Binding-protein-dependent transport systems in Gram-negative bacteria are multicomponent systems in which a soluble periplasmic binding protein of high substrate binding affinity establishes the major substrate recognition site. Usually, there are two membrane proteins which are thought to interact
Frequency-dependent interaction of ultrashort E-fields with nociceptor membranes and proteins
✍ Scribed by Nan Jiang; Brian Y. Cooper
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 732 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0197-8462
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✦ Synopsis
We examined the influence of ultrashort pulses (USP) on sensory neurons. Single and high frequency bursts of 12 ns E-fields were presented to rat skin nociceptors that expressed distinct combinations of voltage-sensitive proteins. A single E-field pulse produced action potentials in all nociceptor subtypes at a critical threshold (E c ) of 403 V/cm. When configured into high frequency bursts, USP charge integrated to reduce the action potential threshold in a frequency and burst duration-dependent manner with E c as low as 16 V/cm (4000 Hz, 25 ms burst). There was no evidence of electroporation at field intensities near the E c for nociceptor activation. USP bursts activated a late, persistent Ca þþ flux that was identified as a dantrolene-sensitive Ca þþ -induced Ca þþ release (CICR). Influx of Ca þþ into the cell was required for the CICR and resulted in a reduction of the single pulse E c by about 50%.
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