Phosphorylation of sperm histone H1 is induced by the egg jelly layer in the sea urchin Strongylocentrotus purpuratus

Porter, Donald C.; Vacquier, Victor D.

doi:10.1016/0012-1606(86)90057-6

Cited by 25 publications

(18 citation statements)

References 46 publications

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“…The antibodies induce the CAMP-dependent phosphorylation of sperm histone H1 as occurs upon treatment of spermatozoa with egg jelly (1 6, 39, 40). However, ionophore A23187 which is known to induce the acrosome reaction and acts as a co-factor of pronase-digested FSG for induction of the acrosome reaction neither induces H1 phosphorylation nor increases cAMP concentration in sea urchin spermatozoa (8,39,66). These support the idea suggesting that cAMP is not directly involved in the acrosome reaction.…”

Section: Discussionsupporting

confidence: 55%

Purification and Characterization of the Egg Jelly Macromolecules, Sialoglycoprotein and Fucose Sulfate Glycoconjugate, of the Sea Urchin Hemicentrotus Pulcherrimus

et al. 1990

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A sialoglycoprotein and a fucose sulfate glycoconjugate (FSG) were purified from egg jelly of the sea urchin Hemicentrotus pulcherrimus. Sialoglycoprotein which consisted of sialic acid (90%, w/w) and protein (10%, w/w) did not cause induction of the acrosome reaction and sperm isoagglutination. FSG which contained one mol sulfate/mol fucose possessed 2.0 times protein to fucose by weight. The proteins in intact FSG were separated to two major (258 kDa and 237 kDa) and one minor (120 kDa) proteins by SDS‐polyacrylamide gel electrophoresis (SDS‐PAGE) in the presence of 2‐mercaptoethanol (2‐ME) while the proteins could not be separated by HPLC in the presence of 0.1% SDS or SDS‐PAGE without 2‐ME. However, after carboxymethylation of FSG, two major (260 kDa and 240 kDa) proteins and two minor (140 kDa and 135 kDa) proteins were separated from the fucose sulfate moiety by HPLC in the presence of 0.1% SDS or SDS‐PAGE without 2‐ME. When FSG was first carboxymethylated with non‐radioactive iodoacetic acid and then reduced with 2‐ME and finally carboxymethylated with 14C‐iodoacetic acid, the most of radioactivity was detected in 140 kDa and 135 kDa proteins. Carboxymethylted‐FSG was less potent than intact FSG in induction of the acrosome reaction. Fucoidan, a fucose sulfate polymer, did not induce the acrosome reaction.

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Section: Discussionsupporting

confidence: 55%

Purification and Characterization of the Egg Jelly Macromolecules, Sialoglycoprotein and Fucose Sulfate Glycoconjugate, of the Sea Urchin Hemicentrotus Pulcherrimus

et al. 1990

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Section: Methodsmentioning

confidence: 99%

“…Externalization of the contents of the acrosome granule was assessed by anti-bindin immunofluorescence (21). The 70% (vol/vol) ethanol-insoluble fraction of eggjelly (FSG) was prepared as described (9,22). Artificial sea water (ASW), calcium-free ASW, and ASW containing various concentrations of Ca2 , were formulated as described (23), and buffered to pH 7 mAbs.…”

Section: Methodsmentioning

confidence: 99%

Monoclonal antibodies increase intracellular Ca2+ in sea urchin spermatozoa.

Trimmer¹,

Schackmann²,

Vacquier³

1986

Proc. Natl. Acad. Sci. U.S.A.

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These mAbs make it possible to separate the increase in [Ca2+ h from the increase in pHi and may be useful in the elucidation of the regulatory role of Ca2+ in sperm physiology.Increases in both cytoplasmic free Ca2" ([Ca2"]j) and pH (pHi) underlie activation of cellular activities such as mitogenesis (1) and fertilization (2). The activation of sea urchin spermatozoa at fertilization consists of the following two major events: (i) initiation ofmotility and respiration resulting from an increase in pHi of about 0.4 unit to pHi 7.4 (3-7) and (it) the exocytotic acrosome reaction (AR), occurring when the sperm encounters the jelly layer surrounding the egg (8). An ethanol-insoluble component of eggjelly, which is a large fucose sulfate-rich glycoconjugate (FSG), possesses the ARinducing activity (9-11). Induction of the AR by FSG is dependent on millimolar concentrations of external Ca2" ([Ca2`],) and an additional increase in pHi to =7.6 (5, 6, 12-15). The AR can also be induced by ionophores or alteration of the ion concentration of seawater to cause both the entrance of Ca2' and the elevation of pH1 (12,13 (Mr, 210,000) of sea urchin spermatozoa has implicated this protein in the regulation of ionic changes associated with the AR (20). We have reported (20) that mAb J10/14 inhibits both the FSG-induced AR and the subsequent long-duration 45Ca2+ accumulation. However, by using the Ca2+ indicators indo-1 and fura-2, we now report that both J10/14 and another mAb to the 210-kDa protein, J18/2, induce rapid increases in sperm [Ca2+]i to levels even greater than those induced by FSG. These mAb-induced increases in sperm [Ca2+], occur without an increase in pHi, and the AR is not induced. When the mAb-induced-increase in [Ca2+], is combined with an NH4Cl treatment to increase pHi, the AR is induced. These mAbs to the 210-kDa protein are thus valuable reagents for studying the physiological effects of increases in sperm [Ca2 ]i in the absence of an elevation in pHi. MATERIALS AND METHODSCells and Media. Gametes of Strongylocentrotus purpuratus were collected directly from the gonopore and stored undiluted ("dry" sperm); the AR was scored; and egg jelly was obtained as described (20). Externalization of the contents of the acrosome granule was assessed by anti-bindin immunofluorescence (21). The 70% (vol/vol) ethanol-insoluble fraction of eggjelly (FSG) was prepared as described (9,22 9055The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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“…These fluxes result in E m changes (215,218) and elevations of [Ca 2ϩ ] i (224,225,257), pH i (225,312), [Na ϩ ] i (437), cAMP (202,204), and IP 3 (153). These physiological AR agonists also stimulate the activity of PKA (207,415), phospholipase D (154), and nitric oxide synthase (302). In mammalian spermatozoa, PLC-␦4 is required for the ZP-and progesterone-induced AR (186).…”

Section: A Generalitiesmentioning

confidence: 99%

Calcium Channels in the Development, Maturation, and Function of Spermatozoa

Darszon

Nishigaki

Beltrán

et al. 2011

Physiological Reviews

319

313

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-permeable channels and located them at distinct sites in spermatozoa so that they can help fertilize the egg. New tools to study sperm ionic currents, and image intracellular Ca 2ϩ with better spatial and temporal resolution even in swimming spermatozoa, are revealing how sperm ion channels participate in fertilization. This review critically examines the involvement of Ca 2ϩ channels in multiple signaling processes needed for spermatozoa to mature, travel towards the egg, and fertilize it. Remarkably, these tiny specialized cells can express exclusive channels like CatSper for Ca 2ϩ and SLO3 for K ϩ , which are attractive targets for contraception and for the discovery of novel signaling complexes. Learning more about fertilization is a matter of capital importance; societies face growing pressure to counteract rising male infertility rates, provide safe male gamete-based contraceptives, and preserve biodiversity through improved captive breeding and assisted conception initiatives.

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Phosphorylation of sperm histone H1 is induced by the egg jelly layer in the sea urchin Strongylocentrotus purpuratus

Cited by 25 publications

References 46 publications

Purification and Characterization of the Egg Jelly Macromolecules, Sialoglycoprotein and Fucose Sulfate Glycoconjugate, of the Sea Urchin Hemicentrotus Pulcherrimus

Purification and Characterization of the Egg Jelly Macromolecules, Sialoglycoprotein and Fucose Sulfate Glycoconjugate, of the Sea Urchin Hemicentrotus Pulcherrimus

Monoclonal antibodies increase intracellular Ca2+ in sea urchin spermatozoa.

Calcium Channels in the Development, Maturation, and Function of Spermatozoa

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