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PubMed2004

Analysis of radiation-induced hydrocarbons and 2-alkylcyclobutanones from dried shrimps (Penaeus aztecus).

We investigated the usefulness of hydrocarbons and 2-alkylcyclobutanones as markers for irradiated, dried shrimps. A method was developed to detect the irradiation of dried shrimps (Penaeus aztecus) by identifying radiation-induced hydrocarbons and 2-alkylcyclobutanones extracted from dried shrimps, which were separated by Florisil column chromatography and identified by a method using gas chromatography/mass spectrometry. Radiation-induced hydrocarbons and 2-alkylcyclobutanones are formed from the fatty acids of the irradiated fats. The quantity of the hydrocarbons and 2-alkylcyclobutanones formed from some fatty acids is related to the composition of fatty acids in a sample. The concentrations of hydrocarbons and 2-alkylcyclobutanones increased with radiation dose. The major hydrocarbons in the irradiated, dried shrimps were 1-tetradecene and pentadecane from palmitic acid; small amounts of heptadecane and 1-hexadecene from stearic acid; and 8-heptadecene and 1,7-hexadecadiene from oleic acid. 2-(5'-Tetradecenyl)cyclobutanone, one of the 2-alkylcyclobutanones, was present at the highest concentration. The radiation-induced hydrocarbons and 2-alkylcyclobutanones were detected at radiation doses of 0.5 kGy and greater. These compounds were not detected in nonirradiated, dried shrimps.

Animals↗

PubMed2005

Salmonella and the sanitary quality of aquacultured shrimp.

In this study, we examined the prevalence of Salmonella and coliform bacteria on shrimp aquaculture farms to develop guidelines or preventative measures for reducing Salmonella and fecal contamination on products harvested from these farms. The U.S. Food and Drug Administration, in conjunction with foreign government regulatory agencies, the aquaculture industry, and academia affiliates, analyzed 1,234 samples from 103 shrimp aquaculture farms representing six countries between July 2001 and June 2003 for fecal coliforms, Escherichia coli, and Salmonella. A significant relationship was found (P = 0.0342) between the log number of fecal bacteria and the probability that any given sample would contain Salmonella. The likelihood of any given sample containing Salmonella was increased by 1.2 times with each 10-fold increase in either fecal coliform or E. coli concentration. The statistical relationship between Salmonella concentration and that of both fecal coliforms and E. coli was highest in grow-out pond water (P = 0.0042 for fecal coliforms and P = 0.0021 for E. coli). The likelihood of finding Salmonella in grow-out pond water increased 2.7 times with each log unit increase in fecal coliform concentration and 3.0 times with each log unit increase in E. coli concentration. Salmonella is not part of the natural flora of the shrimp culture environment nor is it inherently present in shrimp grow-out ponds. The occurrence of Salmonella bacteria in shrimp from aquaculture operations is related to the concentration of fecal bacteria in the source and grow-out pond water.

Animals↗

PubMed1992

Scanning electron microscope observations of brine shrimp larvae from space shuttle experiments.

Brine shrimp are encysted as gastrula stage embryos, and may remain dehydrated and encysted for years without compromising their viability. This aspect of brine shrimp biology is desirable for studying development of animals during space shuttle flight, as cysts placed aboard a spacecraft may be rehydrated at the convenience of an astronaut, guaranteeing that subsequent brine shrimp development occurs only on orbit and not on the pad during launch delays. Brine shrimp cysts placed in 5 ml syringes were rehydrated with salt water and hatched during a 9 day space shuttle mission. Subsequent larvae developed to the 8th larval stage in the sealed syringes. We studied the morphogenesis of the brine shrimp larvae and found the larvae from the space shuttle experiments similar in rate of growth and extent of development, to larvae grown in sealed syringes on the ground. Extensive differentiation and development of embryos and larvae can occur in a microgravity environment.

Animals↗

PubMedDate not supplied

[Cholesterol oxidation products in fresh and frozen shrimps, raw and grilled].

Cholesterol oxidation products (COPs) have been related to different toxic effects, being the atherosclerotic process one of the best known. The presence of cholesterol oxides in freshly and frozenly commercialised shrimps, both raw and grilled, was studied. The determination was made by gas chromatography-mass spectrometry (GCMS). Fresh shrimps showed significant amounts of all analysed COPs, except for 7alpha-hydroxycholesterol, accounting in total for 33.15 microg COPs/g fat. In contrast, in frozen commercialised shrimps only 7-ketocholesterol and 7beta-hydroxycholesterol were detected. These results point out the great effectiveness of the commercialisation of this type of products under freezing, in terms of to the minimisation of the COPs formation. The cooking method (grilling) increased the COPs content in both types of shrimps, reaching 55.43 microg COPs/g fat in fresh shrimps and only 13.06 microg COPs/g fat in frozen ones.

Animals↗

PubMed2006

Shrimps survive white spot syndrome virus challenge following treatment with Vibrio bacterin.

Taking an innovative approach, a vaccination study using five bacterial strains viz. Vibrio campbelli (B60), V. alginolyticus (B73), V. parahaemolyticus-like (B79), V. parahaemolyticus (R8) and V. harveyi (RG203) was conducted in Penaeus monodon against white spot syndrome virus (WSSV) infection, considered as one of the serious pathogens of shrimps. Oral challenge with shrimps infected with WSSV showed a relative percentage survival of 5 and 47% in the P. monodon juveniles vaccinated with V. parahaemolyticus and V. harveyi, respectively. Results showed that there is a possibility of specifically immunising the shrimps against WSSV using bacterin prepared out of Vibrio harveyi isolates taken from shrimps infected with WSSV. Also, there was a level of protection attained by the shrimps due to immunisation with Vibrio strains.

Animals↗

PubMed2006

Mantis shrimp allergy.

We report the case of a 25-year-old female who experienced two immediate episodes of labial, lingual and larynx angiodema after eating fried mantis shrimp (Squilla empusa), a crustacean belonging to the Squillidae family, and a third episode after eating shellfish pudding. Prick by prick tests to mantis shrimp and to other crustacean were positive. Serum specific IgE showed higher values than 0.35 kU/L to extracts from mantis shrimp shell, prawn, large prawn and crab. Serum specific IgE against large prawn tropomyosin were below 0.35 kU/L. Sodium dodecyl sulfate polyacrylamide gel electropheresis (SDS-PAGE) immunoblotting results with raw mantis shrimp shell revealed IgE-binding bands of 46 kDa and 25 kDa, in non reducing and reducing conditions, respectively. Cross-reactivity studies using the enzyme allergo sorbent test (EAST)-inhibition and Immunoblotting-inhibition methods showed the existence of significant cross-reactivity between the IgE-binding proteins present in mantis shrimp and those from prawn, large prawn and small crab.

Adult↗

PubMed1989

Yeasts associated with the white shrimp Penaeus schmitti, sediment, and water of Sepetiba Bay, Rio de Janeiro, Brasil.

Samples were collected in a polluted site with mean fecal coliform counts of the water being 9.0 x 10(2)/100 ml and less polluted areas including commercial fishing areas with fecal coliforms typically below 2.0 x 10(1)/100 ml. Yeast populations from the polluted site were 4.6 x 10(2) to 9.2 x 10(3)/g of shrimp intestine, 1.0 x 10(1) to 2.4 x 10(2)/g of sediment and 4.0 x 10(-1) to 4.6 x 10(1)/ml of water, and in the less polluted site 3.0 x 10(1) to 2.3 x 10(2)/g of intestines and 3.0 x 10(-1) to 2.4 x 10(1)/ml of water. About half of these yeast populations were fermentative. Prevalent yeasts isolated from shrimp were Candida famata, Candida intermedia, Candida tropicalis, Candida krusei, Geotrichum sp., Trichosporon sp., Debaryomyces hansenii, Rhodotorula rubra, Kloeckera apiculata, Cryptococcus sp., Hansenula anomala, and Candida spp. The species found in water and sediment were similar to those of shrimp except that C. tropicalis was more prevalent in sediment with 25% of the population and D. hansenii in water with 12%. Yeasts normally associated with warm blooded animals and sewage were predominant in the shrimp from the polluted site, but yeasts from the less polluted site were more typical of clean water. Yeasts were concentrated in the shrimp intestine suggesting that this is a favorable environment for them but no species were found to be selectively associated with this niche.

Animals↗

PubMed1996

Effect of tadpole shrimp, Triops longicaudatus, (Notostraca: Triopsidae), on the efficacy of the microbial control agent Bacillus thuringiensis var. israelensis in experimental microcosms.

Laboratory bioassays using Culex quinquefasciatus larvae evaluated the effect of tadpole shrimp on the persistence of Bacillus thuringiensis var. israelensis (B.t.i.) in water collected from the surface of field microcosms. Time elapsed since B.t.i. treatment, as well as presence or absence of soil and tadpole shrimp, affected B.t.i. persistence at the water surface in 15- and 30-cm total depths. The presence of tadpole shrimp slowed the natural decline in B.t.i. effectiveness over time, but this effect was depressed when soil was present. Tadpole shrimp foraged throughout the water column and stirred up the substrate, keeping more particles in suspension at the surface than in microcosms with no shrimp, in microcosms with water depths of 15 and 30 cm.

Animals↗

PubMed2026

Intestinal content accelerates muscle protein degradation in red shrimp (Solenocera crassicornis) during refrigeration: Insights from metagenomics and metabolomics.

This study systematically explored the effects of intestinal components on muscle quality deterioration and protein degradation of red shrimp during refrigerated storage. The results demonstrated that refrigeration induced continuous quality degradation and muscle protein breakdown in red shrimp, whereas eliminating intestinal tissues effectively retarded muscle spoilage and protein degradation, and optimized muscle texture. The intestinal microorganisms could secrete extracellular proteases to promote muscle protein degradation were primarily Vibrio, Bacillus, Pseudomonas, Photobacterium, and Shewanella. These microorganisms promote protein degradation by secreting zinc proteases, serine proteases, and aspartyl proteases. This study elucidates the molecular mechanisms of intestinal microbial metabolism influences the muscle protein degradation of red shrimp during refrigeration. The findings provide a theoretical foundation for precise regulation of intestinal-targeted microorganisms, thereby maintaining optimal quality of shrimps during refrigeration.

Animals↗

PubMed2000

Disrupting the geranylgeranylation at the C-termini of the shrimp Ras by depriving guanine nucleotide binding at the N-terminal.

In order to assess the effects of guanine nucleotide binding on the geranylgeranylation at the CAAX box of the shrimp Ras, we experimented with the shrimp Penaeus japonicus Ras (S-Ras) which is geranylgeranylated at the C-termini, shares 85% homology with mammalian K(B)-Ras protein and demonstrates identity in the guanine nucleotide binding domains (Huang C-F, Chuang N-N. 1999. J Exp Zool 283:510-521). Several point mutations in the S-ras gene were generated at codons 12 (G12V), 61 (Q61K), and 116 (N116I). The bacterially expressed mutant S-Ras proteins, G12V and Q61K, were bound with GTP without hydrolysis. In contrast, the mutant S-Ras N116I was defective in its ability to bind any guanine nucleotides. Autoradiography studies showed that the purified shrimp protein geranylgeranyltransferase I (Lin R-S, Chuang N-N. 1998. J Exp Zool 281:565-573) was unable to catalyze the transfer of [(3)H]-geranylgeranylpyrophosphate to this mutant N116I but very competently caused the geranylgeranylation of GTP-locked mutants, G12V and Q61K. These results demonstrate that the geranylgeranylation at the CAAX box of the shrimp Ras protein requires the proper binding of guanine nucleotide at its N-terminal region. J. Exp. Zool. 286:441-449, 2000.

Alkyl and Aryl Transferases↗

PubMed2002

Complete mitochondrial DNA sequence of a tadpole shrimp (Triops cancriformis) and analysis of museum samples.

The complete mitochondrial DNA (mtNDA) of the tadpole shrimp Triops cancriformis was sequenced. The sequence consisted of 15,101 bp with an A+T content of 69%. Its gene arrangement was identical with those sequences of the water flea (Daphnia pulex) and giant tiger prawn (Penaeus monodon), whereas it differed from that of the brine shrimp (Artemia franciscana) in the arrangement of its genes for tRNAs. Phylogenetic analysis revealed T. cancriformis to be more closely related to the water flea than to the brine shrimp and giant tiger prawn. We also compared the 16S rRNA sequences of five formalin-fixed tadpole shrimps that had been collected in five different locations and stored in a museum. The sequence divergence was in the range of 0-1.51%, suggesting that those samples were closely related to each other.

Animals↗

PubMed2004

A mu-class glutathione S-transferase from the marine shrimp Litopenaeus vannamei: molecular cloning and active-site structural modeling.

A cDNA clone coding for a mu-class glutathione S-transferase (GST) was isolated from a hepatopancreas cDNA library from the shrimp Litopenaeus vannamei. The deduced amino acid sequence (215 amino acids) has >50% identity to rodents and other mammals mu-class GSTs. Using RT-PCR, the shrimp GST transcript was detected in hepatopancreas, hemocytes, gills, and muscle, but not in pleopods. The shrimp GST sequence was computer modeled and found to fit the classical two-domain GST structure. Domain I, containing the glutathione (GSH) binding site, is more conserved compared to the flexible C-terminal domain II. Residue Q208 appears to be a key to substrate specificity by comparison with mammalian GST mutants. This position is commonly occupied by serine or threonine in mammalian mu-class GSTs, and shrimp Q208 may affect the affinity to substrates like aminochrome or 1,3-dimethyl-2-cyano-1-nitrosoguanidine. This is the first report of molecular cloning and structural modeling of a crustacean GST and provides new insights into the nature of the detoxification response on marine invertebrates.

Amino Acid Sequence↗

PubMed2002

Selective enhanced phosphorylation of shrimp beta-tubulin by PKC-delta with PEP(taxol), a synthetic peptide encoding the taxol binding region.

Beta-tubulin cDNA from the shrimp Penaeus japonicus was isolated by homology cloning. Expression of cDNA in Escherichia coli yielded a 55 kDa polypeptide, positive for monoclonal antibodies against mammalian beta-tubulin. Autoradiography demonstrated the bacterially expressed hepatopancreas beta-tubulin of P. japonicus is specifically phosphorylated by the delta isoenzyme of protein kinase C (PKC-delta) purified from the plasma membrane of the shrimp heart, in the presence of the receptor for activated PKC (RACK), but not in its absence. Purified shrimp heart PKC-delta is able to phosphorylate bacterially expressed shrimp beta-tubulin without the presence of Ca(++), but requires Mg(++). The kinase activity of purified PKC-delta on bacterially expressed beta-tubulin was enhanced by incubation with PEP(taxol), a synthetic peptide encoding the taxol-binding region of beta-tubulin. In other words, PEP(taxol) modulates the kinase activity of PKC-delta through RACK.

Amino Acid Sequence↗

PubMed2001

Disrupting the transforming activity of shrimp ras(Q(61)K) by deleting the CAAX box at the C-terminus.

BALB/3T3 cells were transformed by transfection with DNA encoding the mutated ras(Q(61)K) from shrimp Penaeus japonicus. Ras transcription and protein levels had increased significantly in the cells transfected with the S-ras plasmid, compared to cells transfected with a control plasmid pcDNA3.1. The bacterially expressed GTP-locked S-Ras(Q(61)K) is successfully prenylated by rat protein geranylgeranyltransferase I (PGGTase I) and then polymerized with tubulin, in agreement with findings for GTP-locked mammalian K(B)-Ras(Q(61)K) in vitro. Shrimp protein farnesyltransferase (PFTase) of shrimp did not prenylate the GTP-locked shrimp S-Ras(Q(61)K) (Lin and Chuang. 1998. J Exp Zool 281:565-573), whereas rat PFTase efficiently catalyzed the farnesylation of GTP-locked S-Ras(Q(61)K). To investigate the effect of geranylgeranylation on cellular transformation, we generated S-ras(Q(61)K) mutants with deletion of the CAAX box [S-ras(Q(61)K)(-caax)] or replacement of the CAAX box [S-ras(Q(61)K)(Kcaax)] or replacement of the arginine-rich domain [S-ras(Q(61)K)(K-Lys)] with corresponding sequences from rat K(B)-ras(Q(61)K). BALB/3T3 cells transfected with DNA encoding S-ras(Q(61)K), S-ras(Q(61)K)(KCAAX), S-ras(Q(61)K)(K-Lys) were transformed successfully, but S-ras(Q(61)K)(-CAAX) was defective in its ability to transform. Thus, prenylation at CAAX is required for transformation. Either the geranylgeranylated or the farnesylated S-Ras(Q(61)K) was endowed with abilities to transform. The arginine-rich region in S-Ras or the lysine-rich clusters from the rat K(B)-Ras appear not essential for activity to transform.

3T3 Cells↗

PubMed2004

Molecular characterization of a cDNA encoding vitellogenin in the coonstriped shrimp, Pandalus hypsinotus and site of vitellogenin mRNA expression.

In order to determine the primary structure of vitellogenin in a protandric species, the coonstriped shrimp Pandalus hypsinotus, we previously purified four vitellin components (designated as VnA, VnB, VnC, and VnD, respectively), and chemically analyzed their partial amino acid sequences. In this study, we subsequently cloned a cDNA encoding vitellogenin in this species based on the N-terminal and internal amino acid sequences of VnA, as well as the N-terminal sequence of VnC. The open reading frame of this cDNA encoded a pro-vitellogenin in which vitellins were arranged as follows: NH2-VnA-VnB-VnC/D-COOH. The deduced amino acid sequence possessed a single consensus cleavage sequence, R-X-K/R-R, along the lines of vitellogenins reported in other crustaceans and insects, and the N-terminal sequence of VnB was immediately preceded by this sequence. The comparison of primary structures revealed the existence of a basic and characteristic structure for the vitellogenin molecule in decapod crustacean species, and phylogenetic analysis reflected the current taxonomic classifications of Crustacea. An approximately 8 kb-long transcript of the vitellogenin gene was detected in the hepatopancreas of female shrimps having a gonadosomatic index higher than 1.0 by Northern blot analysis, but was not observed in the hepatopancreas and gonads of male shrimps and the hepatopancreas of female shrimps having a gonadosomatic index lower than 1.0. These results indicate that the hepatopancreas is responsible for vitellogenin synthesis.

Amino Acid Sequence↗

PubMed1996

Characterization of hyperglycemic and molt-inhibiting activity from sinus glands of the penaeid shrimp Penaeus vannamei.

To design a homologous bioassay for the molt-inhibiting hormone and the crustacean hyperglycemic hormone of the shrimp Penaeus vannamei, the effect of sinus gland homogenate (SGh), in vitro, on ecdysteroid production by Y-organs (YOs), and the effect of the injection of SGh, in vivo, on the glycemia of shrimps have been investigated. Addition of SGh to incubation medium of shrimp YOs dose dependently reduced, within a few hours, ecdysteroid release into the medium. Moreover, inhibition by SGh decreases drastically in YOs from animals in late premolt stages, when there is maximal ecdysteroid production. Injection of SGh into shrimps evokes a hyperglycemic response maximal after 2 hr. Immunoadsorption of SGh with an anti-Homarus americanus cHHA antiserum inhibited both biological activities of the homogenate. After fractionation of acidic sinus gland extract by RP-HPLC, the maximal response in both bioassays was associated with the major UV absorbent peak, which was also the major immunoreactive peak when tested by ELISA with the anti-lobster cHHA. After a further purification step, the molecular mass of the bioactive and immunoreactive peptide was found to be 8627 +/- 0.3 Da by electrospray ionization mass spectrometry. The amino acid sequence of the first 38 residues of this peptide was established by gas-phase microsequencing. This sequence shows 55% homology with the first 38 residues of the lobster cHHA.

Amino Acid Sequence↗

PubMed1996

IgE and monoclonal antibody reactivities to the major shrimp allergen Pen a 1 (tropomyosin) and vertebrate tropomyosins.

Pen a 1, the major shrimp allergen from brown shrimp Penaeus aztecus has been identified as the muscle protein tropomyosin. To identify Pen a 1 IgE binding sites, the reactivities of Pen a 1-specific monoclonal antibodies (mAbs) and shrimp-allergic subjects' IgE to shrimp and homologous mammalian tropomyosins were analyzed. Pen a 1, purified by preparative SDS-PAGE and commercially obtained porcine, bovine and rabbit tropomyosin were cleaved by CNBr or digested by endoproteinases Lys-C, Glu-C, trypsin, Arg-C and chymotrypsin. Reactivities of Pen a 1-specific mAbs and IgE to the resulting peptides were analyzed by dot blot and immunoblotting. The dot blot analysis showed that mAbs and IgE antibodies did not react with any of the mammalian tropomyosins. The immunoblot analysis showed that all Pen a 1 digests bound IgE or mAbs. However, not all peptides in each digest possessed an IgE binding site. IgE binding intensity and frequency varied by subject and peptide digest. IgE and mAb reactivity patterns were similar but no mAb reproduced the IgE binding patterns indicating that subject' IgE bound some epitopes that were not recognized by the Pen a 1-specific mAbs. These studies suggest that IgE-binding epitopes are restricted to certain parts of the Pen a 1 molecule, Pen a 1 may have several similar epitopes, and that Pen a 1 epitopes do not appear to be located in the highly homologous parts of the tropomyosin molecule.

Allergens↗

PubMed2004

Comparative embryonic and larval developmental responses of estuarine shrimp (Palaemonetes pugio) to the juvenile hormone agonist fenoxycarb.

Grass shrimp (Palaemonetes pugio) were reared separately through both embryonic and total larval development during exposure to fenoxycarb at measured concentrations of <2.2 to 888 microg L(-1). A fenoxycarb concentration of 888 microg L(-1) significantly (p < 0.05) inhibited embryonic development to larval hatching and extended the embryonic developmental period from 11.9 to 12.7 days. Exposure to fenoxycarb concentrations < or = 502 microg L(-1) had no significant (p > 0.05) effect on complete embryonic development. Significantly fewer shrimp successfully metamorphosed to postlarvae when exposed through complete larval development to fenoxycarb concentrations > or = 4 microg L(-1). Larval development of grass shrimp was therefore >2 orders of magnitude more sensitive to this juvenile hormone agonist than was embryonic development. Viability of larvae developing in fenoxycarb was concentration dependent. Development beyond third zoeal stage was significantly inhibited at fenoxycarb concentrations > or = 190 microg L(-1), whereas development beyond fourth zoeal stage was inhibited by a concentration of > or = 45 microg L(-1). Fenoxycarb exposure of developing larvae did not alter either the duration of total larval development or the total number of larval stages before metamorphosis. Rearing of fenoxycarb-exposed embryos through larval development without further exposure had no significant effect on number of larval stages, larval development rate, or metamorphic success of larvae. Similarities in the sensitivity of grass shrimp larvae and mosquito larvae to fenoxycarb suggests that the use of a bioassay protocol measuring the metamorphic success of crustacean larvae would be a valuable adjunct to the hazard assessment of newly developed pesticides that target endocrine control of metamorphosis in insects and possibly other endocrine-disrupting xenobiotics as well.

Animals↗