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Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel

Author

Listed:
  • Yuriy Kirichok

    (Harvard Medical School Enders 1309)

  • Betsy Navarro

    (Harvard Medical School Enders 1309)

  • David E. Clapham

    (Harvard Medical School Enders 1309)

Abstract

Sperm ion flux pinned down Ion channels have an important role in the key physiological functions of mammalian sperm, but despite attempts over the past 20 years to record ion currents from sperm directly, no success had been achieved. Now a simple, reproducible patch-clamp method of recording sperm cell ion currents has been developed, and it reveals that the principal alkaline-activated Ca2+-selective channel in mouse spermatozoa is an alkaline-activated channel in the flagellum, containing the sperm-specific protein CatSper1.

Suggested Citation

  • Yuriy Kirichok & Betsy Navarro & David E. Clapham, 2006. "Whole-cell patch-clamp measurements of spermatozoa reveal an alkaline-activated Ca2+ channel," Nature, Nature, vol. 439(7077), pages 737-740, February.
    • Handle: RePEc:nat:nature:v:439:y:2006:i:7077:d:10.1038_nature04417
    DOI: 10.1038/nature04417
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    Cited by:

    1. Julio C Chávez & José L de la Vega-Beltrán & Jessica Escoffier & Pablo E Visconti & Claudia L Treviño & Alberto Darszon & Lawrence Salkoff & Celia M Santi, 2013. "Ion Permeabilities in Mouse Sperm Reveal an External Trigger for SLO3-Dependent Hyperpolarization," PLOS ONE, Public Library of Science, vol. 8(4), pages 1-13, April.
    2. Lifeng Tian & Hao Zhang & Shilong Yang & Anna Luo & Peter Muiruri Kamau & Jingmei Hu & Lei Luo & Ren Lai, 2023. "Vertebrate OTOP1 is also an alkali-activated channel," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    3. Takafumi Kawai & Shin Morioka & Haruhiko Miyata & Rizki Tsari Andriani & Sharmin Akter & Gabriel Toma & Tatsuya Nakagawa & Yuki Oyama & Rie Iida-Norita & Junko Sasaki & Masahiko Watanabe & Kenji Sakim, 2024. "The significance of electrical signals in maturing spermatozoa for phosphoinositide regulation through voltage-sensing phosphatase," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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