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Wyszukujesz frazę "Sobczak, Magdalena" wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
Myosin VI is associated with secretory granules and is present in the nucleus in adrenal medulla chromaffin cells
Autorzy:
Majewski, Łukasz
Sobczak, Magdalena
Rędowicz, Maria
Powiązania:
https://bibliotekanauki.pl/articles/1040436.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
myosin VI
chromaffin granules
PC12 cells
Golgi apparatus
Opis:
Myosin VI (MVI) is the only known myosin walking towards minus end of actin filaments. Here, MVI, but not myosins IB or IIB, was detected in chromaffin granules isolated from bovine medulla and found to be tightly associated with the granule apical surface. MVI also localized to secretory granules within rat pheochromocytoma PC12 cells as well as to the Golgi apparatus, endoplasmic reticulum and clathrin-coated pits. Notably, it was also found in the nucleus. RT-PCR revealed that MVI splice variants with a large insert (LI), characteristic of polarized cells, were barely detectable in PC12 cells, whereas variants with a small insert (SI) were the major isoforms. The presented data indicate that MVI in adrenal medulla cells is engaged in secretory vesicle trafficking within the cytoplasm and possibly also involved in transport within the nucleus.
Źródło:
Acta Biochimica Polonica; 2010, 57, 1; 109-114
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Calcium-binding calmyrin forms stable covalent dimers in vitro, but in vivo is found in monomeric form.
Autorzy:
Sobczak, Adam
Blazejczyk, Magdalena
Piszczek, Grzegorz
Zhao, Gang
Kuznicki, Jacek
Wojda, Urszula
Powiązania:
https://bibliotekanauki.pl/articles/1041431.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
covalent dimer
calmyrin monomer
human lymphocytes
EF-hand calcium-binding proteins
Opis:
The EF-hand Ca^(2+)-binding protein calmyrin is expressed in many tissues and can interact with multiple effector proteins, probably as a sensor transferring Ca^(2+) signals. As oligomerization may represent one of Ca^(2+)-signal transduction mechanisms, we characterised recombinant calmyrin forms using non-reducing SDS/PAGE, analytical ultracentrifugation and gel filtration. We also aimed at identification of biologically active calmyrin forms. Non-reducing SDS/PAGE showed that in vitro apo- and Ca^(2+)-bound calmyrin oligomerizes forming stable intermolecular disulfide bridges. Ultracentrifugation indicated that at a 220 µM initial protein concentration apo-calmyrin existed in an equilibrium of a 21.9 kDa monomer and a 43.8 kDa dimer (trimeric or tetrameric species were not detected). The dimerization constant was calculated as Ka = 1.78 × 103 M^(-1) at 6oC. Gel filtration of apo- and Ca^(2+)-bound calmyrin at a 100 µM protein concentration confirmed an equilibrium of a monomer and a covalent dimer state. Importantly, both monomer and dimer underwent significant conformational changes in response to binding of Ca^(2+). However, when calmyrin forms were analyzed under non-reducing conditions in cell extracts by Western blotting, only monomeric calmyrin was detected in human platelets and lymphocytes, and in rat brain. Moreover, in contrast to recombinant calmyrin, crosslinking did not preserve any dimeric species of calmyrin regardless of Ca^(2+) concentrations. In summary, our data indicate that although calmyrin forms stable covalent dimers in vitro, it most probably functions as a monomer in vivo.
Źródło:
Acta Biochimica Polonica; 2005, 52, 2; 469-476
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Functional characteristic of PC12 cells with reduced microsomal glutathione transferase 1
Autorzy:
Sobczak, Monika
Boczek, Tomasz
Ferenc, Bozena
Taha, Joanna
Kozaczuk, Anna
Wiktorska, Magdalena
Sacewicz-Hofman, Izabela
Niewiarowska, Jolanta
Zylinska, Ludmila
Powiązania:
https://bibliotekanauki.pl/articles/1042731.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
necrosis
pc12 cells
signaling pathways
microsomal glutathione transferase 1
pseudoneuronal phenotype
metastatic potential
Opis:
Microsomal glutathione transferase 1 (MGST1) possesses glutathione transferase and peroxidase activities and is active in biotransformation of xenobiotics and in defense against oxidative stress. To assess MGST1 role in the development and functioning of PC12 cells, we constructed a cell line with reduced MGST1 (PC12_M). Real-time PCR and immunoblot assays showed MGST1 expression lowered to 60 % and immunocytochemical analyses demonstrated an altered concentration and distribution of the enzyme. PC12_M cells revealed a larger tendency to grow in clusters, weaker adhesion, irregular shape of bodies, short neurite outgrowth and higher percentage of necrotic cells (34 %). The total GSTs activity determined with non-specific substrate CDNB (1-chloro-2,4-dinitrobenzene) decreased by 15-20 %, whereas that with DCNB (2,4-dichloro-1-nitrobenzene), a substrate more specific for cytosolic GSTs, was similar to the one in control cells. This suggests that reduction of MGST1 cannot be compensated by other glutathione transferases. In PC12_M cells the total glutathione content was higher by 15-20 %, whereas the GSSG/GSH ratio was lower than in control cells. Moreover, the laminin-dependent migration rate was much faster in control cells than in PC12_M, suggesting some alterations in the metastatic potential of the line with suppressed MGST1. The amount of MAP kinases (p38, JNK, ERK1/2) was elevated in PC12_M cells but their phosphorylation level declined. Microarray analysis showed changed expression of several genes, which may be linked with differentiation and necrosis of PC12_M cells. Our data suggest that MGST1 could be an important regulator of PC12 cells development and might have significant effects on cell growth and proliferation, probably through altered expression of genes with different biological function.
Źródło:
Acta Biochimica Polonica; 2010, 57, 4; 589-596
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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