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1

Annexins and membrane organisation in the endocytic pathway

100%
Gerke V.
Cellular and Molecular Biology Letters
|
2001
|
tom 06
|
nr 2
2

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

100%
Bandorowicz J., Pikula S.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 3
3

Homing of annexin-labeled stem cells to apoptopic cells

75%
Gerasimou A., Ramella R., Brero A., Boero O., Sheiban I., Levi R., Gallo M. P.
Cellular and Molecular Biology Letters
|
2009
|
tom 14
|
nr 1
100-112
Ischemic diseases are characterized by the presence of pro-apoptotic stimuli, which initiate a cascade of processes that lead to cell injury and death. Several molecules and events represent detectable indicators of the different stages of apoptosis. Among these indicators is phosphatidylserine (PS) translocation from the inner to the outer leaflet of the plasma membrane, which can be detected by annexinV (ANXA5) conjugation. This is a widely used in vivo and in vitro assay marking the early stages of apoptosis. We report here on an original method that employs PS-ANXA5 conjugation to target stem cells to apoptotic cells. Mesenchymal stem cells (MSCs) from GFP-positive transgenic rats were biotinylated on membrane surfaces with sulfosuccinimidyl-6-(biotinamido) hexanoate (sulfo-NHS-LC-biot) and then bound to avidin. The avidin-biotinylated MSCs were labeled with biotin conjugated ANXA5. Bovine aortic endothelial cells (BAE-1 cells) were exposed to UVC to induce caspasedependent apoptosis. Finally, we tested the ability of ANXA5-labeled MSCs to bind BAE-1 apoptotic cells: suspended ANXA5-labeled MSCs were seeded for 1 hour on a monolayer of UV-treated or control BAE-1 cells. After washing, the number of MSCs bound to BAE-1 cells was evaluated by confocal microscopy. Statistical analysis demonstrated a significant increase in the number of MSCs tagged to apoptotic BAE-1 cells. Therefore, stem cell ANXA5 tagging via biotin-avidin bridges could be a straightforward method of improving homing to apoptotic tissues.
4

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

75%
Bandorowicz-Pikula J., Pikula S.
Acta Biochimica Polonica
|
1998
|
tom 45
|
nr 3
The paradigm of annexins as phospholipid-binding proteins interacting with membranes in a calcium-dependent manner has been recently questioned in light of observations that some annexin isoforms may behave like membrane integral proteins or remain associated with their target membranes at low, resting, concentrations of Ca2+ in the cytoplasm. In addition, an evidence has been presented that some annexins (annexins I, VI and VII) bind in vitro ATP and GTP, and upon binding the nucleotide the in vitro activity of these proteins is modified. However, annexins do not contain Walker A and B consensus sequences for ATP/GTP binding. This review presents the hypothesis that a new ATP-binding motif exists within the annexin molecules and that ATP may play a role of functional ligand for annexins also in vivo
5

Annexins as mediators in intracellular signalling pathways - are they intracellular GTP biosensors?

75%
Pikula S., Danieluk M., Golczak M., Kirilenko A., Bandorowicz-Pikula J.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr Suppl.
6

The roles of annexins and alkaline phosphatase in mineralization process

75%
Balcerzak M., Hamade E., Zhang L., Pikula S., Azzar G., Radisson J., Bandorowicz-Pikula J., Buchet R.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 4
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 (Pi), 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 under-stood, 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.
7

Annexins and membrane dynamics

75%
Gerke V.
Cellular and Molecular Biology Letters
|
1998
|
tom 03
|
nr 2
8

Monitoring of membrane phospholipid scrambling in human erythrocytes and K562 cells with FM1-43 - a comparison with annexin V-FITC

63%
Wrobel A., Bobrowska-Hagerstrand M., Lindqvist C., Hagerstrand H.
Cellular and Molecular Biology Letters
|
2014
|
tom 19
|
nr 2
The styryl dye FM1-43 becomes highly fluorescent upon binding to cell membranes. The breakdown of membrane phospholipid asymmetry in ionophore-stimulated T-lymphocytes further increases this fluorescence [Zweifach, 2000]. In this study, the capacity of FM1-43 to monitor membrane phospholipid scrambling was explored using flow cytometry in human erythrocytes and human erythrocyte progenitor K562 cells. The Ca2+-dependent phosphatidylserine-specific probe annexin V-FITC was used for comparison. The presented data show that the loss of phospholipid asymmetry that could be induced in human erythrocytes by elevated intracellular Ca2+ or by structurally different membrane intercalated amphiphilic compounds increases the FM1-43 fluorescence two- to fivefold. The profile of FM1-43 fluorescence for various treatments resembles that of phosphatidylserine exposure reported by annexin V-FITC. FM1-43 detected the onset of scrambling more efficiently than annexin V-FITC. The amphiphile-induced scrambling was shown to be a Ca2+-independent process. Monitoring of scrambling in K562 cells caused by NEM-induced Ca2+-release from intracellular stores and by Ca2+ and ionophore A23187 treatment showed that the increase in FM1-43 fluorescence correlated well with the number of annexin V-FITC-detected phosphatidylserine-positive cells. The results presented here show the usefulness of FM1-43 as a Ca2+-independent marker of dissipation in asymmetric membrane phospholipid distribution induced by various stimuli in both nucleated and non-nucleated cells.
9

Interactions of annexins IV and VI with erythrocyte membrane in the presence of Ca2. A biochemical and electron microscopy study

63%
Bandorowicz-Pikula J., Sobota A.
Cellular and Molecular Biology Letters
|
1996
|
tom 01
|
nr 1
Annexins IV and VI were found to interact with human erythrocyte membrane in a calcium-dependent manner. Chemical and enzymatic modification of the membrane constituents pointed to phosphatidylserine as a target membrane molecule responsible for the interaction of the annexin/Ca complexes with the membrane. The membrane-associated annexins were shown to form clusters reflecting, perhaps, the presence of PS microdomains in a lateral plane of membrane.
10

Effect of divalent metal ions on annexin-mediated aggregation of asolectin liposomes

51%
Mel'gunov V. I., Akimova E. I., Krasavchenko K. S.
Acta Biochimica Polonica
|
2000
|
tom 47
|
nr 3
Annexins belong to a family of Ca2+- and phospholipid-binding proteins that can mediate the aggregation of granules and vesicles in the presence of Ca2+. We have studied the effects of different divalent metal ions on annexin-mediated aggregation of liposomes using annexins isolated from rabbit liver and large unilamellar vesicles prepared from soybean asolectin II-S. In the course of these studies, we have found that annexin-mediated aggregation of liposomes can be driven by various earth and transition metal ions other than Ca2+. The ability of metal ions to induce annexin-mediated aggregation decreases in the order: Cd2+>Ba2+, Sr2+> Ca2+>>Mn2+>Ni2+>>Co2+. Annexin-mediated aggregation of vesicles is more selective to metal ions than the binding of annexins to membranes. We speculate that not every type of divalent metal ion can induce conformational change sufficient to promote the interaction of annexins either with two opposing membranes or with opposing protein molecules. Relative concentration ratios of metal ions in the intimate environment may be crucial for the functioning of annexins within specialized tissues and after treatment with toxic metal ions.
11

Calcium signaling in the brain

51%
Heizmann C. W.
Acta Neurobiologiae Experimentalis
|
1993
|
tom 53
|
nr 1
12

Smooth muscle actomyosin promotes Ca2plus - dependent interactions between annexin VI and detergent-insoluble glycosphingolipid-enriched membrane domains

51%
Babiychuk V. S., Draeger A., Babiychuk E. B.
Acta Biochimica Polonica
|
2000
|
tom 47
|
nr 3
The mechanical link coupling cytoskeletal and contractile proteins to the sarcolemma of smooth muscle cells is essential for transmitting tension from the cell's interior to exterior. In addition to the well-characterized actin-integrin associations present in adhaerens junctions, our recent work has postulated the existence of a reversible annexin-dependent membrane-cytoskeleton complex, forged in response to a rise in intracellular Ca2+ concentration following smooth muscle cell stimulation (Babiychuk et al., J. Biol Chem. 1999, 274, 35191-35195). Detailed biochemical characterization of the interactions responsible for the formation of this complex revealed that annexins II and VI interact with actomyosin, or detergent-insoluble glycosphingolipid-enriched membrane domains (rafts) purified from smooth muscle, in a concentration- and Ca2+-dependent manner. Annexin II interacted with lipid rafts with high Ca2+-sensitivity, while for annexin VI this interaction required non-physiologically high concentrations of free Ca2+. However, the Ca2+-sensitivity of the latter interaction strongly increased in the presence of purified smooth muscle actomyosin. The detailed biochemical analysis of the interactions occurring between annexin II, annexin VI, actomyosin and rafts suggests that annexins regulate sarcolemmal organization during smooth muscle cell contraction.
13

Bile flow, vesicular trafficking, and interactions of cytoskeleton with the canalicular domain of hepatocyte plasma membrane

51%
Pikula S., Bandorowicz-Pikula J.
Cellular and Molecular Biology Letters
|
1996
|
tom 01
|
nr 2
Liver is an epithelial organ which removes many substances from the blood, metabolizes them, and secretes back into circulation or directly into the bile. Liver parenchymal cells (hepatocytes) are involved in the overall detoxification of the organism through the bile. These highly polarized cells are unique among others due to the domain structure of their plasma membrane, organization of their cytoskeleton connected to the canalicular region of plasmalemma, and the specific distribution of various transport systems involved in detoxification phase III. In this mini-review the possible influence of canalicular motility modulated by cytoskeleton on the bile flow is discussed. In addition, the role of annexins, calcium- and phospholipid-binding proteins exhibiting high expression level in liver, in vesicular trafficking leading to the transport of some of biliary components is also postulated.
14

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

51%
Bandorowicz-Pikula J., Pikula S.
Acta Biochimica Polonica
|
1998
|
tom 45
|
nr 3
Annexins, calcium- and membrane-binding multifunctional proteins, have been implicated in N-ethylmaleimide (NEM)-independent fusion of vesicular structures involved in membrane traffic. This view is based on intracellular localization of annexins, which frequently associated with endosomes, chromaffin granules, caveolae, clathrin-coated pits, and other membrane compartments, engaged in endo- and exocytosis. Moreover, annexins were found to modulate budding and aggregation of vesicle membranes, to interact with cytoskeletal proteins, and, upon binding to membranes, to change the structure of lipid bilayer, leading to membrane fusion. In addition, some annexins are substrates for various protein kinases and, in membrane-bound form, reveal calcium channel activity. Recently, annexins were observed to interact in vitro and in vivo with nucleotides, ATP, GTP or cAMP, which are potent mediators of membrane traffic processes. In addition, annexin VII showed hydrolytic activity towards GTP, and similarities in the mechanism of action to that of small GTP-binding proteins were found. The aim of the present review is to summarize the observations implying annexins as possible effectors in endo- and exocytosis and to compare them with well known complexes of cytosolic and membrane proteins forming the true membrane fusion machinery within a cell, conserved from yeast to the neurons of humans.
15

Annexins - calcium- and membrane-binding proteins in the plant kingdom. Potential role in nodulation and mycorrhization in Medicago truncatula

45%
Talukdar T., Gorecka K. M., de Carvalho-Niebel F., Downie J. A., Cullimore J., Pikula S.
Acta Biochimica Polonica
|
2009
|
tom 56
|
nr 2
199-210
 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.
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