Disease relevance of ANXA6

• To further delineate the molecular mechanisms underlying kinase regulation, we attempted to express the P68 protein kinase in insect cells using a baculovirus vector [1].

High impact information on ANXA6

• These results suggest that annexin VI can dissociate and redistribute calspectin in a Ca2+/phospholipid-dependent manner under the plasma membrane and that annexin VI may be involved in the regulation of the membrane skeleton of neuronal cells in response to Ca2+ [2].
• Annexin VI bound to about 14 species of proteins in the whole homogenate of rat forebrain, when examined with 125I-annexin VI using blots of SDS-polyacrylamide gels [2].
• Cosedimentation assay showed that annexin VI dissociates calspectin from F-actin in the presence of Ca2+ and PS [2].
• Kinetics of annexin VI, calcium, and phospholipid association and dissociation [3].
• 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 [4].

Biological context of ANXA6

• Chromaffin granules release calcium on contact with annexin VI: implications for exocytosis [5].
• Phosphorylation of synapsin I by cyclic AMP-dependent protein kinase and by Ca2+/calmodulin-dependent protein kinase II inhibited the annexin VI binding [6].
• Finally, we determined that the P68 amino terminus was both necessary and sufficient for binding dsRNA as we were able to transfer dsRNA-binding properties to a reporter gene product previously unable to bind RNA [1].
• Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: identification as a homologue for annexin VI and intracellular localization [7].
• The amount (IC50) of CPB-II causing the inhibition at 50% was estimated to be approximately 10 nM [8].

Anatomical context of ANXA6

• Under neurofilament assembly conditions, only the P70 polypeptide was able to reassemble into an intermediate filament in the absence of the other two polypeptides [9].
• When the subcellular fractions of rat forebrain were examined with a blot from a sodium dodecyl sulfate-polyacrylamide gel, each annexin VI-binding protein showed a different distribution, suggesting that annexin VI is a multifunctional protein [6].
• Characterization and ultrastructural localization of annexin VI from mitochondria [10].
• Annexin VI, a member of a family of related intracellular proteins that associate reversibly with membrane phospholipids in a Ca(2+)-dependent manner, has been purified from bovine liver mitochondria and characterized [10].
• 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 [11].

Associations of ANXA6 with chemical compounds

• The P70 and P150 polypeptides obtained after the DEAE column were separable on a hydroxylapatite column [9].
• The A-VI-induced release of 45Ca2+ was rapid, being essentially complete by our first time point of 7 s, and corresponded to 40% of the total sequestered 45Ca2+ [5].
• Annexin VI bound to > 14 species of proteins in the whole homogenate of rat forebrain in a Ca2+/phosphatidylserine- or phosphatidic acid-dependent manner [6].
• The P68 protein kinase (referred to as P68 based on its M(r) of 68,000 in human cells) is a serine/threonine kinase induced by interferon treatment and activated by dsRNAs [1].

Analytical, diagnostic and therapeutic context of ANXA6

• We then purified the kinase by immunoaffinity chromatography to raise monospecific antiserum which recognized not only the human native wild-type P68, but also kinase homologues in murine, bovine, and monkey cells as determined by immunoblot and immunoprecipitation analysis [1].
• Analysis by two-dimensional SDS PAGE and fluorography revealed that heat shock protein 68 (HSP68) and two other putative heat shock proteins, P71 and P70, were synthesized by all oocytes regardless of treatment [12].
• Antisera to 68,000 (P68), 150,000 (P150) and 200,000 (P200) dalton neurofilament proteins showed greatest activity with the corresponding protein immunogen but also revealed cross-reactivity with the other two neurofilament proteins when assessed by the ELISA method [13].

References