Cyclic GMP-specific phosphodiesterase-5 regulates motility of sea urchin spermatozoa.

Abstract:

:Motility, chemotaxis, and the acrosome reaction of animal sperm are all regulated by cyclic nucleotides and protein phosphorylation. One of the cyclic AMP-dependent protein kinase (PKA) substrates in sea urchin sperm is a member of the phosphodiesterase (PDE) family. The molecular identity and in vivo function of this PDE remained unknown. Here we cloned and characterized this sea urchin sperm PDE (suPDE5), which is an ortholog of human PDE5. The recombinant catalytic domain of suPDE5 hydrolyzes only cyclic GMP (cGMP) and the activity is pH-dependent. Phospho-suPDE5 localizes mainly to sperm flagella and the phosphorylation increases when sperm contact the jelly layer surrounding eggs. In vitro dephosphorylation of suPDE5 decreases its activity by approximately 50%. PDE5 inhibitors such as Viagra block the activity of suPDE5 and increase sperm motility. This is the first PDE5 protein to be discovered in animal sperm. The data are consistent with the hypothesis that suPDE5 regulates cGMP levels in sperm, which in turn modulate sperm motility.

journal_name

Mol Biol Cell

authors

Su YH,Vacquier VD

doi

10.1091/mbc.e05-08-0820

keywords:

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

114-21

issue

1

eissn

1059-1524

issn

1939-4586

pii

E05-08-0820

journal_volume

17

pub_type

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