‘New’ functions for ‘old’ proteins: The role of the calcium-binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice
Analysis of different brain regions suggests that these proteins are involved in regulating calcium pools critical for synaptic plasticity, and a major role of any of these three calcium-binding proteins as an endogenous neuroprotectant is not generally supported.
Parvalbumin Is a Mobile Presynaptic Ca2+ Buffer in the Calyx of Held that Accelerates the Decay of Ca2+ and Short-Term Facilitation
- Martin Müller, F. Felmy, B. Schwaller, R. Schneggenburger
- BiologyJournal of Neuroscience
- 28 February 2007
In young calyces of Held, a mobile Ca2+ buffer with slow binding kinetics, primarily represented by parvalbumin, accelerates the decay of spatially averaged [Ca2+]i and paired-pulse facilitation.
Cytosolic Ca2+ buffers.
- B. Schwaller
- BiologyCold Spring Harbor Perspectives in Biology
- 1 November 2010
"Ca(2+) buffers," a class of cytosolic Ca(2+)-binding proteins, act as modulators of short-lived intracellular Ca(2+) signals; they affect both the temporal and spatial aspects of these transient…
Cellular toxicity of carbon-based nanomaterials.
This work clearly indicated that carbon-based nanomaterials are toxic while the hazardous effect is size-dependent, and cytotoxicity is enhanced when the surface of the particles is functionalized after an acid treatment.
Role of the calcium-binding protein parvalbumin in short-term synaptic plasticity.
- O. Caillard, H. Moreno, B. Schwaller, I. Llano, M. Celio, A. Marty
- BiologyProceedings of the National Academy of Sciences…
- 21 November 2000
Paired-pulse stimulations at GABAergic synapses between interneurons and Purkinje cells show that parvalbumin potently modulates short-term synaptic plasticity.
Guidebook to the calcium-binding proteins
Kinetics of Ca2+ binding to parvalbumin in bovine chromaffin cells: implications for [Ca2+] transients of neuronal dendrites
It is concluded that Ca2+ buffers with slow kinetics, such as PV, may cause biexponential decays in [Ca2+] transients, thereby complicating the analysis of endogenous Ca2- binding ratios (κS) based on time constants.
Mutational analysis of dendritic Ca2+ kinetics in rodent Purkinje cells: role of parvalbumin and calbindin D28k
- H. Schmidt, K. M. Stiefel, P. Račay, B. Schwaller, J. Eilers
- BiologyJournal of Physiology
- 1 August 2003
Numerical simulations imply that the effect of uncharacterised endogenous Ca2+ binding proteins is negligible, that buffered diffusion and dye saturation significantly affects spineous Ca2- transients but not those in the dendritic shafts, and that neither CB nor PV undergoes saturation in spines or dendrites during climbing fibre‐evoked Ca 2+ transients.
Nanodomain Coupling between Ca2+ Channels and Ca2+ Sensors Promotes Fast and Efficient Transmitter Release at a Cortical GABAergic Synapse
Developmental Changes in Parvalbumin Regulate Presynaptic Ca2+ Signaling
It is shown that expression of the slow CBP parvalbumin (PV) in cerebellar interneurons is cell specific and developmentally regulated, leading to characteristic changes in presynaptic Ca2+ dynamics (Cai).