| First Author | Müller M | Year | 2007 |
| Journal | J Neurosci | Volume | 27 |
| Issue | 9 | Pages | 2261-71 |
| PubMed ID | 17329423 | Mgi Jnum | J:119800 |
| Mgi Id | MGI:3703282 | Doi | 10.1523/JNEUROSCI.5582-06.2007 |
| Citation | Muller M, et al. (2007) Parvalbumin is a mobile presynaptic Ca2+ buffer in the calyx of held that accelerates the decay of Ca2+ and short-term facilitation. J Neurosci 27(9):2261-71 |
| abstractText | Presynaptic Ca2+ signaling plays a crucial role in short-term plasticity of synaptic transmission. Here, we studied the role of mobile endogenous presynaptic Ca2+ buffer(s) in modulating paired-pulse facilitation at a large excitatory nerve terminal in the auditory brainstem, the calyx of Held. To do so, we assessed the effect of presynaptic whole-cell recording, which should lead to the diffusional loss of endogenous mobile Ca2+ buffers, on paired-pulse facilitation and on intracellular Ca2+ concentration ([Ca2+]i) transients evoked by action potentials. In unperturbed calyces briefly preloaded with the Ca2+ indicator fura-6F, the [Ca2+]i transient decayed surprisingly fast (tau(fast), approximately 30 ms). Presynaptic whole-cell recordings made without additional Ca2+ buffers slowed the decay kinetics of [Ca2+]i and paired-pulse facilitation (twofold to threefold), but the amplitude of the [Ca2+]i transient was changed only marginally. The fast [Ca2+]i decay was restored by adding the slow Ca2+ buffer EGTA (50-100 microM) or parvalbumin (100 microM), a Ca2+-binding protein with slow Ca2+-binding kinetics, to the presynaptic pipette solution. In contrast, the fast Ca2+ buffer fura-2 strongly reduced the amplitude of the [Ca2+]i transient and slowed its decay, suggesting that the mobile endogenous buffer in calyces of Held has slow, rather than fast, binding kinetics. In parvalbumin knock-out mice, the decay of [Ca2+]i and facilitation was slowed approximately twofold compared with wild-type mice, similar to what is observed during whole-cell recordings in rat calyces of Held. Thus, 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. |
