The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Characterization of Ca2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins
Open accessAbstract
The annexins are a family of structurally similar, Ca2(+)-dependent, phospholipid-binding proteins. We compared six members of this family (calpactin I heavy chain, lipocortins I and III, endonexin II, p68 and protein II) to determine their phospholipid-binding specificities, as well as their ability to promote aggregation and fusion of phospholipid vesicles. The Ca2+ requirement for all of the proteins was lowest for binding to vesicles composed of phosphatidic acid, followed by phosphatidylserine and then phosphatidylinositol. Only protein II, p68, lipocortin III and endonexin II bound to vesicles composed of phosphatidylethanolamine, and none bound to phosphatidylcholine. Both calpactin I heavy chain and lipocortin I promoted aggregation of phosphatidylserine- or phosphatidylinositol-containing vesicles in the presence of less than 10 microM-Ca2+. Lipocortin I promoted fusion of liposome membranes by lowering threshold Ca2+ concentrations. Although calpactin I heavy chain did not affect threshold Ca2+ concentrations, it did increase the rate and extent of spontaneous fusion. In contrast, p68 inhibited fusion at threshold Ca2+ concentrations. Whereas previous reports have emphasized properties that the annexins have in common, these findings reveal quantitative and qualitative differences among the annexins which may relate to distinct intracellular functions.
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Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
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Calcium-dependent phospholipid- (and membrane-) binding proteins
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A simple method for the accurate determination of free [Ca] in Ca-EGTA solutions
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The Distribution and Function of Phosphatidylserine in Cellular Membranes
Leventis, P. A., & Grinstein, S. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131234 · Cited by 988
Annexin-Phospholipid Interactions. Functional Implications
Lizarbe, M., Barrasa, J., Olmo, N., Gavilanes, F., & Turnay, J. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14022652 · Cited by 234
Asbestos causes apoptosis in alveolar epithelial cells: Role of iron-induced free radicals
Aljandali, A., Pollack, H., Yeldandi, A., LI, Y., Weitzman, S. A., & Kamp, D. W. (2001) · Journal of Laboratory and Clinical Medicine · doi:10.1067/mlc.2001.114826 · Cited by 92
Annexin A2 Regulates β1 Integrin Internalization and Intestinal Epithelial Cell Migration
Rankin, C. R., Hilgarth, R. S., Leoni, G., Kwon, M., Den Beste, K. A., Parkos, C. A., & Nusrat, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.440909 · Cited by 55
Metadata
- Authors
- Blackwood, R. A., & Ernst, J. D.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1990-02-15
- Volume
- 266
- Issue
- 1
- Pages
- 195-200
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1714325720
- Cited by
- 290
- References
- 10
- FWCI
- 6.08
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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