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1

Woda morska i dziury w błonach - Nagroda Nobla z chemii za rok 2003

100%

Pikuła S.

Kosmos

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2004

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vol. 53

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issue 3-4

243-249

EN

Summary 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.

2

Hipotetyczna rola autokatalitycznych właściwości kwasów nukleinowych w procesie biogenezy

64%

Adamala K., Pikuła S.

Kosmos

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2004

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vol. 53

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issue 2

123-131

EN

Summary 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.

3

Alzheimer's disease: Its origin at the membrane, evidence and questions.

64%

Buchet R., Pikuła S.

|

2000

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vol. 47

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issue 3

725-733

EN

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.

4

10-Undecynoic acid, an inhibitor of cytochrome P450 4A1, inhibits ethanolamine-specific phospholipid base exchange reaction in rat liver microsomes

63%

Lenart J., Pikuła S.

Acta Biochimica Polonica

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1999

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vol. 46

|

issue 1

203-210

5

Is the glutathione conjugate of trans-4-hydroxy-2-nonenal transported by the multispecific organic anion transporting-ATPase of human erythrocytes?

51%

Dygas A., Makowski P., Pikuła S.

Acta Biochimica Polonica

|

1998

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vol. 45

|

issue 1

59-65

6

The induction of cytochrome P450 isoform, CYP4A1, by clofibrate coincides with activation of ethanolamine-specific phospholipid base exchange reaction in rat liver microsomes

51%

Lenart J., Komańska I., Jasińska R., Pikuła S.

Acta Biochimica Polonica

|

1998

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vol. 45

|

issue 1

119-126

7

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

51%

Danieluk M., Buś R., Pikuła S., Bandorowicz-Pikuła J.

Acta Biochimica Polonica

|

1999

|

vol. 46

|

issue 2

419-429

8

Circular dichroism and fluorescence studies on interaction of calmodulin (CaM) with purified (Ca^2+-Mg^2+) ATPase of erythrocyte ghosts

51%

Wrzosek A., Famulski K. S., Pikuła S.

Acta Biochimica Polonica

|

1990

|

vol. 37

|

issue 1

173-176

9

GTP-binding properties of the membrane-bound form of porcine liver annexin VI.

51%

Kirilenko A., Golczak M., Pikuła S., Bandorowicz-Pikuła J.

|

2001

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vol. 48

|

issue 4

851-865

EN

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.

10

Adenosine 5'-triphosphate - a new regulator of annexin function. A hypothesis.

51%

Bandorowicz-Pikuła J., Pikuła S.

Acta Biochimica Polonica

|

1998

|

vol. 45

|

issue 3

735-744

11

Annexins and ATP in membrane traffic: A comparison with membrane fusion machinery

51%

Bandorowicz-Pikuła J., Pikuła S.

Acta Biochimica Polonica

|

1998

|

vol. 45

|

issue 3

721-733

12

Annexins- multifunctional, calcium-dependent, phospholipid-binding proteins

45%

Bandorowicz J., Pikuła S.

|

vol. 40

|

issue 3

281-293

13

Annexin VI: An intracellular target for ATP

39%

Bandorowicz-Pikuła J., Danieluk M., Wrzosek A., Buś R., René Buchet, Pikuła S.

Acta Biochimica Polonica

|

1999

|

vol. 46

|

issue 3

801-812

14

Purification and functional reconstitution of intact ral-binding GTPase activating protein, RLIP76, in artificial liposomes.

33%

Singhal S., Singhal J., Cheng J., Pikuła S., Sharma R., Zimniak P., Awasthi Y., Awasthi S.

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2001

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vol. 48

|

issue 2

551-562

EN

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.

15

ATP-sensitive K^+ channel in mitochondria

33%

Szewczyk A., Mikołajek B., Pikuła S., Nałęcz M.

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vol. 40

|

issue 3

329-336

Refine search results

Woda morska i dziury w błonach - Nagroda Nobla z chemii za rok 2003

Hipotetyczna rola autokatalitycznych właściwości kwasów nukleinowych w procesie biogenezy

Alzheimer's disease: Its origin at the membrane, evidence and questions.

10-Undecynoic acid, an inhibitor of cytochrome P450 4A1, inhibits ethanolamine-specific phospholipid base exchange reaction in rat liver microsomes

Is the glutathione conjugate of trans-4-hydroxy-2-nonenal transported by the multispecific organic anion transporting-ATPase of human erythrocytes?

The induction of cytochrome P450 isoform, CYP4A1, by clofibrate coincides with activation of ethanolamine-specific phospholipid base exchange reaction in rat liver microsomes

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

Circular dichroism and fluorescence studies on interaction of calmodulin (CaM) with purified (Ca^2+-Mg^2+) ATPase of erythrocyte ghosts

GTP-binding properties of the membrane-bound form of porcine liver annexin VI.

Adenosine 5'-triphosphate - a new regulator of annexin function. A hypothesis.

Annexins and ATP in membrane traffic: A comparison with membrane fusion machinery

Annexins- multifunctional, calcium-dependent, phospholipid-binding proteins

Annexin VI: An intracellular target for ATP

Purification and functional reconstitution of intact ral-binding GTPase activating protein, RLIP76, in artificial liposomes.

ATP-sensitive K^+ channel in mitochondria