport jądrowy, a także w utrzymywanie architektury jądra. Niniejszy artykuł opisuje dotychczasowy stan wiedzy o roli układu akto-miozynowego w jądrze komórkowym.
EN
Actin and myosins are the proteins mainly known from their key roles in muscle contraction. However, besides typical muscle isoforms there are actins and myosins that are present in all cell and tissue types. Studies performed within the last two decades have irrefutably shown that both the cytoplasmic actin isoforms (along with numerous actin-binding proteins) as well as many myosins (representing class I, II, V, VI, XVI and XVIII) are present within the nucleus. They play important roles in nuclear processes as they are involved in transcription and DNA repair, intranuclear transport as well as nuclear import and export, and in maintenance of nuclear architecture. This article describes the current knowledge on the acto-myosin system in this biggest cellular compartment.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.