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Tytuł:
Annexins - calcium- and membrane-binding proteins in the plant kingdom Potential role in nodulation and mycorrhization in Medicago truncatula
Autorzy:
Talukdar, Tanuja
Gorecka, Karolina
de Carvalho-Niebel, Fernanda
Downie, J
Cullimore, Julie
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1040554.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
plant annexins
Nod factors
Medicago truncatula
Opis:
Annexins belong to a family of multi-functional membrane- and Ca2+-binding proteins. The characteristic feature of these proteins is that they can bind membrane phospholipids in a reversible, Ca2+-dependent manner. While animal annexins have been known for a long time and are fairly well characterized, their plant counterparts were discovered only in 1989, in tomato, and have not been thoroughly studied yet. In the present review, we discuss the available information about plant annexins with special emphasis on biochemical and functional properties of some of them. In addition, we propose a link between annexins and symbiosis and Nod factor signal transduction in the legume plant, Medicago truncatula. A specific calcium response, calcium spiking, is an essential component of the Nod factor signal transduction pathway in legume plants. The potential role of annexins in the generation and propagation of this calcium signal is considered in this review. M. truncatula annexin 1 (MtAnn1) is a typical member of the plant annexin family, structurally similar to other members of the family. Expression of the MtAnn1 gene is specifically induced during symbiotic associations with both Sinorhizobium meliloti and the mycorrhizal fungus Glomus intraradices. Furthermore, it has been reported that the MtAnn1 protein is preferentially localized at the nuclear periphery of rhizobial-activated cortical cells, suggesting a possible role of this annexin in the calcium response signal elicited by symbiotic signals from rhizobia and mycorrhizal fungi.
Źródło:
Acta Biochimica Polonica; 2009, 56, 2; 199-210
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Calcium- and proton-dependent relocation of annexin A6 in Jurkat T cells stimulated for interleukin-2 secretion
Autorzy:
Podszywalow-Bartnicka, Paulina
Strzelecka-Kiliszek, Agnieszka
Bandorowicz-Pikula, Joanna
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1041071.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
interleukin-2
ionomycin
calcium
annexin A6
Jurkat T cells
vesicular traffic
Opis:
Annexin A6 (AnxA6) is a Ca2+-dependent membrane-binding protein involved in vesicular traffic. The likely participation of AnxA6 in the response of lymphocytes to Ca2+ signals has not been investigated yet. The present study focuses on intracellular relocation of AnxA6 in human Jurkat T lymphoblasts upon stimulation followed by transient increase of intracellular [Ca2+] and exocytosis of interleukin-2 (IL-2). Stimulation of the cells under different experimental conditions (by lowering pH and/or by rising extracellular [Ca2+] in the presence of ionomycin) induced time-dependent transients of intracellular [Ca2+] and concomitant changes in AnxA6 intracellular localization and in IL-2 secretion, with only minor effects on cell viability and apoptosis. In resting conditions (in the presence of EGTA or with no ionophore) AnxA6 was localized uniformly in the cytosol, whereas it translocated to vesicular structures beneath the plasma membrane within 5 min following stimulation of Jurkat T cells and rise of intracellular [Ca2+] at pH 7.4. Lowering the extracellular pH value from 7.4 to 6.0 significantly enhanced this process. AnxA6 changed its location from the cytosol to the secretory granules and early endosomes which seem to represent membranous targets for annexin. In conclusion, AnxA6 is sensitive to variations in intracellular [Ca2+] upon stimulation of Jurkat T cells, as manifested by a switch in its intracellular localization from the cytosol to vesicular structures located in close proximity to the plasma membrane, suggestive of participation of AnxA6 in calcium- and proton-dependent secretion of cytokines by lymphocytes.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 261-271
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Hipotetyczna rola autokatalitycznych właściwości kwasów nukleinowych w procesie biogenezy
Hypotetical role of autocatalytic properties of nucleic acids in biogenesis
Autorzy:
Adamala, Katarzyna
Pikuła, Sławomir
Powiązania:
https://bibliotekanauki.pl/articles/1199450.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Przyrodników im. Kopernika
Opis:
Ribozymes are catalytic RNA molecules. In this article their various types and activities in contrasts with corresponding DNA molecules are briefly characterized. The revolutionary discovery of the autocatalytic properties of nucleic acids by theNobel Prizewinners, Sidney Altman, Thomas R. CECH and their co-workers, led to the hypothesis of RNA world and to speculation on the role of RNA in the origin of life and the early stages of its evolution on Earth. The possible role of the autocatalytic properties of nucleic acids in prebiotic evolution is, therefore, discussed.
Źródło:
Kosmos; 2004, 53, 2; 123-131
0023-4249
Pojawia się w:
Kosmos
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Woda morska i dziury w błonach - Nagroda Nobla z chemii za rok 2003
Sea water and holes in membranes - Nobel Prize in chemistry for 2003
Autorzy:
Pikuła, Sławomir
Powiązania:
https://bibliotekanauki.pl/articles/1199380.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Przyrodników im. Kopernika
Opis:
The Nobel Prize in Chemistry for 2003 was awarded by the Royal Swedish Academy of Sciences in equal parts to two American scientists: Peter Agre from Johns Hopkins University School of Medicine in Baltimore, for the discovery of the water channels, aquaporins, and Roderick MacKinnon from Howard Hughes Medical Institute, the Rockefeller University in New York, for structural and mechanistic studies of the ion channels, especially the potassium and chloride channels. The major breakthrough made by the two scientists in our understanding of water and ion transport processes through biological membranes are briefly described in this editorial note, and the list of their recent selected publications is provided.
Źródło:
Kosmos; 2004, 53, 3-4; 243-249
0023-4249
Pojawia się w:
Kosmos
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The network of calcium regulation in muscle.
Autorzy:
Martonosi, Anthony
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1043643.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
sodium:calcium exchanger
calcium pump
calcium homeostasis
calcium channel
skeletal and cardiac muscles
mitochondria
sarcoplasmic reticulum
excitation-contraction coupling
Opis:
In this review the molecular characteristics and reaction mechanisms of different Ca2+ transport systems associated with various membranes in muscle cells will be summarized. The following topics will be discussed in detail: a brief history of early observations concerning maintenance and regulation of cellular Ca2+ homeostasis, characterization of the Ca2+ pumps residing in plasma membranes and sarco(endo)plasmic reticulum, mitochondrial Ca2+ transport, Ca2+-binding proteins, coordinated expression of Ca2+ transport systems, a general background of muscle excitation-contraction coupling with emphasis to the calcium release channels of plasma membrane and sarcoplasmic reticulum, the structure and function of dihydropyridine and ryanodine receptors of skeletal and cardiac muscles, and finally their disposition in various types of muscles.
Źródło:
Acta Biochimica Polonica; 2003, 50, 1; 1-30
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The roles of annexins and alkaline phosphatase in mineralization process.
Autorzy:
Balcerzak, Marcin
Hamade, Eva
Zhang, Le
Pikula, Slawomir
Azzar, Gérard
Radisson, Jacqueline
Bandorowicz-Pikula, Joanna
Buchet, Rene
Powiązania:
https://bibliotekanauki.pl/articles/1043372.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
mineralization
hydroxyapatite
alkaline phosphatase
annexin
matrix vesicle
Opis:
In this review the roles of specific proteins during the first step of mineralization and nucleation are discussed. Mineralization is initiated inside the extracellular organelles-matrix vesicles (MVs). MVs, containing relatively high concentrations of Ca2+ and inorganic phosphate (Pgi), create an optimal environment to induce the formation of hydroxyapatite (HA). Special attention is given to two families of proteins present in MVs, annexins (AnxAs) and tissue-nonspecific alkaline phosphatases (TNAPs). Both families participate in the formation of HA crystals. AnxAs are Ca2+- and lipid-binding proteins, which are involved in Ca2+ homeostasis in bone cells and in extracellular MVs. AnxAs form calcium ion channels within the membrane of MVs. Although the mechanisms of ion channel formation by AnxAs are not well understood, evidence is provided that acidic pH or GTP contribute to this process. Furthermore, low molecular mass ligands, as vitamin A derivatives, can modulate the activity of MVs by interacting with AnxAs and affecting their expression. AnxAs and other anionic proteins are also involved in the crystal nucleation. The second family of proteins, TNAPs, is associated with Pi homeostasis, and can hydrolyse a variety of phosphate compounds. ATP is released in the extracellular matrix, where it can be hydrolyzed by TNAPs, ATP hydrolases and nucleoside triphosphate (NTP) pyrophosphohydrolases. However, TNAP is probably not responsible for ATP-dependent Ca2+/phosphate complex formation. It can hydrolyse pyrophosphate (PPi), a known inhibitor of HA formation and a byproduct of NTP pyrophosphohydrolases. In this respect, antagonistic activities of TNAPs and NTP pyrophosphohydrolases can regulate the mineralization process.
Źródło:
Acta Biochimica Polonica; 2003, 50, 4; 1019-1038
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The structure of the Ca2+-ATPase of sarcoplasmic reticulum.
Autorzy:
Martonosi, Anthony
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1043610.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calcium pump
calcium homeostasis
calcium transport
skeletal and cardiac muscles
sarcoplasmic reticulum
excitation-contraction coupling
Opis:
In this article the morphology of sarcoplasmic reticulum, classification of Ca2+-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca2+-ATPase determined by electron and X-ray crystallography, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca2+-ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca2+-ATPase to the sarcoplasmic reticulum is discussed.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 337-365
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Transport functions and physiological significance of 76 kDa Ral-binding GTPase activating protein (RLIP76).
Autorzy:
Awasthi, Sanjay
Sharma, Rajendra
Yang, Yusong
Singhal, Sharad
Pikula, Slawomir
Bandorowicz-Pikula, Joanna
Singh, Shivendra
Zimniak, Piotr
Awasthi, Yogesh
Powiązania:
https://bibliotekanauki.pl/articles/1043688.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
RLIP76
RalBP1
glutathione conjugate
multidrug resistance
transport
Opis:
We have recently demonstrated that a previously known Ral-binding GTPase activating protein, RLIP76, can also catalyze ATP-dependent transport of various structurally unrelated xeno- and endobiotics irrespective of their net charge (Awasthi et al., 2000, Biochemistry, 39: 9327). RLIP76 is a non-ATP binding cassette (ABC) protein but it has two ATP-binding sites and shows basal ATPase activity which is stimulated in the presence of its transport substrates (allocrites) such as doxorubicin (DOX) and S-(2,4-dinitrophenyl) glutathione (DNP-SG). Proteoliposomes reconstituted with purified RLIP76 catalyze ATP-dependent, saturable transport of DOX, as well as of glutathione-conjugates including leukotrienes (LTC4) and the GSH-conjugate of 4-hydroxynonenal (GS-HNE). In erythrocytes the majority of transport activity for DOX, GS-HNE, and LTC4 is accounted for by RLIP76. Cells exposed to mild oxidative stress show a rapid and transient induction of RLIP76 resulting in an increased efflux of GS-HNE and acquire resistance to oxidative stress mediated toxicity and apoptosis. Cells transfected with RLIP76 acquire resistance to DOX through increased efflux of the drug suggesting its possible role in the mechanisms of drug-resistance. In this article, we discuss the significance of transport functions of RLIP76 highlighting its role in the defense mechanisms against oxidative injury, and modulation of signaling mechanisms.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 855-867
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
GTP-binding properties of the membrane-bound form of porcine liver annexin VI.
Autorzy:
Kirilenko, Aneta
Golczak, Marcin
Pikuła, Sławomir
Bandorowicz-Pikuła, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1044028.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
annexin VI
GTP-binding domain
TNP-GTP
circular dichroism
GTP binding
Opis:
Annexin VI (AnxVI) of molecular mass 68-70 kDa belongs to a multigenic family of ubiquitous Ca2+ - and phospholipid-binding proteins. In this report, we describe the GTP-binding properties of porcine liver AnxVI, determined with a fluorescent GTP analogue, 2'-(or 3')-O-(2,4,6-trinitrophenyl)guanosine 5'-triphosphate (TNP-GTP). The optimal binding of TNP-GTP to AnxVI was observed in the presence of Ca2+ and asolectin liposomes, as evidenced by a 5.5-fold increase of TNP-GTP fluorescence and a concomitant blue shift (by 17 nm) of its maximal emission wavelength. Titration of AnxVI with TNP-GTP resulted in the determination of the dissociation constant (Kd) and binding stoichiometry that amounted to 1.3 μM and 1:1 TNP-GTP/AnxVI, mole/mole, respectively. In addition, the intrinsic fluorescence of the membrane-bound form of AnxVI was quenched by TNP-GTP and this was accompanied by fluorescence resonance energy transfer (FRET) from AnxVI Trp residues to TNP-GTP. This indicates that the GTP-binding site within the AnxVI molecule is probably located in the vicinity of a Trp-containing domain of the protein. By controlled proteolysis of human recombinant AnxVI, followed by purification of the proteolytic fragments by affinity chromatography on GTP-agarose, we isolated a 35 kDa fragment corresponding to the N-terminal half of AnxVI containing Trp192. On the basis of these results, we suggest that AnxVI is a GTP-binding protein and the binding of the nucleotide may have a regulatory impact on the interaction of annexin with membranes, e.g. formation of ion channels by the protein.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 851-865
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Purification and functional reconstitution of intact ral-binding GTPase activating protein, RLIP76, in artificial liposomes.
Autorzy:
Singhal, Sharad
Singhal, Jyotsana
Cheng, JiZhong
Pikuła, Sławomir
Sharma, Rajendra
Zimniak, Piotr
Awasthi, Yogesh
Awasthi, Sanjay
Powiązania:
https://bibliotekanauki.pl/articles/1044153.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
RLIP76
glutathione-conjugate
anthracycline
transport
proteolysis
Opis:
We have recently shown that RLIP76, a ral-binding GTPase activating protein, mediates ATP-dependent transport of glutathione-conjugates (GS-E) and doxorubicin (DOX) (S. Awasthi et al., Biochemistry 39, 9327, 2000). Transport function of RLIP76 was found to be intact despite considerable proteolytic fragmentation in preparations used for those studies, suggesting either that the residual intact RLIP76 was responsible for transport activity, or that the transport activity could be reconstituted by fragments of RLIP76. If the former were true, intact RLIP76 would have a much higher specific activity for ATP-hydrolysis than the fragmented protein. We have addressed this question by comparing transport properties of recombinant RLIP76 and human erythrocyte membrane RLIP76 purified in buffers treated with either 100 or 500 μM serine protease inhibitor, PMSF. The purity and identity of recombinant and human erythrocyte RLIP76 was established by SDS/PAGE and Western-blot analysis. These studies confirmed the origin of the 38 kDa protein, previously referred to as DNP-SG ATPase, from RLIP76. Higher PMSF concentration resulted in lower yield of the 38 kDa band and higher yield of intact RLIP76 from both human and recombinant source. In contrast, the substrate-stimulated ATPase activity in presence of DNP-SG, doxorubicin, daunorubicin, or colchicine were unaffected by increased PMSF; similarly, ATP-dependent transport of doxorubicin in proteoliposomes reconstituted with RLIP76 was unaffected by higher PMSF. These results indicated that limited proteolysis by serine proteases does not abrogate the transport function of RLIP76. Comparison of transport kinetics for daunorubicin between recombinant vs human erythrocyte RLIP76 revealed higher specific activity of transport for tissue purified RLIP76, indicating that additional factors present in tissue purified RLIP76 can modulate its transport activity.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 551-562
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Alzheimers disease: Its origin at the membrane, evidence and questions.
Autorzy:
Buchet, Rene
Pikuła, Sławomir
Powiązania:
https://bibliotekanauki.pl/articles/1044315.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
β-amyloid precursor protein
membrane proteases
Alzheimer's disease
lipid composition
membrane microdomains
Opis:
Numerous results on membrane lipid composition from different regions of autopsied Alzheimer's disease brains in comparison with corresponding fractions isolated from control brains revealed significant differences in serine- and ethanolamine-containing glycerophospholipid as well as in glycosphingolipid content. Changes in membrane lipid composition are frequently accompanied by alterations in membrane fluidity, hydrophobic mismatch, lipid signaling pathways, transient formation and disappearance of lipid microdomains, changes in membrane permeability to cations and variations of other membrane properties. In this review we focus on possible implications of altered membrane composition on β-amyloid precursor protein (APP) and on proteolysis of APP leading eventually to the formation of neurotoxic β-amyloid (Aβ) peptides, the major proteinaceous component of extracellular senile plaques, directly involved in Alzheimer's disease pathogenesis.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 725-733
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
10-Undecynoic acid, an inhibitor of cytochrome P450 4A1, inhibits ethanolamine-specific phospholipid base exchange reaction in rat liver microsomes
Autorzy:
Lenart, Jacek
Pikuła, Sławomir
Powiązania:
https://bibliotekanauki.pl/articles/1044558.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1999, 46, 1; 203-210
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Affinity labeling of annexin VI with a triazine dye, Cibacron blue 3GA. Probable interaction of the dye with C-terminal nucleotide-binding site within the annexin molecule
Autorzy:
Danieluk, Małgorzata
Buś, Renata
Pikuła, Sławomir
Bandorowicz-Pikuła, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1044526.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1999, 46, 2; 419-429
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Wyświetlanie 1-15 z 21

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