Insights into the Molecular Mechanisms Involved in Sea Urchin Fertilization Envelope Assembly

Somers, Cynthia E.; Shapiro, Bennett M.

doi:10.1111/j.1440-169x.1989.00001.x

Cited by 14 publications

(4 citation statements)

References 51 publications

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“…It serves as a simple model system to investigte the production, assembly, posttranslational modification, and degradation of an extracellular matrix. We first intended to analyze the FE component proteins to localize the tyrosine-derived cross-links DT and TT as well as the isopeptide cross-link formed by transglutaminase (Battaglia & Shapiro, 1987), and to add further information on the molecular mechanism of sea urchin FE assembly, which was recently reviewed by Somers and Shapiro (1989).…”

Section: Discussionmentioning

confidence: 99%

Pulcherosine, a novel tyrosine-derived, trivalent crosslinking amino acid from the fertilization envelope of sea urchin embryo

Nomura

Suzuki²,

Matsumoto³

1990

Biochemistry

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The normally hardened and aminotriazole-induced soft fertilization envelopes (FEs) of the sea urchin Hemicentrotus pulcherrimus and two other species were isolated and investigated for component proteins and cross-linking amino acids. From the acid hydrolysate of the hard FE of H. pulcherrimus, we isolated by reversed-phase high-performance liquid chromatography a novel fluorescent compound as well as dityrosine and trityrosine, the major tyrosine-derived cross-linking amino acids. These three compounds were also isolated from the reaction products of the tyrosine/horseradish peroxidase/H2O2 system. The structure of the novel compound, designated "pulcherosine", was determined to be 5-[4"-(2-carboxy-2-aminoethyl)phenoxy]-3,3'-dityrosine. With respect to the position of diphenyl ether bond between the tyrosine and dityrosine moieties, it is an isomer of isotrityrosine found in Ascaris cuticle collagen [Fujimoto et al. (1981) Biochem. Biophys. Res. Commun. 99, 637-643]. Isotrityrosine was not found in either of the above systems as a major component. The contents of tyrosine, dityrosine, trityrosine, and pulcherosine in the hard FE of H. pulcherrimus were estimated as 255, 5.5, 2.1, and 1.3 residues, respectively, per 10,000 total amino acid residues, while in the soft FE, those of tyrosine and dityrosine were 305 and 0.25 residues, respectively, and trityrosine and pulcherosine were only traces. The molar ratio of dityrosine, trityrosine, and pulcherosine in the hard FE was 100:38:24, while that for tyrosine/horseradish peroxidase/H2O2 reaction products was 100:3:8, respectively.

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Section: Discussionmentioning

confidence: 99%

Pulcherosine, a novel tyrosine-derived, trivalent crosslinking amino acid from the fertilization envelope of sea urchin embryo

Nomura

Suzuki²,

Matsumoto³

1990

Biochemistry

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“…As a consequence, the transformation of the VE into the fertilisation envelope occurs because of the formation of tyrosine cross-linkages contained in proteolyasin. This molecule is released from cortical granules and bound to the VE (Weidman et al, 1985; for a review see Somers & Shapiro, 1989). In D. pictus, peroxidase activity demonstrated in the egg Ringer indicates that this enzyme is released from the egg after fertilisation in frogs also.…”

Section: Discussionmentioning

confidence: 99%

Jelly plug dissolution in Discoglossus pictus eggs (Anura) involves peroxidase-like activity and oxidative opening of disulphide bonds

Pitari

Duprè

Fusco

et al. 1993

Zygote

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SummaryIn amphibian eggs the formation of a capsular chamber is one of the most striking events occurring either upon oviposition or after fertilisation. In the egg of the anuran Discoglossus pictus a capsular chamber forms following fertilisation or activation; the egg with its vitelline envelope rotates in this chamber according to gravity. Previous work showed that the chamber is the product of plug dissolution. The plug is a lens-shaped jelly coat, typical of Discoglossus, covering only part of the animal hemisphere. Its dissolution is caused by material released from the egg about 15 min after fertilisation through exocytosis of at least two types of vacuoles. Liquefaction of the plug correlates with the reduction of disulphide bonds present in the jelly matrix. In this study we investigated the nature of the substances released from the egg and some changes occurring in the plug during liquefaction. SDS-PAGE showed that the proteic profile of the plug changes dramatically after fertilisation, confirming proteic cleavage in the plug matrix during its dissolution. Through in vitro tests and electrophoretic analysis of the Ringer solution in which the egg exudate was collected, an increase in the activity of the solution was determined in the presence of hydrogen peroxide, and peroxidase activity was depicted in the egg exudate. The presence of free thiol groups and cysteic acid residues (or cysteine sulphinic acid) in the plugs of activated eggs was established, suggesting that during plug dissolution some disulphide bonds are oxidatively opened. This suggests that enzyme(s) with peroxidase activity are released following fertilisation. We surmise that such enzymes are contained in the intraovular vacuoles the exocytosis of which triggers the onset of plug liquefaction. The possible release of hydrogen peroxide from the egg is discussed.

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“…the contents of the primary cortical vesicles form the outer, or primary, egg envelope. This layer may correspond to the fertilization envelope of other animals, which is formed from the mixing of the vitelline layer with the exocytosed contents of the cortical vesicles (Kay and Shapiro, 1985;Somers and Shapiro. 1989).…”

Section: Discussionmentioning

confidence: 99%

The Origin of Cortical Vesicles and their Role in Egg Envelope Formation in the "Spiny" Eggs of a Calanoid Copepod, Centropages velificatus

Blades-Eckelbarger

Marcus

1992

The Biological Bulletin

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The mature oocytes of the marine calanoid copepod, Centropages velificatus, contain two morphologically distinct populations of cortical vesicles that undergo sequential exocytoses at the time of spawning. The contents of the primary cortical vesicles are released first and form the primary egg envelope. This is followed by the exocytosis of the secondary cortical vesicles. These contain numerous intracisternal granules that, upon release into the perivitelline space, transform into a mass of fine fibers. The continual accumulation of fibers constitutes an extracellular matrix between the primary envelope and the egg's plasmalemma. Further amassment of the fibers beneath the primary egg envelope results in the formation of long, spiny projections. The evolution of the cortical vesicles was traced to the early vitellogenic oocytes and appears to be unique. The two populations of cortical vesicles are synthesized together within the same cisternal elements of rough endoplasmic reticulum (RER). The RER originates from membranous blebs off both the nuclear membrane and stacks of annulate lamellae in the early vitellogenic oocytes. Numerous intracisternal granules are present within the RER. Some of these granules fuse, forming a dense, ring-like structure in the extremities of the cisternae. These bud off from the RER to become the primary cortical vesicles. The unfused intracisternal granules remain as discrete bodies within irregular profiles of vesicular ER and comprise the secondary cortical vesicles.

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Insights into the Molecular Mechanisms Involved in Sea Urchin Fertilization Envelope Assembly

Cited by 14 publications

References 51 publications

Pulcherosine, a novel tyrosine-derived, trivalent crosslinking amino acid from the fertilization envelope of sea urchin embryo

Pulcherosine, a novel tyrosine-derived, trivalent crosslinking amino acid from the fertilization envelope of sea urchin embryo

Jelly plug dissolution in Discoglossus pictus eggs (Anura) involves peroxidase-like activity and oxidative opening of disulphide bonds

The Origin of Cortical Vesicles and their Role in Egg Envelope Formation in the "Spiny" Eggs of a Calanoid Copepod, Centropages velificatus

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