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(Received for publication, August 29, 1997)
From the Ca2+ oscillations can be
induced in mammalian eggs and somatic cells by microinjection of a
cytosolic sperm protein factor. The nature of the sperm factor-induced
Ca2+ signaling was investigated by adding sperm protein
extracts to homogenates of sea urchin eggs, which contain multiple
classes of Ca2+ release mechanisms. We show that the sperm
factor mobilizes Ca2+ from non-mitochondrial
Ca2+ stores in egg homogenates after a distinct latency.
This latency is abolished by preincubation of sperm extracts with egg
cytosol. The preincubation step is highly
temperature-dependent and generates a high molecular
weight, protein-based Ca2+-releasing agent that can also
mobilize Ca2+ from purified egg microsomes. This
Ca2+ release appears to be mediated via both inositol
1,4,5-trisphosphate and ryanodine receptors, since homologous
desensitization of these two release mechanisms by their respective
agonists inhibits further release by the sperm factor. However, sperm
factor-induced Ca2+ release by these channels is
independent of inositol 1,4,5-trisphosphate or cADPR since antagonists
of either of these two messengers did not block the Ca2+
release effected by the sperm factor. The sperm protein factor may
cause Ca2+ release via an enzymatic step that generates a
protein-based Ca2+-releasing agent.
Volume 272, Number 46,
Issue of November 14, 1997
pp. 28901-28905
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
A Cytosolic Sperm Protein Factor Mobilizes Ca2+ from
Intracellular Stores by Activating Multiple Ca2+ Release
Mechanisms Independently of Low Molecular Weight Messengers
,
and
University Department of Pharmacology,
Medical Research Council National Institute for Medical
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