dorsal/arxiv
View SchemaA theory of Plasma Membrane Calcium Pump stimulation and activity
| Authors | Michael Graupner, Frido Erler, Michael Meyer-Hermann |
|---|---|
| Categories | |
| ArXiv ID | physics/0306121 |
| URL | https://arxiv.org/abs/physics/0306121 |
| DOI | 10.1007/s10867-005-4472-2 |
| Journal | Michael Graupner, Frido Erler, Michael Meyer-Hermann, A Theory of Plasma Membrane Calcium Pump Stimulation and Activity, Journal of Biological Physics, Volume 31, Issue 2, May 2005, Pages 183 - 206 |
Abstract
The ATP-driven Plasma Membrane Calcium pump or Ca(2+)-ATPase (PMCA) is characterized by a high affinity to calcium and a low transport rate compared to other transmembrane calcium transport proteins. It plays a crucial role for calcium extrusion from cells. Calmodulin is an intracellular calcium buffering protein which is capable in its Ca(2+) liganded form of stimulating the PMCA by increasing both the affinity to calcium and the maximum calcium transport rate. We introduce a new model of this stimulation process and derive analytical expressions for experimental observables in order to determine the model parameters on the basis of specific experiments. We furthermore develop a model for the pumping activity. The pumping description resolves the seeming contradiction of the Ca(2+):ATP stoichiometry of 1:1 during a translocation step and the observation that the pump binds two calcium ions at the intracellular site. The combination of the calcium pumping and the stimulation model correctly describes PMCA function. We find that the processes of calmodulin-calcium complex attachment to the pump and of stimulation have to be separated. Other PMCA properties are discussed in the framework of the model. The presented model can serve as a tool for calcium dynamics simulations and provides the possibility to characterize different pump isoforms by different type-specific parameter sets.
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"abstract": "The ATP-driven Plasma Membrane Calcium pump or Ca(2+)-ATPase (PMCA) is\ncharacterized by a high affinity to calcium and a low transport rate compared\nto other transmembrane calcium transport proteins. It plays a crucial role for\ncalcium extrusion from cells. Calmodulin is an intracellular calcium buffering\nprotein which is capable in its Ca(2+) liganded form of stimulating the PMCA by\nincreasing both the affinity to calcium and the maximum calcium transport rate.\nWe introduce a new model of this stimulation process and derive analytical\nexpressions for experimental observables in order to determine the model\nparameters on the basis of specific experiments. We furthermore develop a model\nfor the pumping activity. The pumping description resolves the seeming\ncontradiction of the Ca(2+):ATP stoichiometry of 1:1 during a translocation\nstep and the observation that the pump binds two calcium ions at the\nintracellular site. The combination of the calcium pumping and the stimulation\nmodel correctly describes PMCA function. We find that the processes of\ncalmodulin-calcium complex attachment to the pump and of stimulation have to be\nseparated. Other PMCA properties are discussed in the framework of the model.\nThe presented model can serve as a tool for calcium dynamics simulations and\nprovides the possibility to characterize different pump isoforms by different\ntype-specific parameter sets.",
"arxiv_id": "physics/0306121",
"authors": [
"Michael Graupner",
"Frido Erler",
"Michael Meyer-Hermann"
],
"categories": [
"physics.bio-ph",
"q-bio.BM"
],
"doi": "10.1007/s10867-005-4472-2",
"journal_ref": "Michael Graupner, Frido Erler, Michael Meyer-Hermann, A Theory of\n Plasma Membrane Calcium Pump Stimulation and Activity, Journal of Biological\n Physics, Volume 31, Issue 2, May 2005, Pages 183 - 206",
"title": "A theory of Plasma Membrane Calcium Pump stimulation and activity",
"url": "https://arxiv.org/abs/physics/0306121"
},
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