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1

Lipid-binding proteins as stabilizers of membrane microdomains - possible physiological significance.

100%

Bandorowicz-Pikuła J.

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2000

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vol. 47

|

issue 3

553-564

EN

Below the melting point temperature of lipids, artificial lipid membranes usually exist in the ordered gel phase. Above these temperatures lipid acyl chains become fluid and disordered (liquid-crystalline phase). Depending on the chemical composition of artificial membranes, phase separation may occur, leading to the formation of transient or stable membrane domains. A similar phase separation of lipids into ordered and disordered domains has been observed in natural membranes at physiological temperature range. Moreover, it has been reported that certain proteins prefer certain organization of lipids, as for example glycosylphosphatidylinositol-anchored proteins or Src family of tyrosine kinases. The aim of present review is to discuss the possibility that some lipid microdomains are induced or stabilized by lipid-binding proteins that under certain conditions, for example due to a rise of cytosolic Ca2+ or pH changes, may attach to the membrane surface, inducing clustering of lipid molecules and creation of ordered lipid microdomains. These domains may than attract other cytosolic proteins, either enzymes or regulatory proteins. It is, therefore, postulated that lipid microdomains play important roles within a cell, in signal transduction and enzymatic catalysis, and also in various pathological states, as Alzheimer's disease, anti-phosphatidylserine syndrome, or development of multidrug resistance of cancer cells.

2

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

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1999

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vol. 46

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issue 2

419-429

3

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

51%

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

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2001

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vol. 48

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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.

4

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

51%

Bandorowicz-Pikuła J., Pikuła S.

Acta Biochimica Polonica

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1998

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vol. 45

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issue 3

735-744

5

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

51%

Bandorowicz-Pikuła J., Pikuła S.

Acta Biochimica Polonica

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1998

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vol. 45

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issue 3

721-733

6

Annexin VI: An intracellular target for ATP

39%

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

Acta Biochimica Polonica

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1999

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vol. 46

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issue 3

801-812

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Lipid-binding proteins as stabilizers of membrane microdomains - possible physiological significance.

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

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

Annexin VI: An intracellular target for ATP