A Calcium-Dependent Mechanism for Synapse and Nerve Cell Membrane Modulation

Hydén, Holger

doi:10.1073/pnas.71.8.2965

Cited by 33 publications

(4 citation statements)

References 14 publications

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“…Although considerable attention has recently been directed at the subsurface structure beneath the cytoplasmic membrane (Hyden, 1974;Metuzals, 1969;Metuzals and Izzard, 1969;Metuzals and Mushynski, 1974;Le Beux and Willemot, 1975), it is still too early to identify those submembrane structures related to the released proteins in this study. Recently, the fine structure of the pronasetreated squid axon membrane was examined by scanning electron microscopy (Metuzals and Tasaki, 1976).…”

Section: Discussionmentioning

confidence: 99%

Release of proteins from the inner surface of squid axon membrane labeled with tritiated N-ethylmaleimide.

Inoue¹,

Pant²,

Tasaki³

et al. 1976

The Journal of General Physiology

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Proteins in the inner surface of the squid axon membrane were labeled by intracellular perfusion of [aH]N-ethylmaleimide (NEM), which forms covalent bonds with free sulfhydryl groups. The excitability of the axon was unaffected by the [aH]NEM perfusion. After washout of the unbound label, the perfusate was monitored for the release of labeled proteins. Labeled proteins were released from the inner membrane surface by potassium depolarization of the axon only in the presence of external calcium ions. Replacement of the fluoride ion in the perfusion medium by various anions also caused labeled protein release. The order of effectiveness was SCN->> Br-> C1-> F-. The extent of labeled protein release by the various anions was correlated with their effects on axonal excitability. The significance of these results is discussed.

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Section: Discussionmentioning

confidence: 99%

Release of proteins from the inner surface of squid axon membrane labeled with tritiated N-ethylmaleimide.

Inoue¹,

Pant²,

Tasaki³

et al. 1976

The Journal of General Physiology

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“…The electrostatic and hydrophobic interactions between MBP and membrane lipids are the main reasons for the formation of the double-bilayer structure and the stability of the myelin sheath (16). The glial cell membrane (52, 53) is composed of a lipid bilayer and the proteins located thereon. MBP is located on the inner surface of the membrane (cytoplasmic surface) (43), making it positively charged and hydrophobic.…”

mentioning

confidence: 99%

Myelin sheath structure and regeneration in peripheral nerve injury repair

Liu

Wang

Tan

et al. 2019

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

107

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Observing the structure and regeneration of the myelin sheath in peripheral nerves following injury and during repair would help in understanding the pathogenesis and treatment of neurological diseases caused by an abnormal myelin sheath. In the present study, transmission electron microscopy, immunofluorescence staining, and transcriptome analyses were used to investigate the structure and regeneration of the myelin sheath after end-to-end anastomosis, autologous nerve transplantation, and nerve tube transplantation in a rat model of sciatic nerve injury, with normal optic nerve, oculomotor nerve, sciatic nerve, and Schwann cells used as controls. The results suggested that the double-bilayer was the structural unit that constituted the myelin sheath. The major feature during regeneration was the compaction of the myelin sheath, wherein the distance between the 2 layers of cell membrane in the double-bilayer became shorter and the adjacent double-bilayers tightly closed together and formed the major dense line. The expression level of myelin basic protein was positively correlated with the formation of the major dense line, and the compacted myelin sheath could not be formed without the anchoring of the lipophilin particles to the myelin sheath.

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“…These studies showed that the response depended on a narrow band of slow modulation frequencies (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) Hz), and not on the presence of the unmodulated carrier wave alone (147 MHz, 0.8 mW/cm2). In the present study, chick cerebral hemisphere and cat cerebral cortex were exposed, in vitro, to weak (5-100 V/m) extremely low frequency (ELF) fields .…”

mentioning

confidence: 99%

Sensitivity of calcium binding in cerebral tissue to weak environmental electric fields oscillating at low frequency.

Bawin¹,

Adey²

1976

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

386

143

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Weak sinusoidal electric fields modify the calcium efflux from freshly isolated chick and cat cerebral tissues bathed in Ringer's solution, at 360. Following incubation (30 min) with radioactive calcium (45Ca2+), each sample, immersed in fresh solution, was exposed for 20 min to fields at 1, 6, 16, 32, or We have previously described a sharply increased efflux of calcium from isolated chick brain tissues exposed to modulated radio frequency fields (16). These studies showed that the response depended on a narrow band of slow modulation frequencies (6-25 Hz), and not on the presence of the unmodulated carrier wave alone (147 MHz, 0.8 mW/cm2). In the present study, chick cerebral hemisphere and cat cerebral cortex were exposed, in vitro, to weak (5-100 V/m) extremely low frequency (ELF) fields (1-75 Hz). MATERIALS AND METHODSField exposure was performed in an environmental screened chamber, between two parallel metal plates, one square meter in area, 50 cm apart. Sine wave electric fields were applied to the plates at levels of 5-100 V/m and at frequencies of 1-75 Hz. Equal voltages with respect to ground were applied to each plate.Chick cerebral hemispheres were rapidly removed following decapitation. The hemispheres were separated and after weighing each was incubated at 36' for 30 min in 1 ml of a physiological medium [155 mM NaCl, 5.6 mM KCI, 2.16 mM CaCl2, 24 mM NaHCO3, and D-glucose (2 g/liter)] together with 0.2 ml of a solution containing 45Ca2+ (0.2 1ACi, specific activity 1.39 Ci/mmol). The incubated samples were then rinsed three times and exposed for 20 min to an environmental electric field while immersed in 1.0 ml of the physiological medium. At the conclusion of field exposure, an aliquot of 0.2 ml of the bathing solution was taken for scintillation counting. Prior to counting this aliquot was mixed with 9.0 ml of a scintillation adjuvant (Packard Dimilume). The brain samples were dissolved overnight in a digestive medium (Soluene 350, Packard) and then assayed for radioactivity. For each field condition (in both frequency and amplitude) "sets" of 10 brain samples were used simultaneously in field exposure and control conditions. Control samples were tested identically to the test samples except for the field exposure. All tissues were maintained at 36' during the whole experiment (16).The same experimental procedure was applied to striated muscles (lateral head of the gastrocnemius) in a series of chicks to evaluate possible effects in nonnervous tissue. Fifty muscle specimens were tested with 20 V/mi, 16 Hz field and compared with nonexposed muscles (30 samples). The statistical treatment of the data was identical to that applied to brain tissues.Samples of freshly removed cat cortex were similarly tested. Under ether anesthesia, the cerebral hemispheres were exposed. After completion of surgery, general anesthesia was discontinued and local anesthesia was instituted in all incisions and pressure points and thereafter the animal was immobilized with gallamine triethiodide (6.0 mg, intra...

show abstract

A Calcium-Dependent Mechanism for Synapse and Nerve Cell Membrane Modulation

Cited by 33 publications

References 14 publications

Release of proteins from the inner surface of squid axon membrane labeled with tritiated N-ethylmaleimide.

Release of proteins from the inner surface of squid axon membrane labeled with tritiated N-ethylmaleimide.

Myelin sheath structure and regeneration in peripheral nerve injury repair

Sensitivity of calcium binding in cerebral tissue to weak environmental electric fields oscillating at low frequency.

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