High impact information on ANXA5

• There was evidence for apoptosis in azacytidine-treated cells, as demonstrated by nuclear condensation and fragmentation (days 27 and 35) using transmission electron microscopy, and the detection of exposed phosphatidylserine on the plasma membrane surface of apoptotic chondrocytes (day 27) using fluorescence-labelled annexin V [1].
• Annexin V staining without propidium iodide staining confirmed that these cells were apoptotic [2].
• Phosphatidylserine (PS) exposure was determined by flow cytometry by binding of FITC-labeled annexin V [3].
• In addition, fluorescent annexin-V staining identified externalized phosphatidylserine in neutrophils treated with tilmicosin, penicillin, ceftiofur, oxytetracycline, or dexamethasone [4].
• Phosphatidylserine (PS) externalization was detected by annexin-V labeling, nuclear morphology was studied by staining with Hoechst 33342 stain (Hoechst, Frankfurt, Germany), and the percentage of apoptotic cells was determined by the TdT-dUTP terminal nick-end labeling (TUNEL) assay [5].

Biological context of ANXA5

• Novel isoforms of CaBP 33/37 (annexin V) from mammalian brain: structural and phosphorylation differences that suggest distinct biological roles [6].
• The consensus sequence for high-affinity Ca(2+)-binding pockets obtained from the annexin V crystal structure is GXGT-38 residues-D/E [Huber, R., et al. (1992) J. Mol. Biol. 223, 683-704] [7].
• Phospholipid determinants for annexin V binding sites and the role of tryptophan 187 [8].
• The nucleotide sequence is 55 to 61% identical to that of the related membrane-binding proteins lipocortin, calpactin, endonexin II and (half of) 68kDa calelectrin [9].
• Cell viability was assessed by annexin-V FITC/propidium iodide staining [10].

Anatomical context of ANXA5

• Annexin V is part of a family of Ca(2+)-dependent phospholipid-binding proteins, whose purported functions are related to their interactions with biological membranes [8].
• Bull fertility was significantly related to the percentage of necrotic or viable sperm in fresh semen as detected by the Annexin V/PI assay, to the number of apoptotic sperm in fresh semen as detected by the TUNEL assay, and to the level of chromatin or DNA condensation as detected by PI staining [11].
• Granulosa and theca cell cultures in which killing occurred in response to FasL stained positively for annexin V, an early marker for cells undergoing apoptosis [12].
• Flow cytometric analysis initially detected annexin V on chondrocytes following isolation; the level of detection subsequently decreased by 24 hours, whereas that of alpha5 and beta1 integrins increased [13].
• The incidence of annexin-V-positive spermatozoa significantly correlated to the SCSA variable xalphat (r=0.53, P<0.05) [14].

Associations of ANXA5 with chemical compounds

• FRAP experiments were carried out with the probes C12-NBD-PC and C12-NBD-PS: at saturation, annexin V reduced the lateral diffusion rate of PC by 40% and nearly blocked the diffusion of PS [15].
• Binding of annexin V does not specifically require an ester carbonyl oxygen, as it occurs with ether-linked, amide-linked, and phosphonate-linked sn-2 hydrocarbon chains, under these conditions.(ABSTRACT TRUNCATED AT 250 WORDS)[8]
• Influence of annexin V on the structure and dynamics of phosphatidylcholine/phosphatidylserine bilayers: a fluorescence and NMR study [15].
• Annexin V, which binds but does not aggregate liposomes, can be assayed on the basis of inhibition of Ca(2+)-dependent liposome aggregation [16].
• In vitro, NF-kappaB activity and minimal incidence of apoptosis (<4%), as measured by Annexin V and TUNEL assays, were associated with production of estradiol [17].

Physical interactions of ANXA5

• Annexin VI contains twice as many putative calcium binding units as annexin V and the same pattern of behavior occurred for this pair of proteins [18].

Other interactions of ANXA5

• No apparent increase in annexin V expression on CD18-deficient neutrophils was found with OPZ stimulation [19].
• In both assays, treatment of cells with reagents that block CD44 (hyaluronan oligosaccharides or monoclonal Ab IM7) or annexin V (polyclonal Ab #8958) had no detectable effect on adhesion [20].
• Altogether, these findings suggest that, by an as yet unknown mechanism, following Ca(2+)-dependent association of annexin V isoforms and annexin VI with membranes, substantial fractions of these proteins remain bound to membranes in a Ca(2+)-independent way and behave like integral membrane proteins [21].
• A delay in apoptosis was demonstrated in CD18-deficient bovine neutrophils and this appeared to be closely associated with lowered signalling via [Ca2+]i, diminished annexin V expression on the cell surface, and decreased caspase 3 activity in lysates [19].

Analytical, diagnostic and therapeutic context of ANXA5

• Complete sequence analysis has revealed that these two proteins are isoforms of annexin V [6].
• We are investigating mutants of annexin V by single channel measurements, X-ray crystallography and electron microscopy in order to understand the structure-function relationships of the ion channel activity [22].
• Subsequently, peptide mapping, amino acid sequencing, and mass spectrometry analysis identified this protein as bovine annexin-V [23].
• The incidence of annexin-V-positive cells was negatively related (r=-0.59, P<0.01) to the percentage of viable cells, as detected by fluorometry [14].

References