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At least 19 recordsLinked to original sources
PubMed2006

Ecological role of purple sea urchins.

Sea urchins are major components of marine communities. Their grazing limits algal biomass, and they are preyed upon by many predators. Purple sea urchins (Strongylocentrotus purpuratus) are among the best studied species. They live in environments that alternate between two stable states: luxuriant, species-rich kelp forests and sea urchin-dominated "barrens." The transition from one state to the other can be initiated by several factors, including the abundance of algal food, predators, storm intensities, and incidence of disease. Purple sea urchins compete with other grazers, some of which are important fishery resources (such as abalones and red sea urchins), and they are harvested for scientific research. Revelations from their genome will lead to a better understanding of how they maintain their ecological importance, and may in turn enhance their economic potential.

Animals↗
PubMed1988

Synonymous nucleotide substitution rates of beta-tubulin and histone genes conform to high overall genomic rates in rodents but not in sea urchins.

Sea urchin and rodent genomes have been posited to evolve rapidly as indicated by divergences in single copy nuclear DNA sequences. We have examined whether the synonymous substitution rates of three highly conserved genes, beta-tubulin, histone H4, and histone H3, adhere to these high genomic substitution rates by comparing sequences between two sea urchins, Strongylocentrotus purpuratus and Lytechinus pictus, and between rodents and humans. Whereas the rate of change between the 3' untranslated regions of the beta-tubulin cDNA of S. purpuratus (Sp-beta 1), sequenced in this study, and of L. pictus (Lp-beta 3) was consistent with the overall rate of change estimated from previous DNA hybridization results between these species, the synonymous substitution rates for the carboxyl domains of these beta-tubulins, as well as for the late histones H4 and H3, were significantly depressed. In contrast, synonymous nucleotide substitution rates between rodents and between rodent and human for the carboxyl domain proper of identical beta-tubulin isotypes and for histone H4 and H3.1 did not differ from the overall rate of change for the rodent genomes. Moreover, an analysis of paralogous human and mouse beta-tubulin sequences supported the conclusion that the synonymous substitution rates in the mouse were higher than those in the human. Differences in constraint on evolutionary change were not evident strictly from the conserved amino acid sequences and base compositions of these genes. Other constraining influences seemed more relevant to the departure of the synonymous substitution rates of the sea urchin beta-tubulin and histone coding regions from the average genomic rate.

Amino Acid Sequence↗
PubMed2004

Proteolytic cleavage of the cell surface protein p160 is required for detachment of the fertilization envelope in the sea urchin.

Sea urchin eggs secrete a serine protease activity, CGSP1, at fertilization that is essential for the block to polyspermy. Several targets of this proteolytic activity on the plasma membrane were identified here using a cell surface biotinylation approach. Amino acid microsequencing of one of these proteins led to the identification of a 4.75-kb cDNA clone from a Strongylocentrotus purpuratus ovary cDNA library that encodes a 160-kDa protein called p160. This protein contains five CUB domains and a putative transmembrane domain suggesting that p160 is an integral membrane protein with protein-protein interaction motifs facing the extracellular matrix of the egg. Whole-mount immunolocalization studies demonstrate that p160 is on the surface of the egg, enriched at the tips of microvilli. The protein is removed at fertilization in a protease-dependent manner, and functional assays suggest that p160 serves to link the plasma membrane to the vitelline layer until fertilization. Thus, p160 is a key candidate for a vitelline-layer linker protein, the selective proteolysis of which functions in the block to polyspermy in the sea urchin egg.

Amino Acid Sequence↗
PubMed2005

The tube feet of sea urchins and sea stars contain functionally different mutable collagenous tissues.

Echinoderms possess mutable collagenous tissues (MCTs), which are capable of undergoing rapid changes in their passive mechanical properties mediated by secretions from a specific cell type, the juxtaligamental cell. In this study, the possible presence of MCTs in the tube feet of the echinoid Paracentrotus lividus and the asteroid Marthasterias glacialis was investigated by measuring their extensibility, tensile strength, stiffness and toughness after different treatments known to influence the physiological state of MCTs. Calcium removal reversibly induced a significant plasticization of the tube feet of both species. When exposed to cell-disrupting solutions, the tube foot stem of sea urchins and sea stars showed a significant increase in strength, stiffness and toughness in the absence of calcium. This response, combined with the ultrastructural observation of juxtaligamental-like cells in the connective tissue, confirms that an MCT is present in both echinoid and asteroid tube feet. It was observed, however, that the tube foot stems of P. lividus and M. glacialis are affected differently by exposure to cell-disrupting solutions in the presence of calcium, indicating that their MCTs could be functionally different. In their soft state, MCTs could assist the muscles in tube foot protraction, bending and retraction; in their stiff state, they could play a role in the energy-sparing maintenance of position; for example, during strong attachment to the substratum to resist hydrodynamically generated loads.

Analysis of Variance↗
PubMed2002

cDNA hox sequences 3' of the homeobox isolated from the sea urchin Holopneustes purpurescens are definitive for sea urchin Hox orthologues.

In an investigation into Hox genes in sea urchin development, cDNA nucleotide sequences were isolated from seven Hox genes of Holopneustes purpurescens by 3' RACE. Each sequence extended from the homeobox through the coding region 3' of the homeobox to the 3'untranslated region and, in the majority of sequences, to a poly(A) signal and a poly(A) tail. The cDNA sequences 3' of the homeoboxes were very different between the seven Hox genes. In contrast, the sequences within each Hox gene 3' of the homeobox were very similar, especially at the amino acid level, between the sea urchin species for which sequences are available. The coding regions 3' of the homeodomains are thus a means of unambiguously identifying homologies between sea urchin Hox genes. A phylogenetic analysis where amino acid motifs in these 3' coding regions were aligned with similar motifs in chordate species led us to classify two posterior sea urchin Hox genes, of uncertain affinity, as orthologues of Hox9 and Hox10 genes. Putative cytoplasmic polyadenylation elements were mapped in the 3' untranslated region of sea urchin Hox genes.

3' Untranslated Regions↗
PubMed1994

A monoclonal antibody against the dynein IC1 peptide of sea urchin spermatozoa inhibits the motility of sea urchin, dinoflagellate, and human flagellar axonemes.

To investigate the role of axonemal components in the mechanics and regulation of flagellar movement, we have generated a series of monoclonal antibodies (mAb) against sea urchin (Lytechinus pictus) sperm axonemal proteins, selected for their ability to inhibit the motility of demembranated sperm models. One of these antibodies, mAb D1, recognizes an antigen of 142 kDa on blots of sea urchin axonemal proteins and of purified outer arm dynein, suggesting that it acts by binding to the heaviest intermediate chain (IC1) of the dynein arm. mAb D1 blocks the motility of demembranated sea urchin spermatozoa by modifying the beating amplitude and shear angle without affecting the ATPase activity of purified dynein or of demembranated immotile spermatozoa. Furthermore, mAb D1 had only a marginal effect on the velocity of sliding microtubules in trypsin-treated axonemes. This antibody was also capable of inhibiting the motility of flagella of Oxyrrhis marina, a primitive dinoflagellate, and those of demembranated human spermatozoa. Localization of the antigen recognized by mAb D1 by immunofluorescence reveals its presence on the axonemes of flagella from sea urchin spermatozoa and O. marina but not on the cortical microtubule network of the dinoflagellate. These results are consistent with a dynamic role for the dynein intermediate chain IC1 in the bending and/or wave propagation of flagellar axonemes.

Adenosine Triphosphatases↗
PubMed1983

A factor in sea urchin eggs inhibits transcription in isolated nuclei by sea urchin RNA polymerase III.

Isolated nuclei from sea urchin embryos synthesize RNA at a rate comparable to other animal cell nuclei. All three RNA polymerases are active as judged by alpha-amanitin sensitivity and hybridization to specific cloned DNAs. Extracts were prepared from sea urchin eggs and embryos by extraction with 0.35 M KCl. None of the crude extracts had a large effect on total RNA synthesis. However, extracts from sea urchin eggs inhibited RNA polymerase III activity in nuclei from blastula and gastrula embryos. There was no effect on the synthesis of ribosomal RNA by RNA polymerase I or on the synthesis of two RNA polymerase II products, histone mRNA and the sea urchin analogue of U1 RNA. The inhibitor is present in two different species of sea urchin and has been 50-fold purified by diethylaminoethylcellulose and hydroxylapatite chromatography. The inhibitor is not present in extracts prepared from sea urchin blastula embryos.

Animals↗
PubMed2004

Molecular heterotopy in the expression of Brachyury orthologs in order Clypeasteroida (irregular sea urchins) and order Echinoida (regular sea urchins).

The expression patterns of Brachyury (Bra) orthologs in the development of four species of sand dollars (order: Clypeasteroida), including a direct-developing species, and of a sea urchin species (order: Echinoida) were investigated during the period from blastula to the pluteus stage, with special attention paid to the relationship between the expression pattern and the mode of gastrulation. The sand dollar species shared two expression domains of the Bra orthologs with the Echinoida species, in the vegetal ring (the first domain) and the oral ectoderm (the second domain). The following heterotopic changes in the expression of the Bra genes were found among the sand dollar species and between the sand dollars and the Echinoida species. (1) The vegetal ring expressing Bra in the sand dollars was much wider and was located at a higher position along the AV axis, compared with that in the Echinoida species. The characteristic Bra expression in the vegetal ring of the sand dollar embryos was thought to be involved in the mode of gastrulation, in which involution continues from the beginning of invagination until the end of gastrulation. (2) Two of the three indirect-developing sand dollar species that were examined exhibited a third domain, in which Bra was expressed on the oral side of the archenteron. (3) In the direct-developing sand dollar embryos, Bra was expressed with an oral-aboral asymmetry in the vegetal ring and with a left-right asymmetry in the oral ectoderm. In the Echinoida species, Bra was expressed in the vestibule at the six-armed pluteus stage.

Amino Acid Sequence↗
PubMed1996

Effect of caulerpenyne, a toxin extracted from Caulerpa taxifolia on mechanisms regulating intracellular pH in sea urchin eggs and sea bream hepatocytes.

The proliferation of the green marine alga Caulerpa taxifolia in the Mediterranean led us to investigate the toxic effects on marine organisms of caulerpenyne (Cyn), the major secondary metabolite synthesized by the alga. This study was performed on sea urchin eggs (Paracentrotus lividus) and isolated hepatocytes from the sea bream (Sparus aurata), in which accumulation of the toxins by metabolic processes may be of significance. Cyn provoked an acidification of seawater containing both unfertilized and fertilized eggs, as revealed by a titrable efflux of protons. The pHi in unfertilized eggs continuously increased in the presence of Cyn, whereas there was a biphasic response in both fertilized eggs and isolated hepatocytes, with a decrease of the pHi followed by recovery to the initial value. Cyn inhibited the accumulation of 14C-methylamine in acidic granules present in the cortical zone of sea urchin eggs. Dicyclocarbodiimide (DCCD), a well-known H(+)-ATPase inhibitor, provoked a similar inhibition. Both molecules increased pH in the acidic compartments of isolated bream hepatocytes. These results suggest that Cyn inhibits intracellular sequestration of protons and thus liberates protons into the cell cytoplasm from which they leak toward the extracellular medium.

Animals↗
PubMed2006

Translational control genes in the sea urchin genome.

Sea urchin eggs and early cleavage stage embryos provide an example of regulated gene expression at the level of translation. The availability of the sea urchin genome offers the opportunity to investigate the "translational control" toolkit of this model system. The annotation of the genome reveals that most of the factors implicated in translational control are encoded by nonredundant genes in echinoderm, an advantage for future functional studies. In this paper, we focus on translation factors that have been shown or suggested to play crucial role in cell cycle and development of sea urchin embryos. Addressing the cap-binding translational control, three closely related eIF4E genes (class I, II, III) are present, whereas its repressor 4E-BP and its activator eIF4G are both encoded by one gene. Analysis of the class III eIF4E proteins in various phyla shows an echinoderm-specific amino acid substitution. Furthermore, an interaction site between eIF4G and poly(A)-binding protein is uncovered in the sea urchin eIF4G proteins and is conserved in metazoan evolution. In silico screening of the sea urchin genome has uncovered potential new regulators of eIF4E sharing the common eIF4E recognition motif. Taking together, these data provide new insights regarding the strong requirement of cap-dependent translation following fertilization. The genome analysis gives insights on the complexity of eEF1B structure and motifs of functional relevance, involved in the translational control of gene expression at the level of elongation. Finally, because deregulation of translation process can lead to diseases and tumor formation in humans, the sea urchin orthologs of human genes implicated in human diseases and signaling pathways regulating translation were also discussed.

Amino Acid Sequence↗
PubMed2005

A sea urchin lectin, SUL-1, from the Toxopneustid sea urchin induces DC maturation from human monocyte and drives Th1 polarization in vitro.

The sea urchin Toxopneustes pileolus belonging to the family Toxopneustidae, they have well-developed globiferous pedicellariae with pharmacologically active substances. We have purified a novel sea urchin lectin-1 (SUL-1) from the large globiferous pedicellariae of T. pileolus. Dendritic cells (DC) are professional APC and play a pivotal role in controlling immune responses. This study investigated whether SUL-1 can drive DC maturation from human immature monocyte-derived DC in vitro. Human monocytes were cultured with GM-CSF and IL-4 for 6 days followed by another 1 day in the presence of SUL-1 or LPS. DC harvested on day 7 were examined using functional assays. The expression levels of CD1a, CD80, CD83, CD86 and HLA-DR as expressed by mean fluorescence intensity (MFI) on DC differentiated from immature DC after culture with 1.0 microg/ml of SUL-1 for 1 day were enhanced and decreased endocytic activity. SUL-1-treated DC also displayed enhanced T cell stimulatory capacity in an MLR, as measured by T cell proliferation. Cell surface expression of CD80, CD83 and CD86 on SUL-1-treated DC was inhibited by anti-DC-SIGN mAb, while anti-DC-SIGN mAb had no influence on allogeneic T cell proliferation by SUL-1-treated DC. DC differentiated with SUL-1 induced the differentiation of naïve T cell towards a helper T cell type 1 (Th1) response at DC/T (1:5) cells ratio depending on IL-12 secretion. In CTL assay, the production of IFN-gamma and 51Cr release on SUL-1-treated DC were more augmented than of immature DC or LPS-treated DC. SUL-1-treated DC expressed CCR7 and had a high migration to MIP-3beta. Intracellular Ca2+ mobilization in SUL-1-treated DC was also induced by MIP-3beta. These results suggest that SUL-1 bindings to DC-SIGN on surface of immature DC may lead to differentiate DC from immature DC. Moreover, it suggests that SUL-1 may be used on DC-based vaccines for cancer immunotherapy.

Animals↗
PubMed1991

Localization and characterization of phosphatidylcholine in sea urchin spermatozoa.

Sea urchin spermatozoa obtain energy for movement through oxidation of endogenous phospholipids, particularly phosphatidylcholine (PC). This study was undertaken to determine the localization of PC available for utilization in energy metabolism in spermatozoa of the sea urchin, Hemicentrotus pulcherrimus. Following incubation with sea water, the PC content in sperm heads decreased significantly, while that in sperm tails did not change. PC was abundant in sperm heads, particularly the midpieces. PC composed of unsaturated fatty acids was consumed to a greater extent during incubation than that consisting of saturated fatty acids. Analysis by gas-liquid chromatography indicated most of fatty acid moieties in the midpieces PC to be unsaturated. Phospholipase A2 activity was also distributed in sperm heads, particularly the midpieces. It thus appears that PC as a substrate for energy metabolism is located in the midpieces of sea urchin spermatozoa.

Animals↗
PubMed1994

Detection of vitellogenin in a subpopulation of sea urchin coelomocytes.

Sea urchin vitellogenin is a high molecular weight glycoprotein, which is the precursor of the major yolk protein present in the unfertilized egg. Vitellogenin processing into the major yolk protein and its further enzymatic cleavage during sea urchin embryonic development, has been extensively described, and the adhesive properties of the processed molecule have been studied. The function of vitellogenin in the adult, where it has been found in the coelomic fluid of both male and female individuals, is still unknown, although its role on promoting the adhesion of embryonic cells has been shown. In this report we describe the detection of vitellogenin in lysates of whole circulating coelomocytes of both male and female sea urchins of the species Paracentrotus lividus. By metrizoic acid gradients we purified total coelomocytes into six subpopulations that were tested for the occurrence of the molecule using vitellogenin-specific polyclonal antibodies. We detected vitellogenin only in the coelomocyte subpopulation called colorless spherule cells, packed in kidney-shaped granules located around the nucleus. We also showed that coelomocytes respond to stress conditions by discharging vitellogenin into the medium. This result together with previous observations on the adhesive properties of the molecule suggest a role for vitellogenin in the clotting phenomenon occurring after host invasion.

Animals↗
PubMed2001

Cyclin E and its associated cdk activity do not cycle during early embryogenesis of the sea Urchin.

Female sea urchins store their gametes as haploid eggs. The zygote enters S-phase 1 h after fertilization, initiating a series of cell cycles that lack gap phases. We have cloned cyclin E from the sea urchin Strongylocentrotus purpuratus. Cyclin E is synthesized during oogenesis, is present in the germinal vesicle, and is released into the egg cytoplasm at oocyte maturation. Cyclin E synthesis is activated at fertilization, although there is no increase in cyclin E protein levels due to continuous turnover of the protein. Cyclin E protein levels decline in morula embryos, while cyclin E mRNA levels remain high. After the blastula stage, cyclin E mRNA and protein levels are very low, and cyclin E expression is predominant only in cells that are actively dividing. These include cells in the left coelomic pouch, which forms the adult rudiment in the embryo. The cyclin E present in the egg is complexed with a protein kinase. Activity of the cyclin E/cdk2 changes little during the initial cell cycles. In particular, cyclin E-cdk2 levels remain high during both S-phase and mitosis. Our results suggest that progression through the early embryonic cell cycles in the sea urchin does not require fluctuations in cyclin E kinase activity.

Amino Acid Sequence↗
PubMed1995

Effects of retinoic acid and dimethylsulfoxide on the morphogenesis of the sea urchin embryo.

Sea urchin embryos of the species Paracentrotus lividus were treated continuously with different concentrations of all-trans retinoic acid (RA) or dimethylsulfoxide (DMSO) at different developmental stages. A delay in embryonic development was observed when embryos were cultured in the presence of 2 x 10(-5) M RA, between 1 and 12 hours of development. Hence, at 48 hours of development, while control embryos had reached the pluteus stage, RA-treated embryos were at the prism stage. At 72 hours of development RA-treated embryos recovered and continued normal development reaching the pluteus stage. No effect was observed when treatment was performed before 1 hour or after 12 hours of development. DMSO treatment had no effect on normal sea urchin embryo development, although we observed that pigment cells, clearly visible at the pluteus stage, become visible earlier with respect to control embryos. This report confirms the advantages that the sea urchin embryo offers for the study of problems in cellular and developmental biology.

Animals↗
PubMed2001

Brachyury homolog (HpTa) is involved in the formation of archenteron and secondary mesenchyme cell differentiation in the sea urchin embryo.

Sea urchin Brachyury homolog (HpTa) is expressed exclusively in the vegetal plate and secondary mesenchyme cells in the embryos of sea urchin Hemicentrotus pulcherrimus. In order to gain insights into the role of HpTa during sea urchin development, we designed experiments to perturb the embryo by inducing ectopic overexpression of HpTa by injecting fertilized eggs with HpTa mRNA. The overexpression of HpTa resulted in suppression of the formation of vegetal plate and secondary mesenchyme cells. We assume that the interaction of HpTa with unknown factors is required for the activation of the HpTa target genes, and that the excess amount of HpTa proteins produced from injected HpTa mRNA depletes the co-factors. In consequence, the target genes of HpTa would be repressed by the overexpression of HpTa. We suggest that HpTa is involved in the formation of the vegetal plate and the differentiation of secondary mesenchyme cells.

Journal Article↗