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PubMed1990

Catecholamines and related o-diphenols in cockroach hemolymph and cuticle during sclerotization and melanization: comparative studies on the order Dictyoptera.

Catecholamines and related o-diphenols extracted from the cuticle and hemolymph of adult cockroaches during sclerotization and pigmentation of the cuticle were analyzed by reverse phase HPLC with electrochemical detection. At ecdysis, dopamine (DA) o-conjugates predominated in the hemolymph of Periplaneta americana, P. australasiae, P. fuliginosa, P. brunnea, and Blatta orientalis (Blattidae); Blattella germanica (Blattellidae); and Gromphadorhina portentosa and Blaberus craniifer (Blaberidae). N-Acetyldopamine (NADA) conjugates were second in abundance in these species, but were major in the hemolymph of the other blaberoid species, Leucophaea maderae and Nauphoeta cinerea. After ecdysis NADA became the major hemolymph catecholamine in all species as DA decreased rapidly. N-beta-Alanyldopamine (NBAD) concentrations in the hemolymph remained low in all species, although NBAD and its metabolite, N-beta-alanylnorepinephrine (NBANE), were generally the major catecholamines in tanning cuticle. Catechol (1,2-dihydroxybenzene) occurred mainly as a conjugate(s) at high levels in the hemolymph of nymphs and adults of all blattid species. Only trace amounts were detected in B. germanica and Cryptocercus punctulatus (Cryptocercidae), and none was found in any of the blaberoid species. High concentrations of NBANE and NBAD accumulated in tanning cuticle of B. germanica, G. portentosa, and all blattid species, whereas NADA and DA predominated in cuticle from the other blaberoid species, particularly L. maderae and N. cinerea. However, cockroaches as a group appear to utilize both the N-acetyl and N-beta-alanyl catecholamines for stabilization of the exoskeleton. The Blattidae differed most from the other families in having considerably higher concentrations of catecholamines in hemolymph and cuticle, as well as the large amounts of catechol conjugates in the hemolymph.

Animals↗
PubMed2000

Osmotic and ionic hemolymph concentrations of bathyal and abyssal amphipods of Lake Baikal (Siberia) in relation to water depth.

We studied the adaptive variations of the hemolymph concentrations in relation to water depth and pressure using deep-dwelling amphipods from Lake Baikal. Hemolymph osmolality was determined in six bathyal and abyssal species immediately after capture when values come closest to the habitat concentrations. In three species, hemolymph osmolalities correlated positively with depth of capture. Prevalent ions in the hemolymph are sodium and chloride. Lactate, our indicator for capture stress, was highest after trawling (2-6 mM) and lowest after retrieval from cages (0-0.6 mM). Acclimation to different pressure was studied by exposing the specimens to different water depths over several days. Hemolymph concentrations did not change after acclimation to surface pressure in the sublittoral Acanthogammarus albus, a native also to shallow water, but decreased by 30-80 mosmol/kg H2O in the bathyal and abyssal species Acanthogammarus grewingki, Acanthogammarus reicherti, and Parapallasea lagowskii. Similarly, hemolymph osmolality decreased in A. reicherti and P. lagowskii originating from deep water, when acclimated to reduced water depth, and, in A. reicherti hemolymph osmolality reached its original high value when returned to the depth of capture. Higher hemolymph osmolalities and NaCl concentrations, demonstrated here for the first time, may provide selective advantages to abyssal species.

Adaptation, Physiological↗
PubMed1985

Ornithodoros moubata: host immunoglobulin G in tick hemolymph.

Hemolymph proteins of a soft tick, Ornithodoros moubata, were analyzed immunochemically and biochemically. The components of tick hemolymph proteins were shown to be totally different from the host (rabbit) serum proteins by polyacrylamide gel electrophoresis with sodium dodecyl sulfate and Coomassie blue or silver stain. However, in the hemolymph of ticks engorged from rabbits immunoglobulin G was detected by immunoblotting analysis with goat anti-rabbit immunoglobulin G. The concentration of rabbit Immunoglobulin G in tick hemolymph changed with the physiological stages after a blood meal. Immunoglobulin G was isolated from tick hemolymph by affinity chromatography on a Protein A-Sepharose 4B column. Analysis of the isolated immunoglobulin G from tick hemolymph with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Ouchterlony double diffusion test showed it to be composed of the same subunits as heavy and light chains of host (rabbit) immunoglobulin G. Tracer experiments showed that 125I-labeled heavy and light chains of immunoglobulin G were detected in an intact form in hemolymph from ticks that sucked 125I-labeled rabbit immunoglobulin G through an artificial membrane. These facts suggested that the host rabbit immunoglobulin G ingested in the tick midgut passed through the gut wall without digestion. By solid-phase enzyme immunoassay, immunoglobulin in the hemolymph was shown to retain its antibody activity.

Animals↗
PubMed1990

High-pressure liquid chromatographic analysis of hemolymph plasma catecholamines in immune-reactive Aedes aegypti.

Tyrosine and catecholamines have been implicated as substrates for the encapsulation reactions involved in the immune response of mosquitoes to microfilariae (mff). Identification and quantitation of tyrosine and catecholamines present in Aedes aegypti hemolymph plasma were accomplished by ion-pair high-pressure liquid chromatography with electrochemical detection at either +650 or +850 mV vs Ag/AgCl. Tyrosine, dopamine, and N-beta-alanyldopamine were detected in the hemolymph plasma of naive A. aegypti. Although no differences in these compounds were observed in hemolymph plasma from A. aegypti inoculated with Dirofilaria immitis mff, the chromatogram showed a single major peak (PI) (65 microM, expressed as dopamine equivalents) that was not present in naive hemolymph plasma. Saline-inoculated controls contained only 5% of the PI in immune reactive hemolymph plasma. A high concentration of PI (127 +/- 39 microM) was also detected after treatment of hemolymph plasma with mild alkaline conditions (pH 9.0), indicating that it is normally present as an electrochemically inert form in naive mosquitoes. High concentrations of PI were also detected in the naive hemolymph plasma from three other mosquito species, but no PI was found in A. trivittatus under any conditions. PI did not cochromatograph with any of the catecholamines commonly thought to be involved in immune responses of dipterans against metazoan parasites, suggesting that it may be a unique substrate for these reactions. The biological relevance of PI was evidenced by its appearance in the hemolymph plasma of two strains of D. immitis-inoculated A. aegypti.

Aedes↗
PubMedDate not supplied

Agglutinin activity in Pacific oyster (Crassostrea gigas) hemolymph following in vivo Vibrio anguillarum challenge.

Hemolymph from the Pacific oyster (Crassostrea gigas) contains lectins that agglutinate horse (Gigalin E) and human (Gigalin H) erythrocytes. The gigalins also agglutinate bacteria, including Vibrio anguillarum, and were adsorbed from oyster hemolymph at different temperatures by living, heat-killed, and freeze-dried V. anguillarum cells. Baseline activities of the two gigalins were established by measuring their activities in oyster hemolymph over a period of 4 years. A normal distribution of Gigalin H activity (mean titer 139) was found, whereas the distribution of Gigalin E activity in the same samples was skew (mean titer 512). No covariance was observed between the two agglutinin activities. Increased lectin activity above this baseline was found in oysters exposed for varying time intervals to V. anguillarum at different seasons and temperatures over a period of 2 years. Such exposure resulted in an increase in activity (titer) of four- to nine-fold for Gigalin E and three- to seven-fold for Gigalin H when compared with controls, and in augmentation in the hemolymph of a protein with the same electrophoretic mobility as affinity-purified oyster lectins (gigalins). Challenge with either living or heat-killed bacteria resulted in a significant increase of Gigalin E activity, whereas results for Gigalin H were variable. Oysters challenged with bacteria were observed to filter normally with open shells during the experiments. Also, no increase was found in hemolymph calcium that could indicate anoxia following bacterial challenge (0.49 +/- 0.004 mg mL-1) compared to unexposed oysters (0.50 +/- 0.001 mg mL-1). Increase in the concentration of free amino acids in oyster hemolymph was observed following exposure to bacteria (15.05 mM) and anaerobiosis (13.51 mM) compared to controls (9.06 mM), and changes (in mol %) of individual amino acids differed considerably between hemolymph from animals challenged with bacteria and animals kept anaerobic. The augmented lectin activity in oyster hemolymph, following in vivo exposure to increased bacteria in the seawater, suggests their involvement in enhancing bacterial clearance and defense in the oyster.

Adhesins, Bacterial↗
PubMed1982

Regulatory effects of temperature and hemolymph on inhibition and enhancement of attachment and filopodia function of phagocytic granular cells of the silkworm, Bombyx mori.

The effect of temperature on the adhesiveness and filopodia elongation of granular cells was examined in the presence or absence of hemolymph. The incubation in hemolymph remarkably increased the number of adherent cells almost irrespective of temperatures. Marked inhibition of attachment was seen in incubation media without hemolymph or with 20% hemolymph but at much lower temperatures. Filopodia elongation was markedly inhibited at a low temperature even when the cells were incubated in hemolymph alone. However, the number of filopodia-elongated cells was increased by raising the temperature even without hemolymph. These results show that hemolymph of B. mori is suggested to contain at least two kinds of humoral factors which affect the initial phases of cellular reactions to foreign materials. One is to promote attachment and the other to activate filopodia function. Moreover, it is shown that attachment is a temperature-independent process in the presence of hemolymph unlike filopodia elongation. However, since both attachment and filopodia elongation were increased by raising the temperature, temperature is considered to be another important cofactor in enhancement of foreignness-recognition and binding ability.

Animals↗
PubMed2000

Host hemolymph proteins and protein digestion in larval Habrobracon hebetor (Hymenoptera: braconidae).

Host plasma proteins and protein digestion in larval parasitoids were studied during trophic interactions of the ectoparasitoid Habrobracon hebetor Say (Hymenoptera: Braconidae), with a host, larvae of the Indianmeal moth, Plodia interpunctella Hübner (Lepidoptera: Pyralidae). We could detect no apparent differences in host hemolymph protein patterns up to 72 h after paralysation and/or parasitization by H. hebetor. A 190 kDa putative apolipophorin I present in host hemolymph could not be detected in the midguts of feeding H. hebetor larvae indicating that it is rapidly digested. The major 60 kDa storage proteins (putative hexamerins) in host hemolymph were detected in the parasitoid midgut and were completely digested 24 h after cessation of feeding and the beginning of cocoon formation. Host hemolymph had a pH of about 6.4. The pH optima of the midgut proteinases in the larval parasitoid were in the alkaline region, but midgut fluid in feeding parasitoid larvae was about pH 6. 8. Based on enzyme activity against selected artificial proteinase substrates including azocasein, N-alpha-benzoyl-L-Arg p-nitroanilide (BApNA), succinyl-Ala-Ala-Pro-Phe p-nitroanilide (SAAPFpNA), succinyl-Ala-Ala-Pro-Leu p-nitroanilide (SAAPLpNA), and inhibition by selected proteinase inhibitors, serine proteinases appear to be the predominant class of enzymes involved in protein digestion in the midguts of H. hebetor. There is also an active aminopeptidase (LpNA) associated with the microsomal fraction of midgut preparations. There was no evidence for preoral digestion or ingestion of proteinases from host hemolymph by the parasitoid larva. There was a very active BApNAase in the soluble fraction of midgut extracts. This activity increased on a per midgut basis up to 24 h after the beginning of cocoon formation but decreased rapidly by 48 h. Two major (P1 and P3) and several minor proteinases were detected in midgut extracts of H. hebetor analysed with gelatin zymograms. The apparent molecular mass of P1 varied from 95 to 49 kDa depending on protein loading. P3 had an apparent molecular mass of 39 kDa that was independent of protein loading. In summary, electrophoretic evidence indicates that host hemolymph protein patterns do not change significantly for at least 72 h after paralysation by H. hebetor. The role, if any, of envenomization in preventing breakdown of hemolymph proteins during this time remains to be determined. Because the predominant host hemolymph proteins, a putative apolipophorin I and the putative hexamerins, are readily digested by the serine proteinases present in the midguts of this parasitoid larva, these or similar proteins would provide an easily digested source of dietary amino acids that could be used for development of artificial diets for this beneficial insect.

Animals↗
PubMed1998

Purification and properties of two blue biliproteins from the larval hemolymph and integument of Rhodinia fugax (Lepidoptera: Saturniidae).

Blue biliproteins (BPs) are found in the hemolymph and integument of the fifth instar larvae of the saturniid silkworm, Rhodinia fugax. An efficient method of isolating BPs from the hemolymph, epidermis and cuticle using hydrophobic interaction chromatography and ion-exchange chromatography was devised. The BPs from the hemolymph, epidermis and cuticle have molecular weights of approximately 24,000, 48,000 and 23,000 Da by gel-filtration, respectively. Using matrix-assisted laser desorption ionization-time of flight/mass spectrometry (MALDI-TOF/MS), the respective molecular masses were determined to be 22,641, 22,908 and 22,737 Da. Based on these results, BP molecules from the hemolymph and cuticle are assumed to be monomers, whereas the epidermal BP is a dimer. The amino acid composition and N-terminal amino acid sequences of the BPs from the hemolymph and cuticle (BP-I) are very similar, but the BP from the epidermis (BP-II) is quite different. The N-terminal amino acid sequences of these BPs share approximately 50% identity with the biliproteins from other lepidopteran insects. The blue color of BP is due to the presence of bile pigments, which are non-covalently bound to the apoprotein. The absorbance spectrum of BP-I from the hemolymph revealed maxima at 280 and 669 nm, while that of BP-II showed maxima at 280, 385 and 663 nm. The pigment dimethyl esters were extracted from BP-I and BP-II with acidic methanol and dichloromethane. The results of these analyses suggest that the blue pigments of BP-I and BP-II are different; BP-I contains a phorcabilin-like pigment while BP-II contains biliverdin IX gamma. In an immunoblot analysis, anti-BP-I antibodies, produced against hemolymph BP-I, reacted with immunoreactive proteins in the hemolymph and cuticle of R. fugax. These anti-BP-I antibodies did not react with BP-II and only cross-reacted weakly with Samia cynthia ricini biliverdin-binding protein (BBP)-II.

Amino Acid Sequence↗
PubMedDate not supplied

Inhibition of human cell apoptosis by silkworm hemolymph.

Many studies on preventing apoptosis have been carried out from the viewpoint of anti-apoptotic cloned-gene expressions inside cells, whereas in this study, we investigated the inhibition of apoptosis by the addition of silkworm hemolymph, a natural compound, from outside of the cells. In a previous study, we reported the inhibition effect of silkworm hemolymph on the baculovirus-induced insect cell apoptosis. Using the vaccinia virus-HeLa cell system as a model system in this study, we found that silkworm hemolymph, the insect serum, inhibits apoptosis not only in the insect cell system but also in the human cell system. The vaccinia virus-induced HeLa cell apoptosis was analyzed using DNA electrophoresis, TUNEL, and flow cytometry, and the resulting data confirmed that silkworm hemolymph inhibits human cell apoptosis. The inhibition of apoptosis due to silkworm hemolymph was not caused by an inhibition of virus binding and internalization steps, nor did silkworm hemolymph interfere with the virus production. The inhibition of apoptosis by silkworm hemolymph decreased the cell detachment from an adhering surface. With these characteristics, silkworm hemolymph can be effectively used to minimize cell death in commercial animal cell culture.

Animals↗
PubMed2005

Evaluation of a nonlethal technique for hemolymph collection in Elliptio complanata, a freshwater bivalve (Mollusca: Unionidae).

Hemolymph, the circulatory fluid of bivalves, transports nutrients, respiratory gases, enzymes, metabolic wastes, and toxicants throughout the body. Hemolymph can provide information pertinent to health assessment of animals or populations, but is not commonly used in freshwater bivalves partly because of the lack of tested, practical techniques for its nonlethal collection. The objective of this study was to evaluate the effect of hemolymph collection on the growth and survival of Elliptio complanata, a freshwater bivalve (Unionidae). We describe a simple technique for the collection of hemolymph from the anterior adductor muscle sinus of E. complanata. To evaluate the effect of hemolymph sampling on mussel survival and growth, 30 mussels sampled using the technique and 30 unsampled controls were followed for 3 mo post collection. Nine animals were sampled 3 times over 7 mo to monitor effects of repeated sampling. No negative impacts on survival or growth were observed in either the singly or repeatedly sampled animals. We also compared the composition of hemolymph collected from the adductor muscle sinus with that collected from the ventricle of the heart. Calcium levels and cell count of hemolymph obtained from the adductor sinus and ventricle were significantly different. There was no significant difference between collection sites for magnesium, phosphorus, ammonia, protein, sodium, potassium, or chloride. We conclude that collection of hemolymph from the adductor sinus is safe for sampled E. complanata and should be explored as a relatively non-invasive, and potentially useful, approach to the evaluation of freshwater mussel health.

Animals↗
PubMed1994

[Studies on the components of trace elements and macro elements in hemolymph of Anopheles anthropophagus].

The elements in hemolymph of An. anthropophagus were determined by ICAP. There were 18 kinds of trace elements such as Fe,Zn,Cu,Mn,Cr,Mo,Co,Ni,V,Sr,B,Al,Ba,Zr, Cd,Pb,Ga,Li and 6 kinds of macro elements such as Ca,Mg,K,Na,S,P in the hemolymph of the mosquito. The contents of the macro elements and Fe in hemolymph of newly emerged mosquitoes were significantly higher than those of mosquitoes after taking blood meal, whereas Zn and Al were lower. Comparing elements in hemolymph of An. anthropophagus and An. sinensis, there were 14 kinds of elements in newly emerged mosquitoes with striking significant difference, while there were 13 kinds of elements with striking significant difference in the mosquitoes after taking blood meal. Comparing elements in the hemolymph of An. anthropophagus and Ae. albopictus, there were 13 kinds of elements with striking significant difference in the hemolymph of newly emerged mosquitoes and the mosquitoes after taking blood meal. The results suggested that the components of elements in hemolymph were relevant to the nutritional metabolism and development of mosquitoes, and that mosquitoes of different species and with different sensibilities to malaria parasites also showed difference in the contents of elements in their hemolymph.

Aedes↗
PubMed1999

Isolation and identification of terpenoid sex pheromone components from extracts of hemolymph of males of the Caribbean fruit fly.

Extracts obtained from hemolymph of sexually mature males of the Caribbean fruit fly Anastrepha suspensa contained four biologically important terpenoid components of the sex pheromone. The four components were identified as farnesene, bisabolene, anastrephin, and epianastrepin based on their relative retention indexes from capillary gas chromatography analysis, using both apolar and polar phase columns and their chemical ionization (isobutane) mass spectra. The ratio of the components in extracts of hemolymph was the same as the ratio present in the volatile blend of pheromone released by sexually mature males during the reproductive period. Studies conducted to determine the effect of age on amounts of these components in hemolymph indicated that they increased from undetectable levels on the day of adult emergence to maximum levels on day eight. The increases in amounts of the components present in hemolymph with increasing age were correlated with increases in amounts of volatile pheromone released by males. Time of day studies showed that the amounts of these components in hemolymph followed the daily pattern of release of volatile pheromone components. Other components of the sex pheromone including ocimene, (Z)-3-nonen-1-ol, (Z,Z)-3,6-nonadien-1-ol and suspensolide were not found in extracts of hemolymph. The data suggest that the hemolymph plays a role in the transport of these pheromone components during sexual signalling. Arch. Insect Biochem. Physiol. 42:225-232, 1999. Published 1999 Wiley-Liss, Inc.

Age Factors↗
PubMed2000

Amblyomma americanum: specific uptake of immunoglobulins into tick hemolymph during feeding.

The passage of immunoglobulins in the blood meal into hemolymph prompts development of vaccines against internal antigens of ticks, but little is known about kinetics and specificity of the immunoglobulin uptake. We used capillary feeding of adult Amblyomma americanum hard ticks to introduce compounds into the midgut and then examined the hemolymph after various times for their presence and concentration. Immunoglobulins of different sources, albumin, choramphenicol acetyltransferase, inulin, and mannitol were labeled with (125)I, (14)C, or biotin. With the exception of the carbohydrate inulin, all the compounds entered the hemolymph of tick during capillary feeding. The small molecule mannitol had the highest rate of entry at 9% after 6 h. Among proteins, the entry of immunoglobulin G (IgG) of different species into the hemolymph was greater at 6% after 6 h than for the smaller proteins albumin or choramphenicol acetyltransferase at 1 and 3%, respectively. The entry of denatured IgG was equal to that of nondenatured protein. There was no evidence of degradation of the IgG or of its binding to cells once it entered the hemolymph. A monoclonal IgG antibody labeled with biotin entered the hemolymph and retained its ability to bind to its specific antigen in an immunoassay. Although different proteins entered the hemolymph after capillary feeding, there was evidence of a specific mechanism for immunoglobulin uptake.

Animals↗
PubMed2002

Transfer of lipids between hemolymph and hepatopancreas in the shrimp Macrobrachium borellii.

Crustacean lipids are transported in the hemolymph by an HDL. The hepatopancreas is the most important and active organ regarding lipid metabolism, so we studied the interchange of FA and acylglycerols between both components of the hepatopancreas-hemolymph system in the decapod crustacean Macrobrachium borellii. The hepatopancreas and a sole plasma lipoprotein were labeled by in vivo incubations with 14C palmitic acid injected into the hemolymph. Then they were incubated in vitro with unlabeled hepatopancreas and hemolymph, and the transfer of lipids between them was measured by radiochromatographic techniques. It was determined in vivo that more than 80% of the circulating palmitic acid was taken up by the hepatopancreas and incorporated into PC and TAG. Both classes of lipids, but mainly PC, were transferred back from tissues to the hemolymph. Lipid transfer was also demonstrated in vitro. The transfer of PC (30% of labeling) as well as that of FFA (48% of labeling) from hemolymph to hepatopancreas was determined. On the other hand, FFA were released more efficiently than the acylglycerols from intact hepatopancreas to hemolymph, and they were the only lipid transferred when the hepatopancreas had been previously washed.

Animals↗
PubMed1992

Regulation of methyl farnesoate in the hemolymph and mandibular organ of the lobster, Homarus americanus.

Methyl farnesoate (MF) was measured in the hemolymph and mandibular organs (MO) of the lobster. Although a few animals had detectable MF levels in their hemolymph, this compound was undetectable (less than 0.4 ng/ml) in the hemolymph of most animals. One day after bilateral eyestalk ablation, MF was detected in the hemolymph of all animals, reaching variable levels (2.0-31.2 ng/ml) by the fourth day. Unilateral eyestalk ablation caused a smaller increase in hemolymph levels of MF. Similarly, the MF content of the MO, the only known site of MF synthesis, was low in intact lobsters (8.1 ng/gland) and was elevated in unilaterally and bilaterally eyestalk-ablated animals (54.1 and 106.9 ng/gland, respectively). When extracts of the sinus gland (SG), a source of neuropeptides in the eyestalk, were injected into bilaterally ablated lobsters, hemolymph levels of MF dropped to undetectable levels in 2 to 3 hr. The response to SG extract was dose dependent, and MF levels recovered by 12 to 24 hr after treatment. SG extract also lowered the MF content in the MO from 267.6 to 6.6 ng/gland after 4 hr. These results indicate that MF in the hemolymph and MO is negatively regulated by a factor(s) from the SG.

Analysis of Variance↗
PubMed1980

Hemolymph acid-base balance of the crayfish Astacus leptodactylus as a function of the oxygenation and the acid-base balance of the ambient water.

The acid-base balance of the prebranchial hemolymph of the crayfish Astacus leptodactylus was studied at various acid-base balances and levels of oxygenation of the ambient water at 13 degrees C. The water acid-base balance was controlled automatically by a pH-CO2-stat. Into water of constant titration alkalinity, TA, this device intermittenly injects carbon dioxide to maintain the pH at a preset value. Water pH was reduced to the same value either by hypercapnia (at constant TA) or by adding HCl or H2SO4 to decrease the TA (at constant CO2 tension). Decrease of hemolymph pH and increase of hemolymph PCO2 were similar for the three acidic waters. Water oxygenation changes strongly affected hemolymph ABB. In crayfish living in hyperoxic water (PO2 congruent to 600 Torr) compared to those in hypoxic water (PO2 congruent to 40 Torr), hemolymph pH was 0.3 to 0.4 unit lower and hemolymph PCO2 several times higher, the exact values of pH and PCO2 depending on the controlled ambient acid-base balance. In any study of the hemolymph acid-base balance of the crayfish, it is an important to control ambient water's acid-base balance and oxygenation as it is to control its temperature, a conclusion which probably holds true for studies on all water breathers.

Acid-Base Equilibrium↗
PubMed2005

The effect of sugars and free amino acids from the freshwater prawn Macrobrachium rosenbergii hemolymph on lectin activity and on oxidative burst.

We determined the effect of low molecular weight components (LMWC) from healthy juvenile and adult Macrobrachium rosenbergii hemolymph on lectin activity and oxidative burst (OB) in hemocytes. In an attempt to identify the LMWC that affect the lectin's hemagglutinating activity or oxidative burst, we determined the hemolymph carbohydrates and free amino acids (FAA) concentration. The LMWC (<2000 Da) were obtained after dialysis of the hemolymph. Our results showed that LMWC from juveniles exerted a greater inhibition on lectin than LMWC from adult hemolymph. Production of superoxide radicals by hemocytes was lower in the presence of juvenile (p<0.05) as compared to adult LMWC. FAA composition of the hemolymph and of LMWC from adults showed higher proportion of alanine (which corresponded to 25% of total FAA) and proline (>20%); whereas, in juveniles, the main FAA identified were glycine (>40%) and alanine (26%). N-Acetyl-D-glucosamine (GlcNAc) was the main sugar residue in the hemolymph and LMWC from juveniles; its concentration was 2.4 times higher than glucose (Glc), whereas, in adults, Glc was the main free sugar residue. Our results suggest that the proportion of FAA and carbohydrates in the hemolymph of M. rosenbergii seems to be correlated with the maturation process; furthermore, the high proportion of free GlcNAc and glycine regulate, in the juvenile stage, lectin activity and cellular oxidative mechanisms, respectively.

Amino Acids↗
PubMed2003

A novel function of cockroach (Periplaneta americana) hypertrehalosemic hormone: translocation of lipid from hemolymph to fat body.

The hypertrehalosemic hormones Pea HTH-I and Pea HTH-II have a lipogenic effect in the cockroach, Periplaneta americana. This has been determined by measuring the change in tri-, di-, monoacylglycerol, phospholipid and free fatty acids in the hemolymph and fat body in response to the hormones. The effect of both hormones 6h after injection is comparable and is expressed as an increase in fat body triacylglycerol and a decrease in hemolymph triacylglycerol. Coincident with this effect the concentration of diacylglycerol in the hemolymph decreases while that in the fat body increases. Hemolymph and fat body phospholipid are both lowered by HTH. The concentration of free fatty acids in the hemolymph, as well as fat body, are increased by both hormones. Confirmation of the lipogenic effect of HTH has been obtained by feeding cockroaches [3H]oleic acid and measuring the incorporation of label into hemolymph and fat body lipid. The data show that the specific activity of the hemolymph phospholipid fraction increases more than 50%. In fat body, the specific activity of the label in the triacylglycerol fraction increased more than 2-fold while that in the free fatty acid fraction increased more than 20-fold. The data support the view that the fatty acids incorporated into fat body triacylglycerol under the influence of HTH are not formed de novo but are derived from the sn-1 and sn-2 positions of phospholipid which is initially formed in the midgut wall.

Animals↗