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At least 199 records · Page 11Linked to original sources
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

Endocrine regulation of the phosphatidylinositol pathway in the Norway lobster, Nephrops norvegicus, and the shore crab, Carcinus maenas.

The present study examines the mode of action of eyestalk factors, in particular crustacean hyperglycaemic hormone (CHH), on known target tissues (muscle and hepatopancreas) in two decapod crustacean species, Nephrops norvegicus and Carcinus maenas. The possibility that receptors to CHH are coupled to an elevation of cytosolic Ca2+ derived from intracellular stores via activation of the phosphatidylinositol pathway was investigated. Using an inositol 1,4,5-trisphosphate (InsP3)-specific competitive binding assay, measurable levels of InsP3 were detected in hepatopancreas and muscle in both N. norvegicus and C. maenas. Incubation of these tissues in the presence of sinus gland extracts (two sinus gland equivalents) consistently increased InsP3. In addition, Carcinus CHH (10 nM) increased InsP3 levels in Carcinus hepatopancreas and muscle. Incubation of hepatopancreas from both species in 10 mM lithium saline increased basal levels of InsP3, suggesting a significant turnover of phosphoinositides in this tissue.

Animals↗
PubMed1997

Distribution and regulation of esterases that hydrolyze methyl farnesoate in Homarus americanus and other crustaceans.

Ester hydrolysis of methyl farnesoate (MF) by crustacean tissue homogenates was measured using the substrate [3H]MF in a radiochemical partition assay. Tissues were obtained from the lobster Homarus americanus, penaeid shrimp Sicyonia ingentis, thalanassid shrimp Callianassa californiensis, sand crab Emerita analoga, and spider crab Pugettia producta. The greatest specific activities were recovered from the hepatopancreas (239 to 11,500 pmol MF/min-mg total protein). Hepatopancreatic homogenates of C. californiensis were significantly more active than homogenates from the other species. In the lobster, esterases that hydrolyze MF were associated with lipid storage (R) cells of the hepatopancreas. Enzyme activity of lobster larval homogenates increased 1.5-fold during the second stage of development. The rate of MF hydrolysis by esterases extracted from the juvenile lobster hepatopancreas could not be correlated with molt stage or sex and was not significantly influenced by eyestalk ablation, mandibular organ ablation, or MF injection.

Animals↗
PubMed1997

Localization of a crustacean hyperglycemic hormone-like immunoreactivity in the neuroendocrine system of Euscorpius carpathicus (L.) (Scorpionida, Chactidae).

The neuroendocrine system of Euscorpius carpathicus was immunohistochemically localized using a polyclonal antiserum raised against a purified Homarus americanus crustacean hyperglycemic hormone (Hoa-cHHA). There were cross-reactions in E. carpathicus procerebral and subesophageal neurosecretory cells, neurohemal organs, and intra- and extraganglionic neurosecretory tracts. Among the neurohemal structures, the Kwartirnikov's organ, the Tropfenkomplex, and the coxal disc reacted strongly. In Euscorpius, the differing results between adults and juveniles suggest neurosecretory variations related to developmental stage. These immunohistochemical observations suggest the presence of substances related to the cHH in scorpions; however, in this heterologous system, it is not at present possible to assess physiological significance.

Animals↗
PubMed1998

Quantification of crustacean hyperglycemic hormone by ELISA in hemolymph of the lobster, Homarus americanus, following various stresses.

An ELISA was developed for the crustacean hyperglycemic hormone (CHH) from the lobster, Homarus americanus. It is sensitive to as little as 0.2 fmol of peptide. The assay was used to measure CHH in the hemolymph of intact lobsters after various environmental stresses. Increases in CHH were observed following emersion, exposure to high temperatures (23 degrees and 28 degreesC), and salinity stress (50 and 150% seawater). During emersion, concentrations of hemolymph glucose increased concomitantly with increases in CHH. Significant levels of hemolymph CHH were also measured in lobsters that had been eyestalk-ablated. These latter observations indicate that there may be a source of CHH other than the X-organ/sinus gland in the lobster.

Animals↗
PubMed2001

Carbohydrate dynamics and the crustacean hyperglycemic hormone (CHH): effects of parasitic infection in Norway lobsters (Nephrops norvegicus).

The effects of a dinoflagellate parasite (Hematodinium sp.) on carbohydrate metabolism were examined in the Norway lobster, Nephrops norvegicus. Five stages of infection were observed. These included uninfected (Stage 0), subpatently infected (SP), and patently infected (Stage 1-4) lobsters. During patent infection, the concentration of glucose in the hemolymph was reduced significantly from its value of 180 microg ml(-1) in uninfected (Stage 0) lobsters to 25.3 microg ml(-1) in Stage 3-4. These changes were accompanied by significantly lower levels of hepatopancreatic glycogen in lobsters at Stage 2 (2.01 mg g(-1)) and Stage 3-4 (0.84 mg g(-1)) of infection than in those at Stage 0 (16.19 mg g(-1)) and Stage 1 (14.71 mg g(-1)). Due to disruption of the normal feedback loops which control the release of crustacean hyperglycemic hormone (CHH), plasma concentrations increased with the severity of infection from 32.2 fmol ml(-1) in Stage 0 to 106.6 fmol ml(-1) in Stage 3-4. The increased CHH concentrations occurred concomitantly with reduced concentrations of plasma glucose and tissue glycogen. A significantly increased hemolymph CHH titer (107.7 fmol ml(-1)) was also observed during SP infection. It is concluded that the parasite places a heavy metabolic load on the host lobster.

Animal Diseases↗
PubMed2001

20-hydroxyecdysone causes increased aggressiveness in female American lobsters, Homarus americanus.

Lobsters become transiently more aggressive before ecdysis. This aggressiveness accompanies an increase in hemolymph titers of 20-hydroxyecdysone (20-HE). Combats between intermolt female lobsters, injected with premolt levels of 20-HE, and larger, saline-injected opponents were videotaped. Aggressive, defensive, and avoidance behaviors were ranked according to aggressiveness in a Rank of Aggression hierarchy, which included opponent-directed and (nonopponent) redirected behaviors. Treated animals performed more and more highly aggressive behaviors than saline-injected controls. Opponents of treated animals performed fewer aggressive behaviors than saline-injected control opponents. Controls performed more defensive behaviors than treated animals, when redirected behaviors were considered. Differences in avoidance behaviors among the four types of combatants were not significant. The total aggressive content was the same in treated and control fights, but the interactions between combatants in the two fights were significantly different. Treated animals were equally as aggressive and defensive as their opponents; controls were relatively less aggressive and more defensive than their opponents. These results correlate with molt-cycle variations in behavior, 20-HE titers, and the effects of 20-HE and molt-differentiated hemolymph on the claw opener muscle. They suggest that 20-HE orchestrates intrinsic, cellular, and nuclear events that produce the molt-cycle transformations in agonistic behavior and aggressive state of lobsters.

Aggression↗
PubMed1999

Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.

The structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor was determined in the presence of coenzyme NAD+ at 1.88 A resolution with a final R-factor of 0.175. The structure refinement was carried out on the basis of the structure of holo-GAPDH at 2.0 A resolution using the program XPLOR. The carboxymethyl group connected to Cys149 is stabilized by a hydrogen bond between its OZ1 and Cys149N, and charge interaction between the carboxyl group and the nicotinamide moiety. The modification of Cys149 induced conformational changes in the active site, in particular, the site of sulphate ion 501 (the proposed attacking inorganic phosphate ion in catalysis), and segment 208-218 nearby. Extensive hydrogen-bonding interactions occur in the active site, which contribute to the higher stability of the modified enzyme. The modification of the active site did not affect the conformation of GAPDH elsewhere, including the subunit interfaces. The structures of the green and red subunits in the asymmetric unit are nearly identical, suggesting that the half-site reactivity of this enzyme is from ligand-induced rather than pre-existing asymmetry. It is proposed that the carboxymethyl group takes the place of the acyl group of the reaction intermediate, and the catalytic mechanism of this enzyme is discussed in the light of a comparison of the structures of the native and the carboxymethylated GAPDH.

Animals↗
PubMed2001

Crystal structure of the Escherichia coli RNA degradosome component enolase.

The crystal structure of Escherichia coli enolase (EC 4.2.1.11, phosphopyruvate hydratase), which is a component of the RNA degradosome, has been determined at 2.5 A. There are four molecules in the asymmetric unit of the C2 cell, and in one of the molecules, flexible loops close onto the active site. This closure mimics the conformation of the substrate-bound intermediate. A comparison of the structure of the E. coli enolase with the eukaryotic enolase structures available (lobster and yeast) indicates a high degree of conservation of the hydrophobic core and the subunit interface of this homodimeric enzyme. The dimer interface is enriched in charged residues compared with other protein homodimers, which may explain our observations from analytical ultracentrifugation that dimerisation is affected by ionic strength. The putative role of enolase in the RNA degradosome is discussed; although it was not possible to ascribe a specific role to it, a structural role is possible.

Animals↗
PubMed2000

Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.

d-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) shows cooperative properties for binding coenzymes. The structure of apo-GAPDH from Palinurus versicolor has been solved at 2.0 A resolution by X-ray crystallography. The final model gives a crystallographic R factor of 0.178 in the resolution range 8 to 2 A. The structural comparison with holo-GAPDH from the same species reveals a conformational change induced by coenzyme binding similar to that observed in Bacillus stearothermophilus GAPDH but to a lesser extent. The differences in magnitude during the apo-holo transition between these two enzymes were analyzed with respect to the change of the amino acid composition in the coenzyme binding pocket. In the crystalline state of apo-GAPDH, the overall structures of the subunits are similar to each other; however, significant differences in temperature factors and minor differences in domain rotation upon coenzyme binding were observed for different subunits. These structural features are discussed in relation to the environmental asymmetry of crystallographically independent subunits.

Animals↗
PubMed2000

Chaotic or periodic variation? Looking at Crustacea hearts.

A simple relationship between the burst length of the trigger neurons of the Crustacea cardiac ganglion and the length of the heartbeat, is shown to lead to chaotic heart rate. Interestingly, the same type of relationship is also capable of generating complex periodic deviations from steady heart rhythm. Real Crustacea hearts are not likely to follow strictly either suite. The general procedure of analysis, however, is applicable to various biological rhythms, and explains how variation around the mean value can occasionally show up as intricate patterns which repeat themselves with accuracy.

Animals↗
PubMed2002

The K-Cl cotransporter in the lobster stretch receptor neurone--a kinetic analysis.

Experiments were performed to define quantitatively the substrate (K(+) and Cl(-)) dependence of the transport function (production of equally large and oppositely directed K(+)and Cl(-) flows/currents) of an earlier (Theander et al., 1999) identified electroneutral K-Cl cotransporter in the slowly adapting stretch receptor neurone of the European lobster. The experiments were based on microelectrode techniques. This allowed us to perform steady-state measurements of the so-called "instantaneous" current-voltage relationships (around a holding voltage of -65 mV after a blockage of the cell's action potential and hyperpolarization-activated currents) and intracellular ion concentrations at various settings of the extracellular K(+) and Cl(-) concentrations. From the results, we could then define steady-state values of all of the cell's non-KCl cotransporter K(+) and Cl(-) currents. Finally, the negative sums of the inferred non-KCl cotransporter K(+) and Cl(-) currents could be taken as equivalents of the K-Cl cotransporter's K(+) and Cl(-) currents for the reason that, in steady state, all membrane currents add up to zero. For the cotransporter currents, thus inferred for a range from 2.5/410.5 to 40.0/448.0 mM external K(+)/Cl(-), we found that their absolute values increased in a nonlinear fashion from about 5 nA cell(-1) at the lowest, to about 20 nA cell(-1) at the highest external K(+)/Cl(-) concentrations. Formally, this relationship could be reproduced by a Hill function-based enzyme kinetic expression simulating inward and outward transmembrane electroneutral ion transports. Following insertion of this expression into a comprehensive model of electrical membrane functions and intracellular solute and solvent control in the lobster stretch receptor neurone, the model predictions suggested that the K-Cl cotransporter does play an important role in (a) keeping intracellular Cl(-) low for a proper function of the cell's inhibitory system, and (b) enabling rapid transmembrane K(+) shifts that provide for a stabilization of the cell's membrane voltage and membrane excitability in cases of varying extracellular K(+) concentrations. The model predictions gave, however, no clear evidence that the K-Cl cotransporter is critically involved in the cell's volume regulation in conditions of varying extracellular osmolalities.

Animals↗
PubMed1993

A new crystal form of tropomyosin.

Tropomyosin crystals with a new morphology have been obtained from lobster tail muscle tropomyosin from which 11 residues at the carboxyl-terminus have been proteolytically removed to avoid head-to-tail polymerization. In contrast to the conventional Bailey crystal form in which the elongated tropomyosin molecules form a mesh, in the present crystals the molecules are packed side-to-side with the long axes parallel to the c-axis of the crystal. The unit cell is tetragonal with a = b = 109 A, c = 509 A, and the symmetry is either P4(1)2(1)2 or P4(3)2(1)2, with 4(1)(4(3)) helical axes parallel to the c-axis. This suggests that a group of molecules surrounding a local 4(1)(4(3)) axis is regarded as the building unit of the crystal. It is likely that the unit cell contains eight molecules with one molecule per asymmetric unit.

Amino Acid Sequence↗
PubMed1993

Influence of ionic strength on contractile force and energy consumption of skinned fibers from mammalian and crustacean striated muscle.

Increased ionic strength decreases maximal calcium-activated force (Fmax) of skinned muscle fibers via mechanisms that are incompletely understood. In detergent-skinned fibers from either rabbit (psoas) or lobster (leg or abdomen), Fmax in KCl-containing solutions was less than in potassium methanesulfonate (KMeSO3), which we showed previously was the least deleterious salt for adjusting ionic strength. In either salt, lobster fibers were considerably less sensitive to elevated ionic strength than rabbit fibers. Trimethylamine N-oxide (TMAO, a zwitterionic osmolyte found in high concentration in cells of salt-tolerant animals) increased Fmax, especially in high KCl solutions. In this regard, TMAO was more effective than a variety of other natural or synthetic zwitterions. In rabbit fibers, increasing ionic strength decreases Fmax but has little effect on contractile ATPase rate measured simultaneously using a linked-enzyme assay. Thus high salt increases the tension-cost of contraction (i.e. ratio ATPase/Fmax). At both high and low salt, TMAO decreases tension-cost. Given a simple two-state model of the cross-bridge cycle, these data indicate that ionic strength and TMAO affect the apparent detachment rate constant. High ionic strength KCl solutions extract myosin heavy- and light-chains, and troponin C from rabbit fibers. This extraction is virtually abolished by TMAO. Natural zwitterions, such as TMAO, have been shown to protect proteins against destabilization by high salt or other denaturatants. Our data indicate that, even in the best of salts, destabilization of the actomyosin complex may play a role in the effect of high ionic strength on the contractile process.

Adenosine Triphosphate↗
PubMed1994

Calcium-activated and stretch-induced force responses in two biochemically defined muscle fibre types of the Norway lobster.

Mechanical properties of thin (< 80 microns) myofibrillar bundles from single rehydrated freeze-dried fibres of the superficial abdominal flexor muscle of the lobster Nephrops norvegicus have been measured, and subsequently the protein content of these fibres has been analysed by SDS-PAGE. Two slow fibre phenotypes can be distinguished on the basis of their myofibrillar assemblages and sarcomere length (type S1: 6.0-7.5 microns, type S2: 8.0-10.9 microns). Differences (means +/- SD, average of seven fibres of each type) were observed in the kinetics for Ca2+ activation (half time of force development (ms); S1: 416 +/- 174; S2: 762 +/- 199 plus a delay of 280 +/- 130) and relaxation (half time of force decay (ms); S1: 162 +/- 75, S2: 257 +/- 53), for Ca2+ sensitivity of force generation (-log [Ca2+] for half maximal activation; S1: 5.40 +/- 0.12; S2: 5.55 +/- 0.08), and of the kinetics of stretch activation (delay of the peak of stretch-induced force increase (ms); S1: 91 +/- 30; S2: 493 +/- 436). From these results and partly also in combination with previously obtained mechanical data on intact fibres it can be concluded (1) that S2 fibres are specialized for long-lasting force maintenance whereas S1 fibres are adapted for slow movements; (2) intrinsic myofibrillar kinetics is not the main time-limiting factor for either activation or relaxation of intact fibres under physiological conditions; (3) processes which precede crossbridge cycling seem to be the main time-limiting factors for the Ca2+ activation of the myofibrils.

Animals↗