Physiological Roles of the Sodium‐Calcium Exchanger in Nerve and Muscle<sup><i>a</i></sup>

Blaustein, Mordecai P.; Goldman, W. F.; Fontana, Giovanni; Krueger, Bruce K.; Santiago, Eligio M.; Steele, T.; Weiss, Daniel; Yarowsky, Paul

doi:10.1111/j.1749-6632.1991.tb17315.x

Cited by 122 publications

(38 citation statements)

References 44 publications

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“…In barnacle muscle fibers a membrane depolarization seems to favor Ca 2ϩ influx by means of reverse Na ϩ ͞Ca 2ϩ exchange (33). Elevated [Na ϩ ] o inhibits reverse Na ϩ ͞ Ca 2ϩ exchange in squid axons and some mammalian tissues (26,34,35), observations consistent with what was observed in herring sperm.…”

Section: Discussionsupporting

confidence: 78%

Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange

Vines

Yoshida

Griffin

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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Sperm of the Pacific herring, Clupea pallasi, are unique in that they are immotile upon spawning in the environment. Herring sperm have evolved to remain motionless for up to several days after spawning, yet are still capable of fertilizing eggs. An egg chorion ligand termed ''sperm motility initiation factor'' (SMIF) induces motility in herring sperm and is required for fertilization. In this study, we show that SMIF induces calcium influx, sodium efflux, and a membrane depolarization in herring sperm. Sperm motility initiation by SMIF depended on decreased extracellular sodium (<350 mM) and could be induced in the absence of SMIF in very low sodium seawater. Motility initiation depended on > 1 mM extracellular calcium. Calcium influx caused by SMIF involved both the opening of voltage-gated calcium channels and reverse sodiumcalcium (Na ؉ ͞Ca 2؉ ) exchange. Membrane depolarization was slightly inhibited by a calcium channel blocker and markedly inhibited by a Na ؉ ͞Ca 2؉ exchange inhibitor. Sodium efflux caused by SMIF-initiated motility was observed when using both extracellular and intracellular sodium probes. A Na ؉ ͞Ca 2؉ exchange antigen was shown to be present on the surface of the sperm, primarily over the midpiece, by using an antibody to the canine Na ؉ ͞Ca 2؉ exchanger. This antibody recognized a 120-kDa protein that comigrated with the canine myocyte Na ؉ ͞Ca 2؉ exchanger. Sperm of Pacific herring are now shown to use reverse Na ؉ ͞Ca 2؉ exchange in motility initiation. This mechanism of regulation of motility initiation may have evolved for both maintenance of immotility after spawning as well as ligand-induced motility initiation.T eleost fish sperm are quiescent within the testes and seminal plasma before spawning, but most initiate motility after dilution into the external medium (freshwater or seawater for most species) in which spawning occurs (1). In salmonids, motility initiation occurs with dilution in freshwater, specifically from a reduction in extracellular potassium that drives a membrane hyperpolarization and an increase in intracellular calcium ([Ca 2ϩ ] i ) (2-6). Changes in the concentrations of specific ions (Ca 2ϩ , K ϩ , and possibly Na ϩ and Cl Ϫ ) also have been linked to motility initiation in Atlantic croaker sperm (7). A hyperpolarization of the sperm membrane also has been documented in carp sperm, reportedly linked to the opening of voltage-gated Ca 2ϩ channels and an increase in [Ca 2ϩ ] i (8). In other freshwater teleost sperm (goldfish, zebra fish), as well as in marine teleost sperm (puffer, flounder), motility is believed to occur as a result of nonspecific hypo-or hyperosmotic changes that drive changes in intracellular ion concentrations (5, 9, 10). Thus, in all systems studied to date, a membrane hyperpolarization leads to an increase in [Ca 2ϩ ] i and the initiation of motility.Although the stimulation of sperm motility in the vicinity of eggs has been reported in some teleost fish, only herring sperm have been shown to require an egg chorion-derived ligand for ...

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Section: Discussionsupporting

confidence: 78%

Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange

Vines

Yoshida

Griffin

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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“…In general, PMCAs have ϳ10-fold higher affinity for Ca 2ϩ than NCXs and therefore regulate baseline [Ca 2ϩ ] i and [Ca 2ϩ ] i kinetics during transient depolarizations (Blaustein et al, 1991;Wanaverbecq et al, 2003). The PMCA family consists of four isoforms, which are expressed in a cell type-and tissue-specific manner throughout the brain (Stahl et al, 1992;Stauffer et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Scotopic Visual Signaling in the Mouse Retina Is Modulated by High-Affinity Plasma Membrane Calcium Extrusion

et al. 2006

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Transmission of visual signals at the first retinal synapse is associated with changes in calcium concentration in photoreceptors and bipolar cells. We investigated how loss of plasma membrane Ca 2ϩ ATPase isoform 2 (PMCA2), the calcium transporter isoform with the highest affinity for Ca 2ϩ /calmodulin, affects transmission of rod-and cone-mediated responses. PMCA2 expression in the neuroblast layer was observed soon after birth; in the adult, PMCA2 was expressed in inner segments and synaptic terminals of rod photoreceptors, in rod bipolar cells, and in most inner retinal neurons but was absent from cones. To determine the role of PMCA2 in retinal signaling, we compared morphology and light responses of retinas from control mice and deafwaddler dfw 2J mice, which lack functional PMCA2 protein. The cytoarchitecture of retinas from control and dfw 2J mice was indistinguishable at the light microscope level. Suction electrode recordings revealed no difference in the sensitivity or amplitude of outer segment light responses of control and dfw 2J rods. However, rod-mediated ERG b-wave responses in dfw 2J mice were ϳ45% smaller and significantly slower than those of control mice. Furthermore, recordings from individual rod bipolar cells showed that the sensitivity of transmission at the rod output synapse was reduced by ϳ50%. No changes in the amplitude or timing of cone-mediated ERG responses were observed. These results suggest that PMCA2-mediated Ca 2ϩ extrusion modulates the amplitude and timing of the high-sensitivity rod pathway to a much greater extent than that of the cone pathway.

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“…When the ␤-cell is exposed to glucose, a complex series of events is initiated that culminate in a rise in cytosolic free Ca 2ϩ concentration ([Ca 2ϩ ] i ), which triggers the exocytosis of insulin (1)(2)(3)(4). Like most other cells, the ␤-cell is equipped with a double system responsible for Ca 2ϩ extrusion: a plasma membrane Ca 2ϩ -ATPase and a Na/Ca exchange transport system (5,6). The Na/Ca exchanger is an electrogenic transporter located at the plasma membrane that couples the exchange of Na ϩ and Ca 2ϩ with a stoichiometry of three Na ϩ for one Ca 2ϩ (7).…”

mentioning

confidence: 99%

Overexpression of the Na/Ca Exchanger Shapes Stimulus-Induced Cytosolic Ca2+ Oscillations in Insulin-Producing BRIN-BD11 Cells

Eylen¹,

Horta²,

Barez³

et al. 2002

Diabetes

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Physiological Roles of the Sodium‐Calcium Exchanger in Nerve and Muscle^a

Cited by 122 publications

References 44 publications

Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange

Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange

Scotopic Visual Signaling in the Mouse Retina Is Modulated by High-Affinity Plasma Membrane Calcium Extrusion

Overexpression of the Na/Ca Exchanger Shapes Stimulus-Induced Cytosolic Ca2+ Oscillations in Insulin-Producing BRIN-BD11 Cells

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Physiological Roles of the Sodium‐Calcium Exchanger in Nerve and Musclea

Cited by 122 publications

References 44 publications

Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange

Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange

Scotopic Visual Signaling in the Mouse Retina Is Modulated by High-Affinity Plasma Membrane Calcium Extrusion

Overexpression of the Na/Ca Exchanger Shapes Stimulus-Induced Cytosolic Ca2+ Oscillations in Insulin-Producing BRIN-BD11 Cells

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Physiological Roles of the Sodium‐Calcium Exchanger in Nerve and Muscle^a