Calcium buffering properties of calbindin D28k and parvalbumin in rat sensory neurones.

P. S. Chard*, D. Bleakman, S. Christakos, C. S. Fullmer, R. J. Miller

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

298 Scopus citations

Abstract

1. We have examined the ability of the Ca(2+)‐binding proteins (CABP) calbindin D28k and paravalbumin to modulate increases in the intracellular free Ca2+ concentration ([Ca2+]i), produced by brief depolarizations, in rat dorsal root ganglion (DRG) neurones. 2. In order to obtain good voltage control, we replated DRG neurones prior to performing these experiments. Immunocytochemical staining of these cells revealed that approximately 10% stained for CABPs. 3. Using fluorescently labelled parvalbumin, we demonstrated that in the whole‐cell voltage clamp mode the protein freely entered the cell soma with a mean half‐life t0.5 of 6 min 22 s +/‐ 54 s. 4. Analysis of the effects of calbindin D28k (370 microM) and parvalbumin (1 mM) on Ca2+ currents in the whole‐cell voltage clamp mode, revealed that neither protein changed the rate of inactivation of the Ca2+ current or its rate of run‐down. 5. Introducing either calbindin D28k (370 microM) or parvalbumin (1 mM) into the cell soma did not significantly alter the basal [Ca2+]i when compared to control cells. 6. Compared to control cells, both CABPs significantly reduced the peak [Ca2+]i obtained for a Ca2+ influx of an equivalent charge density, whereas lysozyme (1 mM), a protein with low affinity for Ca2+, failed to do so. 7. Calbindin D28k caused an 8‐fold decrease in the rate of rise in [Ca2+]i and altered the kinetics of decay of [Ca2+]i to a single slow component. Parvalbumin also slowed the rate of rise in [Ca2+]i. Parvalbumin selectively increased a fast component in the decay of the Ca2+ signal. 8. These data demonstrate that both calbindin D28k and paravalbumin effectively buffer Ca2+ in a cellular environment and may therefore regulate Ca(2+)‐dependent aspects of neuronal function.

Original languageEnglish (US)
Pages (from-to)341-357
Number of pages17
JournalThe Journal of Physiology
Volume472
Issue number1
DOIs
StatePublished - Dec 1 1993

ASJC Scopus subject areas

  • Physiology

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