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Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm.

Publication ,  Journal Article
Tash, JS; Krinks, M; Patel, J; Means, RL; Klee, CB; Means, AR
Published in: J Cell Biol
May 1988

Preliminary data demonstrated that the inhibition of reactivated sperm motility by calcium was correlated with inhibited protein phosphorylation. The inhibition of phosphorylation by Ca2+ was found to be catalyzed by the calmodulin-dependent protein phosphatase (calcineurin). Sperm from dog, pig, and sea urchin contain both the Ca2+-binding B subunit of the enzyme (Mr 15,000) and the calmodulin-binding A subunit with an Mr of 63,000. The sperm A subunit is slightly higher in Mr than reported for other tissues. Inhibition of endogenous calmodulin-dependent protein phosphatase activity with a monospecific antibody revealed the presence of 14 phosphoprotein substrates in sperm for this enzyme. The enzyme was localized to both the flagellum and the postacrosomal region of the sperm head. The flagellar phosphatase activity was quantitatively extracted with 0.6 M KCl from isolated flagella from dog, pig, and sea urchin sperm. All salt-extractable phosphatase activity was inhibited with antibodies against the authentic enzyme. Preincubation of sperm models with the purified phosphatase stimulated curvolinear velocity and lateral head amplitude (important components of hyperactivated swimming patterns) and inhibited beat cross frequency suggesting a role for this enzyme in axonemal function. Our results suggest that calmodulin-dependent protein phosphatase plays a major role in the calcium-dependent regulation of flagellar motility.

Duke Scholars

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

May 1988

Volume

106

Issue

5

Start / End Page

1625 / 1633

Location

United States

Related Subject Headings

  • Swine
  • Spermatozoa
  • Sperm Motility
  • Sea Urchins
  • Phosphorylation
  • Phosphoprotein Phosphatases
  • Male
  • Immunoassay
  • Fluorescent Antibody Technique
  • Flagella
 

Citation

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Tash, J. S., Krinks, M., Patel, J., Means, R. L., Klee, C. B., & Means, A. R. (1988). Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J Cell Biol, 106(5), 1625–1633. https://doi.org/10.1083/jcb.106.5.1625
Tash, J. S., M. Krinks, J. Patel, R. L. Means, C. B. Klee, and A. R. Means. “Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm.J Cell Biol 106, no. 5 (May 1988): 1625–33. https://doi.org/10.1083/jcb.106.5.1625.
Tash JS, Krinks M, Patel J, Means RL, Klee CB, Means AR. Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J Cell Biol. 1988 May;106(5):1625–33.
Tash, J. S., et al. “Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm.J Cell Biol, vol. 106, no. 5, May 1988, pp. 1625–33. Pubmed, doi:10.1083/jcb.106.5.1625.
Tash JS, Krinks M, Patel J, Means RL, Klee CB, Means AR. Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J Cell Biol. 1988 May;106(5):1625–1633.

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

May 1988

Volume

106

Issue

5

Start / End Page

1625 / 1633

Location

United States

Related Subject Headings

  • Swine
  • Spermatozoa
  • Sperm Motility
  • Sea Urchins
  • Phosphorylation
  • Phosphoprotein Phosphatases
  • Male
  • Immunoassay
  • Fluorescent Antibody Technique
  • Flagella