ArticleBiophysical journal2013
Membrane modulates affinity for calcium ion to create an apparent cooperative binding response by annexin a5.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Annexin A5 knockdown inhibits cardiomyocyte apoptosis and alleviates cardiac hypertrophy via activating the PI3K/AKT/Bcl-2 signaling pathway.Scientific reports · 2024Article
- Primary and Secondary Binding of Exenatide to Liposomes.Biophysical journal · 2020Article
- Annexin-V stabilizes membrane defects by inducing lipid phase transition.Nature communications · 2020Article
- Proteomic analysis of the response of porcine adrenal gland to heat stress.Research in veterinary science · 2019Article
- High-speed AFM height spectroscopy reveals µs-dynamics of unlabeled biomolecules.Nature communications · 2018Article
- Domain IV of Annexin A5 Is Critical for Binding Calcium and Guarantees Its Maximum Binding to the Phosphatidylserine Membrane.Molecules (Basel, Switzerland) · 2017Article
- An enhanced bioluminescence-based Annexin V probe for apoptosis detection in vitro and in vivo.Cell death & disease · 2017Article
- High-speed atomic force microscopy shows that annexin V stabilizes membranes on the second timescale.Nature nanotechnology · 2016Article
- Quantitative analysis of annexin V-membrane interaction by flow cytometry.European biophysics journal : EBJ · 2015Article
- Randomly organized lipids and marginally stable proteins: a coupling of weak interactions to optimize membrane signaling.Biochimica et biophysica acta · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Isothermal titration calorimetry was used to characterize the binding of calcium ion (Ca²⁺) and phospholipid to the peripheral membrane-binding protein annexin a5. The phospholipid was a binary mixture of a neutral and an acidic phospholipid, specifically phosphatidylcholine and phosphatidylserine in the form of large unilamellar vesicles. To stringently define the mode of binding, a global fit of data collected in the presence and absence of membrane concentrations exceeding protein saturation was performed. A partition function defined the contribution of all heat-evolving or heat-absorbing binding states. We find that annexin a5 binds Ca²⁺ in solution according to a simple independent-site model (solution-state affinity). In the presence of phosphatidylserine-containing liposomes, binding of Ca²⁺ differentiates into two classes of sites, both of which have higher affinity compared with the solution-state affinity. As in the solution-state scenario, the sites within each class were described with an independent-site model. Transitioning from a solution state with lower Ca²⁺ affinity to a membrane-associated, higher Ca²⁺ affinity state, results in cooperative binding. We discuss how weak membrane association of annexin a5 prior to Ca²⁺ influx is the basis for the cooperative response of annexin a5 toward Ca²⁺, and the role of membrane organization in this response.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.