Description of Vibrio alginolyticus infection in cultured Sepia officinalis, Sepia apama, and Sepia pharaonis.
Explore the source record for details and available documents.
Animals↗
SEARCH · PubMed Health
Results for “Sepia”
Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.
Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.
1H NMR spectroscopic characterization of solutions of Sepia melanin, Sepia melanin free acid and human hair melanin.
A 1H nuclear magnetic resonance study of Sepia melanin, Sepia melanin free acid (Sepia MFA) and human hair melanin was carried out in deuterium oxide solution at pH 10-11. The empirical formula of Sepia MFA was calculated and used to estimate the number of protons in the aromatic region of the Sepia MFA polymeric chain and to suggest a possible monomeric unit profile.
Animals↗
Is there evidence for a cGMP-gated cation channel in the photosensory membrane of Sepia? Re publication: 'Evidence for a cGMP gated cation channel in photoreceptor cell membranes of Sepia officinalis'.
Explore the source record for details and available documents.
Animals↗
Photoprotection of human retinal pigment epithelium cells against blue light-induced apoptosis by melanin free radicals from Sepia officinalis.
Cultured retinal pigment epithelium (RPE) cells can phagocytize large foreign particles. Heterogeneous melanin aggregates from Sepia officinalis, a species of cuttlefish, were fed to cultured human RPE cells to produce cells laden with Sepia melanin. Blue light-induced apoptosis (BLIA) assays were performed by flow cytometry on parallel cultures consisting of RPE cells isolated from independent eyes and evenly divided into two cultures, one fed Sepia melanin and one containing only native melanin. After culturing and growth of the cells under blue light illumination for 7 days, the apoptosis percentage of all cultures indicated that Sepia feeding significantly reduced BLIA. To account for Sepia photoprotection, continuous-wave EPR and time-resolved EPR experiments were performed with parallel RPE cultures by using UV (355 nm) and green (532 nm) laser irradiation. Continuous-wave EPR spectra prove that the concentrations of intrinsic and extrinsic melanin free radicals in the Sepia-RPE culture are large compared with those concentrations in the RPE culture. Time-resolved EPR spectra indicate that both UV and green light produced extrinsic melanin radicals as radical pairs from the triplet manifold with a linear dependence on the number of photons per second. These experiments conclusively demonstrate that decreased RPE susceptibility to BLIA correlates with increased intracellular melanin free radical concentrations and that nonnative melanin can supplement native melanin photoprotection of RPE cells.
Animals↗
Similarities between G-proteins in visual cells of Sepia and cattle.
In contrast to antisera against native transducin a polyclonal antiserum raised against heat-denatured bovine transducin crossreacts with the G-protein from Sepia visual cells. This antiserum recognizes a 44 kDa (G alpha) and a 36 kDa (G beta) protein band from Sepia photosensory membrane preparation. Furthermore we purified the antibody-binding G-protein from Sepia by binding it to light-activated rhodopsin of Sepia and GTP-induced extraction, similar to the purification of bovine transducin. This G-protein is probably involved in the phototransduction process. The purified Sepia G-protein did bind to vertebrate photosensoric membrane upon illumination, but was not eluted by GTP-containing buffer solution. After extensive bleaching, the G-protein became soluble.
Animals↗
Electron microscopic studies of various cells in the alveolar wall of mice with special reference to spheroid alveolar epithelial cells after intravenous injection of squid-ink (sepia-melanin) solution.
The effect of an intravenous injection of squid-ink (sepia-melanin) solution on adult mouse spheroid alveolar epithelial cells was observed by the electron microscope. Sepia-melanin particles were seen in all alveolar wall cells examined that seems to suggest the entrance of sepia-melanin particles into the spheroid alveolar epithlial cells from the alveolar blood capillary. In cases of large penetrations of sepia-melanin particles into spheroid alveolar epithelial cells, a greater increase was found in the intramitochondrial granules. In addition, the so-called inclusion body believed to be formed by the degeneration of mitochondria had very high electron density and its quantity was abundant. On the contrary, in cases where the quantity of sepia-melanin entrance into the spheroid alveolar epithelial cell was small, neither an increase of intramitochondrial granules, an increase of the electron density nor an increase in the quantity of specific inclusion body was found.
Animals↗
Hemocyanin and the branchial heart complex of Sepia officinalis: are the hemocytes involved in hemocyanin metabolism of coleoid cephalopods?
Cytobiological experiments using isotopic- and cytochemical-labeled Sepia hemocyanin as well as immunocytochemical localization of the respiratory pigment were carried out to investigate the function of the hemocytes in hemocyanin metabolism of the common cuttlefish Sepia officinalis. For comparison, the rhogocytes (ovoid cells) of the branchial heart complex were included in this study. Hemocyanin molecules were immunocytochemically detected in the lysosomal compartment of the rhogocytes and, at lower levels, in adhesive and circulating hemocytes. (125)I-labeled Sepia hemocyanin was taken up by the rhogocytes only, whereas gold- and/or fluorescein-labeled Sepia hemocyanin was solely taken up by the adhesive and the circulating hemocytes, even though the level of uptake is different. There are also differences in the uptake of pure gold particles and/or fluorescein between rhogocytes and hemocytes. These findings give evidence that circulating and adhesive hemocytes of the branchial heart complex are not involved in hemocyanin turnover, but are a component of the cellular defense and detoxification system of adult coleoid cephalopods.
Animals↗
Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase.
The melanin-free ink of the cephalopod Sepia officinalis is shown to contain a heat labile proteinaceous component toxic to a variety of cell lines, including PC12 cells. Gel filtration chromatography indicated that the toxic component was concentrated in those fractions eluted at a molecular weight higher than 100 kDa and exhibiting the highest tyrosinase activity. SDS-PAGE analysis of the active fractions displayed a single major band migrating at an approximate molecular weight of 100 kDa, identical with that of the single tyrosinase band in the melanin-free ink. These data unambiguously demonstrated the identity of the toxic component with tyrosinase. Treatment of purified Sepia as well as of mushroom tyrosinase with an immobilized version of proteinase K resulted in a parallel loss of tyrosinase activity and cytotoxicity. Sepia apotyrosinase was ineffective in inducing cytotoxicity in PC12 cells. Purified Sepia tyrosinase was found to induce a significant increase in caspase 3 activity in PC12 cells, leading eventually to an irreversible apoptotic process. Overall, these results disclose a hitherto unrecognized property of tyrosinase that may lead to a reappraisal of its biological significance beyond that of a mere pigment producing enzyme.
Animals↗
Electrophoretic and immunochemical study of collagens from Sepia officinalis cartilage.
Electrophoretic and Western blot studies were conducted on collagen fractions extracted from Sepia officinalis (cuttlefish) cartilage using a modified salt precipitation method developed for the isolation of vertebrate collagens. The antibodies used had been raised in rabbit against the following types of collagen: Sepia I-like; fish I; human I; chicken I, II, and IX; rat V; and calf IX and XI. The main finding was that various types of collagen are present in Sepia cartilage, as they are in vertebrate hyaline cartilage. However, the main component of Sepia cartilage is a heterochain collagen similar to vertebrate type I, and this is associated with minor forms similar to type V/XI and type IX. The cephalopod type I-like heterochain collagen can be considered a first step toward the evolutionary development of a collagen analogous to the typical collagen of vertebrate cartilage (type II homochain). The type V/XI collagen present in molluscs, and indeed all phyla from the Porifera upwards, may represent an ancestral collagen molecule conserved relatively unchanged throughout evolution. Type IX-like collagen seems to be essential for the formation of cartilaginous tissue.
Animals↗
The effect of preparation procedures on the morphology of melanin from the ink sac of Sepia officinalis.
The structure of melanin extracted from the ink sac of the cuttlefish Sepia officinalis was examined for different methods of isolation and purification of the pigment. Scanning electron microscopy (SEM) images of Sepia eumelanin prepared by different procedures establish that multi-microm-sized aggregates reported by previous workers are generated by their sample preparation, and that the dominant constituents of Sepia melanin are approximately 150 nm spherical granules. Brunauer-Emmett-Teller (BET) measurements reveal that Sepia eumelanin from Sigma (prepared by spray drying the pigment) has a surface area of 14.3 m2/g. Pigment extracted directly from the fresh ink sac and then freeze-dried has a surface area of 21.5 m2/g, while CO2-supercritically dried has a surface area of 37.5 m2/g. This is consistent with SEM images showing that the process of freeze-drying produces aggregates, but to a lesser extent than spray drying. Supercritical drying of the sample produces suspensions of the individual approximately 150 nm granule, which is more reflective of the natural pigment. Brunauer-Emmett-Teller surface area analysis and Barrett-Joyner-Halenda (BJH) pore volume analysis indicate that the surface of the granules is not smooth and the interior of the granules is not porous, but rather the aggregates of granules are porous. Ultra-high resolution SEM and atomic force microscopy (AFM) images show the granules are easily deformed and are comprised of smaller constituents. De-aggregation of the granules by sonication and ultra-filtration reveal a range of structures depending on the pore size of the membrane used. The implications of these results on quantifying photochemical properties and kinetic reaction rate constants of melanin are discussed.
Animals↗
Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the omega class glutathione S-transferases.
The eye colour mutant sepia (se1) is defective in PDA {6-acetyl-2-amino-3,7,8,9-tetrahydro-4H-pyrimido[4,5-b]-[1,4]diazepin-4-one or pyrimidodiazepine} synthase involved in the conversion of 6-PTP (2-amino-4-oxo-6-pyruvoyl-5,6,7,8-tetrahydropteridine; also known as 6-pyruvoyltetrahydropterin) into PDA, a key intermediate in drosopterin biosynthesis. However, the identity of the gene encoding this enzyme, as well as its molecular properties, have not yet been established. Here, we identify and characterize the gene encoding PDA synthase and show that it is the structural gene for sepia. Based on previously reported information [Wiederrecht, Paton and Brown (1984) J. Biol. Chem. 259, 2195-2200; Wiederrecht and Brown (1984) J. Biol. Chem. 259, 14121-14127; Andres (1945) Drosoph. Inf. Serv. 19, 45; Ingham, Pinchin, Howard and Ish-Horowicz (1985) Genetics 111, 463-486; Howard, Ingham and Rushlow (1988) Genes Dev. 2, 1037-1046], we isolated five candidate genes predicted to encode GSTs (glutathione S-transferases) from the presumed sepia locus (region 66D5 on chromosome 3L). All cloned and expressed candidates exhibited relatively high thiol transferase and dehydroascorbate reductase activities and low activity towards 1-chloro-2,4-dinitrobenzene, characteristic of Omega class GSTs, whereas only CG6781 catalysed the synthesis of PDA in vitro. The molecular mass of recombinant CG6781 was estimated to be 28 kDa by SDS/PAGE and 56 kDa by gel filtration, indicating that it is a homodimer under native conditions. Sequencing of the genomic region spanning CG6781 revealed that the se1 allele has a frameshift mutation from 'AAGAA' to 'GTG' at nt 190-194, and that this generates a premature stop codon. Expression of the CG6781 open reading frame in an se1 background rescued the eye colour defect as well as PDA synthase activity and drosopterins content. The extent of rescue was dependent on the dosage of transgenic CG6781. In conclusion, we have discovered a new catalytic activity for an Omega class GST and that CG6781 is the structural gene for sepia which encodes PDA synthase.
Amino Acid Sequence↗
Subcellular localization and function of melanogenic enzymes in the ink gland of Sepia officinalis.
The ink gland of the cuttlefish Sepia officinalis has traditionally been regarded as a convenient model system for investigating melanogenesis. This gland has been shown to contain a variety of melanogenic enzymes including tyrosinase, a dopachrome-rearranging enzyme and peroxidase. However, whether and to what extent these enzymes co-localize in the melanogenic compartments and interact is an open question. Using polyclonal antibodies that recognize the corresponding Sepia proteins, we have been able to demonstrate that peroxidase has a different subcellular localization pattern from tyrosinase and dopachrome-rearranging enzyme. Whereas peroxidase is located in the rough endoplasmic reticulum and in the matrix of premelanosomes and melanosomes, tyrosinase and dopachrome-rearranging enzyme are present in the rough endoplasmic reticulum-Golgi transport system, at the level of trans-Golgi cisternae, trans-Golgi network and coated vesicles, and in melanosomes on pigmented granules. These results fill a longstanding gap in our knowledge of the melanin-producing system in Sepia and provide the necessary background for dissection at the molecular level of the complex interaction between melanogenic enzymes. Moreover, the peculiar and complex organization of melanin in an invertebrate such as Sepia officinalis is surprising and could provide the basis for understanding the process in more evolved systems such as that of mammals.
Animals↗
New insights into the physicochemical effects of ammonia/peroxide bleaching of hair and Sepia melanins.
Chemically unaltered melanosomes from black hair were isolated using a mild enzymatic procedure reported by Novellino et al. involving sequential treatment of a homogenized hair sample with different protease enzymes. Time-dependent fluorescence studies show, under identical conditions, that the rate of bleaching upon NH3/H2O2 treatment of hair melanosomes is twice that of Sepia melanosomes. The structure and morphology of hair melanosomes are compared to Sepia eumelanin using ESEM and TEM imaging studies. Black hair melanosomes are aggregates of rice-shaped ellipsoidal particles (0.8-1.0 microm in length and 0.2-0.6 microm in width) surrounded by an amorphous material suspected to be made of non-proteinacious materials. Sepia eumelanin aggregates are larger (2-5 microm) particles with a "doughnut" shape comprised of 100-150-nm spherical particles. Time-dependent TEM imaging studies of ammonia-treated (pH 10) hair melanosomes showed an initial breakdown of melanosomal aggregates followed by rupture of the melanosomal membrane, releasing melanin nanoparticles and leaving a ghost membrane behind. After prolonged treatment with aqueous NH3, a total loss of characteristic melanosome morphology was observed leading to an amorphous material. By contrast, Sepia melanosomes under identical conditions of ammonia treatment did not show such changes, probably due to different surface properties and aggregation behavior. Sodium hydroxide or sodium carbonate at identical pH did not show similar changes to ammonia, suggesting that the changes are not merely due to alkaline pH, but, rather, are specific to ammonia. Co-treatment with ammonia and peroxide induced a faster disintegration of the melanosomes, resulting in a complete dissolution and discoloration of melanin in 30 minutes. The data suggest that ammonia helps to release melanin nanoparticles out of melanosomes, making them more susceptible to oxidative attack by H2O2.
Ammonia↗
Mating success of wild type and sepia mutants Drosophila melanogaster in different choice.
Mating behaviour of red-eyed (wt) and brown-eyed (sepia) Drosophila melanogaster was studied under light conditions. Mating success was directly observed in mating vials and techniques usually applied in the studies of sexual selection ("female choice" and "multiple choice"). The comparison of sexual activity of mutant and wild types clearly indicates that they are not equally successful in matings. Sepia eye colour mutation decreases sexual activity of Drosophila melanogaster males, influences the preference ability of females and decreases the number of progeny from homogamic mating of the se x se type, as well as from heterogamic copulations in which sepia females take part. Non-random mating of wild type males and sepia females (in "multiple-choice" situation), with genetically and phenotypically different individuals, could be another mechanism for conservation of genetic polymorphism in natural populations.
Animals↗
[Cytological study of the post-embryonic development of the digestive gland of Sepia officinalis L. Mollusca : Cephalopoda (author's transl)].
A histological and ultrastructural study of the development of the digestive gland of Sepia officinalis L. was carried out on young Sepia reared in the laboratory, during the first month of post-embryonic life. The increasing complexity of the histological structure of the gland is related to the successive appearance of several cell types : immature cell, synthetizing cell, mature digestive cell ("cellule à boules"), and resting cell. These types are, in fact, just the evolutive stages of the same cell, the digestive cell. The sequence of appearance of the different cell types and the changes occurring in feeding can be used to define three stages in the post-embryonic development of the Sepia officinalis L. digestive gland : a multiplication stage (from hatching to the 5th day), a maturation stage (5th to 30th day), and adult stage (after the first month of post-embryonic life). These stages are identical to the three periods previously described by Richard and Decleir (1969) in the life of Sepia.
Animals↗
Roles of glutamate and FMRFamide-related peptides at the chromatophore neuromuscular junction in the cuttlefish, Sepia officinalis.
Body patterning behavior, the expression of highly intricate patterns, is ubiquitous among all unshelled cephalopods. These body patterns are in part generated by the coordinated activity of millions of skin chromatophore organs, each of which is regulated by a set of chromatophore muscles directly innervated by centrally located chromatophore motoneurons. This study addresses the question of the identity and function of the transmitter(s) at the chromatophore neuromuscular junction (NMJ) in the European cuttlefish Sepia officinalis. Glutamate application causes a rapid contraction of the chromatophore muscles, resulting in chromatophore expansion. Pharmacological studies demonstrate that the chromatophore muscles contain receptors blocked by glutamate-specific antagonists. Glutamate-like immunoreactivity is also present in the somata of putative chromatophore motoneurons. These findings suggest that glutamate likely acts as a neurotransmitter at the chromatophore NMJ. Evidence is also presented suggesting that FMRFamide-related peptides (FaRPs) also function as neurotransmitters at the Sepia chromatophore NMJ. FMRFamide application causes contraction of chromatophore muscles; however, the FMRFamide effect is slower and longer lasting than that of glutamate. Pharmacological data show that FMRFamide acts directly on the chromatophore muscles. FMRFamide-immunopositive cells are present in the posterior chromatophore lobe, the putative location of the chromatophore motoneuron somata. A combination of immunocytochemistry and in situ hybridization shows that some putative chromatophore motoneurons express FaRP-like immunoreactivity and an FaRP-coding mRNA transcript. Many FMRFamide-immunopositive cells in the posterior chromatophore lobes also express glutamate-like immunoreactivity. We conclude that glutamate and FaRPs likely function as fast and slow transmitters, respectively, at the Sepia chromatophore NMJ.
Animals↗
Fine structure of the blood-brain interface in the cuttlefish Sepia officinalis (Mollusca, Cephalopoda).
The blood-brain interface was studied in a cephalopod mollusc, the cuttlefish Sepia officinalis, by thin-section electron microscopy. Layers lining blood vessels in the optic and vertical lobes of the brain, counting from lumen outwards, include a layer of endothelial cells and associated basal lamina, a layer of pericytes and a second basal lamina, and perivascular glial cells. The distinction between endothelial cells and pericytes breaks down in small vessels. In the smallest microvessels, equivalent to capillaries, and in venous channels, and endothelial and pericyte layers are discontinuous, but a layer of glial cells is always interposed between blood and neural tissue, except where neurosecretory endings reach the second basal lamina. In microvessels in which cell membranes of the entire perivascular glial sheath could be followed, the glial layer was apparently 'seamless', not interrupted by an intercellular cleft, in ca 90% (27/30) of the profiles. Where a cleft did occur, it showed an elongated overlap zone between adjacent cells. The walls of venous channels are formed by lamellae of overlapping glial processes. In arterial vessels, the pericyte layer is thicker and more complete, with characteristic sinuous intercellular clefts. Arterioles are defined as vessels containing 'myofilaments' within pericytes, and arteries those in which the region of the second basal lamina is additionally expanded into a wide collagenous zone containing fibroblast-like cells and cell processes enclosing myofilaments. The 'glio-vascular channels' observed in Octopus brain are not a prominent feature of Sepia optic and vertical lobe. The organization of cell layers at the Sepia blood-brain interface suggests that it is designed to restrict permeability between blood and brain.
Animals↗
Cytobiological studies on hemocyanin metabolism in the branchial heart complex of the common cuttlefish Sepia officinalis (Cephalopoda, Dibranchiata).
The present study confirms previous investigations that demonstrated a high copper content in the branchial heart and its appendage, and that gave the first indication that this organ complex might be involved in hemocyanin metabolism in Sepia officinalis L. Immunocytochemical localization of hemocyanin molecules within the endocytotic lysosomal system of the ovoid cells and tracer experiments with 125I-labeled Sepia hemocyanin suggest its endocytotic uptake. Energy-dispersive X-ray microanalysis and histochemical methods reveal a high copper content within the ovoid cells of the branchial heart. In view of the turnover of the respiratory pigment in the branchial heart of Sepia officinalis L., we believe that the ovoid cells are a site of hemocyanin catabolism.
Animals↗