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PubMed2003

Field contamination of the starfish Asterias rubens by metals. Part 1: Short- and long-term accumulation along a pollution gradient.

The accumulation of Cd, Pb, Zn, and Cu in the starfish Asterias rubens was studied in a Norwegian fjord characterized by a gradient of metal pollution in the sediments, ranging from very high metal concentrations at its head to much lower levels at its opening. The concentrations of metals in starfish from natural populations along the gradient (long-term accumulation) and in starfish that were transferred up the gradient (short-term accumulation) were compared. At long-term, Cd and Pb accumulations by starfish living at normal salinity (30/1000) were related to the level of contamination of the environment while Cu and, to a lesser extent, Zn accumulations appeared strictly controlled. At short-term, Pb was accumulated steadily, Cd and Zn were accumulated transiently in the pyloric caeca (fast compartment), and Cu was not accumulated at all. Depuration experiments (transfer down the gradient) showed that Cd and Pb were efficiently eliminated from the pyloric caeca but not from the body wall (slow compartment). It is concluded that Pb is chronically accumulated, without apparent control, Cd is subjected to a regulating mechanism in the pyloric caeca which is overwhelmed over the long-term; Zn is tightly controlled in the pyloric caeca and Cu in both pyloric caeca and body wall. A distinct color variety of starfish is restricted to the low salinity (22-26/1000) superficial water layer. This variety showed a different pattern of metal accumulation over the long-term. This pattern is attributed to the particular hydrological conditions prevailing in this upper layer.

Animals↗
PubMed1997

Occurrence of paralytic shellfish poison in the starfish, Asterias amurensis in Kure Bay, Hiroshima Prefecture, Japan.

In May 1996, during surveillance on the toxicity of invertebrates such as bivalves inhabiting the coasts of Hiroshima Bay, the starfish Asterias amurensis collected in the estuary of the Nikoh River was found to contain toxins which showed strong paralytic action in mice; the maximum toxicity (as paralytic shellfish poison, PSP) was 8.0 MU/g for whole body and 28.7 MU/g for viscera throughout the monitoring period, March to July 1996. Attempts were made to identify the paralytic toxins in the starfish. They were extracted with 80% ethanol acidified with acetic acid, followed by defatting with dichloromethane. The aqueous layer obtained was treated with activated charcoal and then applied to a Sep-Pak C18 cartridge. The unbound toxic fraction was analyzed by high-performance liquid chromatography techniques. The starfish toxin was rather unexpectedly identified as PSP. It was comprised of high toxic components (gonyautoxin-1; GTX1, GTX2, GTX3, GTX4, decarbamoyl-GTX3; dcGTX3 and dcSTX) as the major components, which accounted for approximately 77 mole% of all components, along with protogonyautoxin-1, 2, 3 and 4 (PX1-4), which are N-sulfocarbamoyl derivatives. Of the high toxic components, GTX1 was present in the largest amounts. It was concluded that the toxin of starfish collected in the estuary of Nikoh River in May 1996 consisted of PSP, which supposedly came via the food chain from toxic bivalves living in the same area. To our knowledge, this is the first report of the occurrence of PSP in starfish.

Animals↗
PubMed1975

Cytoplasmic activation of starfish oocytes by sperm and divalent ionophore A-23187.

The relationship between onset of the early cytoplasmic stages of oocyte activation (vitelline membrane separation and elevation) and nuclear meiotic maturation was investigated in starfish oocytes after their exposure to divalent ionophore (A-23187) or sperm. Meiotically mature oocytes, isolated in calcium-free seawater, underwent activation in response to sperm or ionophore as previously reported. Large, immature starfish oocytes, arrested in prophase I of meiosis (germinal vesicle stage), underwent vitelline membrane elevation when treated with divalent ionophore A-23187 or starfish sperm. Histological studies demonstrated that cortical granule breakdown in the oocyte cortex was associated with vitelline membrane elevation after these treatments. Activation of oocytes by sperm occurred only in response to starfish sperm. Sea urchin, sand dollar, surf clam, or marine worm sperm did not induce vitelline membrane elevation of either immature or mature starfish oocytes. Sperm- or ionophore-activated immature oocytes underwent nuclear maturation after addition of the meiosis-inducing hormone, l-methyladenine; however, parthenogenetic development did not occur and embryonic development was markedly inhibited. In contrast to previous studies, the present results indicate that cytoplasmic activation can be initiated before and without hormone induction of the nuclear maturation process. Differentiation of the oocyte cell surface or cortex reactivity therefore appears to occur during oogenesis rather than as a consequence of maturation. The data further support the view that divalent ions mediate certain of the early activation responses initiated by sperm at the time of fertilization and that synchronization of fertilization to the meiotic process in the oocyte is important for the occurrence of normal development.

Adenine↗
PubMed2006

p90Rsk is required for G1 phase arrest in unfertilized starfish eggs.

The cell cycle in oocytes generally arrests at a particular meiotic stage to await fertilization. This arrest occurs at metaphase of meiosis II (meta-II) in frog and mouse, and at G1 phase after completion of meiosis II in starfish. Despite this difference in the arrest phase, both arrests depend on the same Mos-MAPK (mitogen-activated protein kinase) pathway, indicating that the difference relies on particular downstream effectors. Immediately downstream of MAPK, Rsk (p90 ribosomal S6 kinase, p90(Rsk)) is required for the frog meta-II arrest. However, the mouse meta-II arrest challenges this requirement, and no downstream effector has been identified in the starfish G1 arrest. To investigate the downstream effector of MAPK in the starfish G1 arrest, we used a neutralizing antibody against Rsk and a constitutively active form of Rsk. Rsk was activated downstream of the Mos-MAPK pathway during meiosis. In G1 eggs, inhibition of Rsk activity released the arrest and initiated DNA replication without fertilization. Conversely, maintenance of Rsk activity prevented DNA replication following fertilization. In early embryos, injection of Mos activated the MAPK-Rsk pathway, resulting in G1 arrest. Moreover, inhibition of Rsk activity during meiosis I led to parthenogenetic activation without meiosis II. We conclude that immediately downstream of MAPK, Rsk is necessary and sufficient for the starfish G1 arrest. Although CSF (cytostatic factor) was originally defined for meta-II arrest in frog eggs, we propose to distinguish ;G1-CSF' for starfish from ;meta-II-CSF' for frog and mouse. The present study thus reveals a novel role of Rsk for G1-CSF.

Animals↗
PubMed1995

MAT1 ('menage à trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK.

The kinase responsible for Thr161-Thr160 phosphorylation and activation of cdc2/cdk2 (CAK:cdk-activating kinase) has been shown previously to comprise at least two subunits, cdk7 and cyclin H. An additional protein co-purified with CAK in starfish oocytes, but its sequencing did not reveal any similarity with any known protein. In the present work, a cDNA encoding this protein is cloned and sequenced in both starfish and Xenopus oocytes. It is shown to encode a new member of the RING finger family of proteins with a characteristic C3HC4 motif located in the N-terminal domain. We demonstrate that the RING finger protein (MAT1: 'menage à trois') is a new subunit of CAK in both vertebrate and invertebrates. However, CAK may also exist in oocytes as heterodimeric complexes between cyclin H and cdk7 only. Stable heterotrimeric CAK complexes were generated in reticulocyte lysates programmed with mRNAs encoding Xenopus cdk7, cyclin H and MAT1. In contrast, no heterodimeric cyclin H-cdk7 complex could be immunoprecipitated from reticulocyte lysates programmed with cdk7 and cyclin H mRNAs only. Stabilization of CAK complexes by MAT1 does not involve phosphorylation of Thr176, as the Thr176-->Ala mutant of Xenopus cdk7 could engage as efficiently as wild-type cdk7 in ternary complexes. Even though starfish MAT1 is almost identical to Xenopus MAT1 in the RING finger domain, the starfish subunit could not replace the Xenopus subunit and stabilize cyclin H-cdk7 in reticulocyte lysate, suggesting that the MAT1 subunit does not (or not only) interact with cyclin H-cdk7 through the RING finger domain.

Amino Acid Sequence↗
PubMed1991

Involvement of G-proteins and adenylate cyclase in the action of gonad-stimulating substance on starfish ovarian follicle cells.

Gonad-stimulating substance (GSS) secreted from radial nerves induces meiotic maturation of starfish oocytes by stimulating production of 1-methyladenine (1-MeAde) in ovarian follicle cells. We have previously shown that cAMP mediates the action of GSS on 1-MeAde synthesis by starfish ovarian follicle cells. The present study examines the possible involvement of guanine nucleotide-binding regulatory proteins (G-proteins) and adenylate cyclase in the action of GSS on 1-MeAde production by starfish (Asterina pectinifera) follicle cells. GSS slightly stimulated adenylate cyclase activity in crude membrane preparations of follicle cells. GTP markedly enhanced this action of GSS in a dose-dependent manner. Nonhydrolyzable GTP analogs such as guanosine 5'-O-(3-thiotriphosphate) and 5'-guanylylimidodiphosphate, NaF, and forskolin also stimulated adenylate cyclase activity. In addition, chorela toxin (CT) stimulated adenylate cyclase activity in membrane preparations in the presence of NAD and GTP. Unlike adenylate cyclase, phosphodiesterase activity was not influenced by GSS. When crude membranes of follicle cells were incubated with [alpha-32P]NAD in the presence of CT and pertussis toxin, 45-kDa and 41-kDa proteins were ADP-ribosylated, respectively, suggesting the presence of two types (stimulatory and inhibitory) of G-proteins. It is concluded that G-proteins and adenylate cyclase play an important role in the action of GSS on 1-MeAde production by starfish ovarian follicle cells.

Adenine↗
PubMed1987

Unusual genetic codes and a novel gene structure for tRNA(AGYSer) in starfish mitochondrial DNA.

The nucleotide sequence of a 3849-bp fragment of starfish mitochondrial genome was determined. The genes for NADH dehydrogenase subunits 3, 4, 5, and COIII, and three kinds of (tRNA(UCNSer), tRNA(His), and tRNA(AGYSer) were identified by comparing with the genes of other animal mitochondria so far elucidated. The gene arrangement of starfish mitochondrial genome was different from those of vertebrate and insect mitochondrial genomes. Comparison of the protein-encoding nucleotide sequences of starfish mitochondria with those of other animal mitochondria suggested a unique genetic code in starfish mitochondrial genome; both AGA and AGG (arginine in the universal code) code for serine, AUA (isoleucine in the universal code but methionine in most mitochondrial systems) for isoleucine, and AAA (lysine) for asparagine. It was also inferred that these AGA and AGG codons are decoded by serine tRNA(AGYSer) originally corresponding to AGC and AGU codons. This situation is similar to the case of Drosophila mitochondrial genome. Variations in the use of AGA and AGG codons were discussed on the basis of the evolution of animals and decoding capacity of various tRNA(AGYSer) species possessing different sizes of the dihydrouridine (D) arm.

Animals↗
PubMed2000

Heteroplasmic conjugates formed by the fusion of starfish oocyte pairs with a 12 minute time difference in the maturation phase.

Two starfish oocytes with a 12 min time difference in the maturation phase were fused together with electric pulses to make a heteroplasmic conjugate. The starfish used were Asterina pectinifera. The emergence of the first meiotic spindle and the extrusion of the polar bodies in the conjugate were timed. Under polarization microscopy two meiotic spindles emerged with a time difference of 10-11 min, which is close to the time difference in the maturation phase between the original oocytes before fusion. In contrast, subsequent formation of the first two polar bodies occurred successively with a short time lag of 1-3 min between them. Times for the formation of both polar bodies were midway between the anticipated times for polar body formation in respective non-fused control oocytes. Thus, in one nucleus the meiotic division was delayed, while in another nucleus it was accelerated, in a single heteroplasmic conjugate. These two sets of observations indicate the presence of a certain control system that regulates progression of the cell cycle at a point during the period from the entry into metaphase through to late anaphase of meiosis I in starfish oocytes. This type of cell cycle control in starfish oocytes is obviously distinct from the currently accepted view of the cell cycle control by the spindle assembly checkpoint that monitors unattached kinetochores of mitotic chromosomes.

Animals↗
PubMed1977

The effect of myosin antibody on the division of starfish blastomeres.

Antiserum against starfish egg myosin was produced in rabbits. Antibody specificity to myosin was demonstrated by Ouchterlony's immunodiffusion test and by immunoelectrophoresis in the presence of sodium dodecylsulfate (SDS). The latter technique showed that the antibody binds to both heavy and light chains of egg myosin. Furthermore, the antibody reacted with starfish sperm mysosin and starfish adult muscle myosin at both the heavy and light chains. It did not react with bovine platelet mysosin or rabbit skeletal muscle myosin in Ouchterlony's test; however, a weak reaction was observed in the presence of SDS between the antibody and these myosin heavy chains. Ca- and Mg-ATPase activities of egg myosin were not affected by the antibody, but it did inhibit actin-activated ATPase activity of egg myosin. Microinjection of the antibody into blastomeres of starfish eggs at the two-cell stage was carried out. Anti-egg myosin gamma-globulin inhibited the subsequent cleavages at an amount of more than 0.3 ng when injected at interphase. The inhibition was reduced when the injection was carried out near the initiation of cleavage. At the onset of the second cleavage the antibody was not inhibitory; however, an appropriate amount inhibited the third cleavage. Although the disappearance of the nuclear membrane was observed in the presence of the antibody, the formation of the mitotic apparatus was more or less disturbed. However the formation of daughter nuclei seemed to be scarcely affected by the antibody except that the distance between the nuclei was significantly smaller than normal.

Actins↗
PubMed2000

[Localization, kinetic parameters, and functions of cholinesterase of the starfish ampulla].

The starfish amplullae cholinesterase was shown to represent acetylcholinesterase and enhance its activity along with increasing motility of the starfish. Bundles of muscle fibres containing cholinesterase were found in the ampullae. Cholinesterase was shown to be localized in the muscle cells and in collagen layer in vicinity of the muscle cells. The data obtained suggest participation of the starfish ampullae cholinesterase in non-synaptic cholinergic transmission between the radial nerve axons and the muscle fibre extension. Besides, the enzyme could take part in functional relationship between the muscle cells and the outer epithelial cells of the starfish ampullae.

Acetylcholinesterase↗
PubMed2000

[The effects of starfish sterol on platelet aggregation].

Through the internal and external experiments of platelet aggregation on rats and rabbits, we study the effects of starfish sterol (No. A1998) on the formation of experimental thrombus in vitro and the effects of platelet aggregation induced by arachidonic acid (AA), ADP, CaCl2. Starfish sterol A 1998 can inhibit the formation of experimental thrombus in vitro of rats on the rates of 10.0%, 20.1%, 25.9% (P < 0.01), p.o. starfish sterol 4.5, 13.5, 40.5 mg/kg. A 1998 can inhibit platelet aggregation induced by AA, ADP, CaCl2 in the same time. It can be concluded that starfish sterol has inhibitory effects on platelet aggregation.

Adenosine Diphosphate↗
PubMed1977

The starfish (Patiria and Pisaster) oocyte: a model system for the study of hormone-surface interaction in oogenesis.

Studies were made to determine if the starfish (Patiria and Pisaster) oocyte could serve as a model system for investigations of hormone-surface interactions in eucaryotic cells. Treatment of starfisch oocytes with maturation inducing hormone, 1-methyladenine, was observed by scanning electron microscopy to induce surface alteration. The action of the hormone was dependent on the presence of the cation Ca++. Although caffeine, theophylline, and theobromine supposedly inhibit maturation of oocytes, studies using the starfish oocyte showed that theobromine does not inhibit maturation and the inhibition caused by caffeine and theophylline is reversible. Other studies using the starfish oocyte and tritiated 1-methyladenine showed that the hormone does not dissociate from the oocyte once bound, and that the oocyte surface may have multiple receptors for 1-methyladenine. From these studies it was concluded that the starfish oocyte is a useful model for studies of hormone-surface interactions in eucaryotic cells.

Adenine↗
PubMed1983

Establishment of embryonic axes in larvae of the starfish, Asterina pectinifera.

In order to clarify the relationships between the first cleavage plane and the embryonic axes, early cleavage pattern of the fertilized eggs of the starfish. Asterina pectinifera was reexamined. It was ascertained that the polar bodies were formed at the site to which the germinal vesicle had closely located before the initiation of the meiotic division, and that the first cleavage plane passed near this site of polar body formation. While some of the early embryos of this starfish were observed to show various cleavage patterns during early cleavage stage, more than 70% of the embryos developed according to, so to say, the 'typical' cleavage pattern. Next, horseradish peroxidase (HRP) was injected into one of the blastomeres of the 2-cell- or 8-cell-stage embryos. The embryos were allowed to develop up to either the early gastrula or the early bipinnaria stage and stained to detect the descendants of the blastomere injected with HRP. In early gastrulae still retaining radial symmetry, the activity of HRP injected at the 2-cell stage was found only in one side of the embryo partitioned by one of the symmetrical planes. When one of the four blastomeres lying nearer to the polar bodies at the 8-cell stage was marked with HRP, its descendants constituted one quarter of the anterior part of the gastrula, and descendants of a blastomere opposite the polar bodies were found in the posterior region of the embryo. It was concluded that the animal-vegetal (AV) axis was pre-existing in the fertilized egg and that the first cleavage plane contained this primary axis. In early bipinnariae with their dorsoventral (DV) axes already established, the region of activity of the HRP injected at the 2-cell stage was still demarcated by a plane which passed through the AV axis, but the plane of the boundary had no fixed relation to the DV axis. The results indicate that the first cleavage plane does not necessarily correspond to the median plane of the starfish larva, unlike the case in sea-urchin eggs (Hörstadius & Wolsky, 1936). In other words, the DV axis of the starfish embryo is not predetermined in the fertilized egg, and might be established in the course of development through cell-to-cell interactions, while the AV axis is established mainly according to the pre-existing egg polarity.

Animals↗
PubMed2005

Accumulation of butyl- and phenyltin compounds in starfish and bivalves from the coastal environment of Korea.

Triphenyltin (TPT) and tributyltin (TBT) concentrations were determined in two starfish species (Asteria pectinifera and Asterias amurensis), bivalves (Crassostrea gigas or Mytilus edulis), and seawater samples from sites around the coasts of Korea. Both TPT and TBT concentrations in starfish ranged from 8 to 1560 ng/g and from <2 to 797 ng/g as Sn on a dry weight basis, respectively. TPT concentration accounted for 75.4% and 86.4% of total phenyltin concentration in A. pectinifera and A. amurensis, respectively, while monobutyltin, a degradation product of TBT, accounted for 86.3% and 57.2% of total butyltin, respectively. Triphenyltin concentrations in A. pectinifera were significantly correlated to water and bivalve TPT concentrations, which implies that dietary uptake of TPT from contaminated prey as well as direct uptake from surrounding water contribute to TPT body residues in the starfish. Starfish could be target organisms for monitoring TPT compound in the marine environment, due to their high accumulation and low degradation capacity towards TPT.

Animals↗
PubMed1984

Electrical stimulation of the starfish's radial nerve in vitro induces the release of a gonadotrophin.

In starfish a neuropeptide responsible for the induction of ovulation and the reinitiation of meiotic maturation in fully grown oocytes appears to be released from the radial nerves at the time of spawning. The objectives of this investigation were to determine if the radial nerve would release this gonadotrophin when electrically stimulated in vitro and to locate other possible sources of this factor. Electrical stimulation of radial nerves isolated from the starfish, Pycnopodia helianthoides, resulted in the release of the gonadotrophin. Significant amounts of this neuropeptide were detected neither in other tissues of the starfish nor in mammalian nervous tissue.

Adenine↗
PubMed2001

Starfish oocytes form intracellular ice at unusually high temperatures.

Starfish oocytes, eggs, and embryos are popular models for studying meiotic maturation, fertilization, and embryonic development. Their large (170- to 200-microm) oocytes are obtainable in copious amounts and are amenable to manipulations that mammalian oocytes are not. The most formidable obstacle to working with marine oocytes is their seasonal availability, yet a successful means of preserving them for use during the nonreproductive season has not been reported. The aim of this study was to investigate the response of starfish oocytes to freezing with rapid and slow cooling rates under a variety of conditions to develop a cryopreservation protocol for these cells. Cryomicroscopic observation revealed that starfish oocytes in isotonic medium undergo intracellular ice formation (IIF) at very high subzero temperatures, such that the mean difference between the temperature of extracellular ice formation (T(EIF)) and IIF (TI(IF)) was less than 3 degrees C and the average T(IIF) was approximately between -4 and -6 degrees C. Neither partial cellular dehydration nor addition of the cryopreservative dimethyl sulfoxide significantly depressed the T(IIF). Under some conditions, we observed ice nucleation at multiple locations within the cytoplasm, suggesting that several factors contribute to the unusually high T(IIF) during controlled-rate freezing and thus vitrification may be a more suitable method for cryopreserving these cells.

Animals↗
PubMed1995

Identification and partial characterization of yolk and cortical granule proteins in eggs and embryos of the starfish, Pisaster ochraceus.

The unfertilized oocyte contains various granules which serve as storage sites for proteins, the majority which are yolk granules or platelets. Yolk granules are thought to provide the developing embryo with nutrients essential for its survival, while other granules contain proteins such as enzymes and extracellular matrix components that are required for fertilization and perhaps for early development. This study uses immunofluorescence and immunogold techniques with two novel monoclonal antibodies against proteins found in egg yolk and cortical granules to study the localizations of these antigens during early starfish development. Partial biochemical characterizations using the anti-yolk antibody have revealed that there are a family of structurally related proteins in oocyte yolk granules and that while the molecular compositions of the yolk proteins change during embryogenesis, their depletion is not significant until the larval stage, suggesting these proteins are not required for early development. In addition, a large immunoreactive protein has been found in the intestine and coelomic fluid, suggesting that, as in other species, the starfish yolk proteins may be derived from a large precursor, such as vitellogenin. Analysis of the anti-cortical granule antibody has revealed that a 120-kDa antigen is stored in antibody has revealed that a 120-kDa antigen is stored in cortical granules of unfertilized eggs. Upon egg activation, the cortical granules located in the peripheral egg cytoplasm undergo exocytosis, and the 120-kDa antigen is released into the perivitelline space. However, other granules, which are also labeled by this antibody, remain dispersed throughout the egg cytoplasm and are still present in the early gastrula, where they appear to contribute to the extracellular matrices of the developing embryo. This suggests that starfish cortical granules play a dual function: At fertilization, where they help create a block to polyspermy, and in embryonic development, where they secrete extracellular matrix components.

Animals↗
PubMed1995

A periodic network of G protein beta gamma subunit coexisting with cytokeratin filament in starfish oocytes.

Heterotrimeric G proteins are membrane-bound and carry signals from activated receptors on plasma membranes to cytoplasmic effector enzymes and channels. In starfish oocytes, the beta gamma subunit of G protein mediates 1-methyladenine stimulation of oocyte maturation. In order to investigate the localization of beta gamma subunits in starfish oocytes during oocyte maturation, we raised a monoclonal antibody against the beta subunit. By immunofluorescence microscopy using the antibody, immature oocytes show a network of fibers in the cytoplasm. The staining of fibers is beaded with a periodicity of 0.7 microns. The same staining pattern is obtained by anti-gamma subunit antibody. In addition, the fibers are stained by anti-cytokeratin antibody. These results indicate that the G protein beta gamma subunit coexists with cytokeratin filaments in starfish oocytes. Stimulation of oocyte maturation by 1-methyladenine causes the beta gamma subunit to be disassembled.

Animals↗