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At least 19 recordsLinked to original sources

Presence of the Periplaneta lectin-related protein family in the American cockroach Periplaneta americana.

We determined the partial amino acid sequences of Periplaneta lectin, which we had purified and characterized previously from the hemolymph of the American cockroach (Periplaneta americana) [Kubo T. and Natori S. (1987) Eur. J. Biochem. 168, 75-82]. Based on these sequences, we performed PCR and found that the cDNA library of the Periplaneta fat body contained many similar, but not identical, Periplaneta lectin-related cDNAs. Analysis of the cloned cDNAs suggested that Periplaneta has a protein family, of which the periplaneta lectin and LPS binding protein purified previously are members.

Amino Acid Sequence↗

A comparison of behavioral alterations in the brown cockroach, Periplaneta brunnea, and the American cockroach, Periplaneta americana, infected with the acanthocephalan, Moniliformis moniliformis.

We examined behavioral alterations in the brown cockroach, Periplaneta brunnea, infected with the acanthocephalan, Moniliformis moniliformis. The responses of infected and uninfected P. brunnea to light, substrate choice, and activity were compared. Infected brown cockroaches spent more time on white horizontal substrates under red and white light. Infected brown cockroaches also had a shorter freeze time than uninfected cockroaches after being presented with a light source. There was no difference in photophilia or activity of infected and uninfected brown cockroaches. These behavioral alterations in brown cockroaches were compared to those in Periplaneta americana, the American cockroach, infected with the same parasite. American and brown cockroaches differed in some responses to substrate, phototaxis, and activity.

Animals↗

Isolation, characterization and biological activity of a CRF-related diuretic peptide from Periplaneta americana L.

A diuretic peptide (Periplaneta-DP) has been isolated from extracts of whole heads of the cockroach, Periplaneta americana. The purified peptide increases cyclic AMP production and the rate of fluid secretion by isolated Malpighian tubules in vitro. In the fluid secretion assay, the response to native Periplaneta-DP is comparable to that obtained with crude extracts of cockroach corpora cardiaca, and the EC50 lies between 10(-8) and 10(-9) M. The primary structure of Periplaneta-DP was established as a 46-residue amidated peptide: T G S G P S L S I V N P L D V L R Q R L L L E I A R R R M R Q S Q D Q I Q A N R E I L Q T I-NH2. Periplaneta-DP is a further member of the recently established family of CRF-related insect diuretic peptides.

Amino Acid Sequence↗

The nature and development of sex attractant specificity in cockroaches of the genus Periplaneta. I. Sexual dimorphism in the distribution of antennal sense organs in five species.

Sexual dimorphism in the distribution of antennal sense organs is common among adults of the genus Periplaneta. In three out of the four strains of Periplaneta americana examined, adult males had more contact chemoreceptros than females. In the fourth strain of P. americana and in P. australasiae, P. brunnea, P. fuliginosa, and P. japonica, no statistically supportable sexual dimorphism of contact chemoreceptors was found. However, in all strains and species of Periplaneta examined, sexual dimorphism was found in the total number and/or density of olfactory sensilla. Male adults had nearly twice as many olfactory sensilla as female adults. These observations are consistent with the behavioral observation that males within the genus Periplaneta rely on the reception of an airborne pheromone for the initiation of courtship behavior. In P. americana, where sexual dimorphism was found in the contact chemoreceptors, contact stimuli release the full wing raising display and presentation in males during courtship.

Animals↗

Transplantation immunity in the American cockroach, Periplaneta americana: the rejection of integumentary grafts from Blatta orientalis.

The results from several previous studies have indicated that the American cockroach is able to respond to integumentary xenografts, but doubt remained as to whether cockroaches could effectively discriminate between self and allogeneic differences. This was emphasized by the fact that while one study reported that Periplaneta americana responded to grafts donated by the closely related genus Blatta orientalis, the data reported elsewhere, using a different assay system, found no such reactivity. Since we have subsequently reported, using a direct histological assay, that Periplaneta can in fact recognize and destroy integumentary allografts, we initiated a study to hopefully sort out the enigma presented by previous data using Blatta as a transplant donor. Integument from Blatta orientalis was transplanted orthotopically onto Periplaneta americana, and at various time points post-transplant, scored histologically for the survival of the subcuticular epidermal layer. The results clearly demonstrated that Periplaneta reacted to the Blatta tissue, because approximately 82% of the grafts had the epidermal layer destroyed by day 7 posttransplant. The kinetics of the response to Blatta was more in line with our allograft data, which would be in agreement with other work indicating that the closer the donor and recipient are on the phylogenetic tree, the less intense the reactivity to the foreign transplant.

Animals↗

Cloning, expression and functional analysis of an octopamine receptor from Periplaneta americana.

Octopamine regulates multiple physiological functions in invertebrates. The biological effects of octopamine and the pharmacology of octopamine receptors have been extensively studied in the American cockroach, Periplaneta americana. This paper reports the cloning of the first octopamine receptor from Periplaneta americana. A cDNA encoding a putative 7 transmembrane receptor was isolated from the head of Periplaneta americana. The encoded protein contains 628 amino acids and has sequence similarity to other biogenic amine receptors. This protein was expressed in COS-7 cells for radioligand binding studies using the antagonist 3H-yohimbine. Competitive binding comparing biogenic amines that could potentially function as endogenous ligands demonstrated this receptor had the highest affinity for octopamine (Ki = 13.3 microM) followed by tyramine, dopamine, serotonin and histamine. Octopamine increased both cAMP levels (EC50 = 1.62 microM) and intracellular concentrations of calcium through the receptor expressed in HEK-293 cells. Tyramine increased levels of both of these second messengers but only at significantly higher concentrations than octopamine. The cAMP increase by octopamine was independent of the increase in calcium. Competitive binding with antagonists revealed this receptor is similar to Lym oa1 from Lymnaea stagnalis. The data indicate that this cDNA is the first octopamine receptor cloned from Periplaneta americana and therefore has been named Pa oa1.

Amino Acid Sequence↗

A novel role of Periplaneta lectin as an opsonin to recognize 2-keto-3-deoxy octonate residues of bacterial lipopolysaccharides.

1. Periplaneta lectin of the American cockroach was shown to have affinity to bacterial lipopolysaccharides (LPS) of chemotypes Rb-Re, but not to lipid A. 2. 2-Keto-3-deoxy octonate (KDO) was the most effective sugar so far tested for inhibition of the hemagglutinating activity of Periplaneta lectin. 3. Periplaneta lectin was suggested to participate in the clearance of bacteria injected into the abdominal cavity of the cockroach.

Animals↗

Cloning and characterization of the adipokinetic hormone receptor from the cockroach Periplaneta americana.

Cockroaches have long been used as insect models to investigate the actions of biologically active neuropeptides. Here, we describe the cloning and functional expression in Chinese hamster ovary cells of an adipokinetic hormone (AKH) G protein-coupled receptor from the cockroach Periplaneta americana. This receptor is only activated by various insect AKHs (we tested eight) and not by a library of 29 other insect or invertebrate neuropeptides and nine biogenic amines. Periplaneta has two intrinsic AKHs, Pea-AKH-1, and Pea-AKH-2. The Periplaneta AKH receptor is activated by low concentrations of both Pea-AKH-1 (EC50, 5 x 10(-9)M), and Pea-AKH-2 (EC50, 2 x 10(-9)M). Insects can be subdivided into two evolutionary lineages, holometabola (insects with a complete metamorphosis during development) and hemimetabola (incomplete metamorphosis). This paper describes the first AKH receptor from a hemimetabolous insect.

Amino Acid Sequence↗

The molting gland of the cockroach Periplaneta americana: secretory activity and its regulation.

1. The prothoracic gland is the main source of ecdysteroids in larvae of the cockroach Periplaneta americana. 2. Besides ecdysone the molting gland of Periplaneta secretes 3-dehydroecdysone and proteins. 3. The molting gland of Periplaneta is regulated in different successive steps of cooperation of nervous and neuroendocrine activity. 4. Neurogenic effects on the molting gland via the prothoracic gland nerves are concentrated on the period of prepeak production of ecdysteroids. 5. Prior to the 17th day, the glands secretory activity is inhibited by GABA-ergic neuronal pathways from the subesophageal ganglion. 6. Neurogenic disinhibition by a peptidergic brain factor elicits the competence of the gland for prepeak activity, completed by the glandotropic effect of PTTH. 7. The 17th day of the larval stage is characterized as the head critical period, i.e., after this period the ecdysteroid secretion of the gland is independent of the prothoracicotropic hormone (PTTH) from the brain. 8. The main peak of ecdysteroid production is regulated by prothoracicotropic neuropeptids from the brain.

Animals↗

Antisera against Periplaneta americana Cu,Zn-superoxide dismutase (SOD): separation of the neurohormone bursicon from SOD, and immunodetection of SOD in the central nervous system.

In an effort to characterize the insect molting hormone bursicon from the cockroach, Periplaneta americana, amino acid sequences with high identity of Cu,Zn-superoxide dismutase (SOD) of Drosophila virilis were identified. Antisera against a conserved region of SOD, and a sequence unique to Periplaneta SOD were produced and used to test whether bursicon might be a form of SOD. Western blots of one- and two-dimensional gels revealed that the dimeric form of SOD and bursicon have a similar molecular mass (30 kDa). The two proteins can be separated, however, according to their different isoelectric points. Bursicon is identified in two-dimensional gels by elution from four unique spots not labeled by the anti-SOD antisera. In sections of Periplaneta nerve cords the antisera labeled glial material surrounding neuronal somata close to the neural sheath. Bursicon, however, is contained in unique cell pairs in the ganglia of the ventral nerve cord. These neurons were labeled with new antisera produced against novel sequences of one of the four above-mentioned bursicon active spots. The results show unequivocally that SOD and bursicon are distinctly different proteins. Furthermore, the anti-SOD antisera provided a tool to isolate and sequence bursicon.

Amino Acid Sequence↗

Hemolymph transfer as an assay for immunorecognition in the cockroach Periplaneta americana and the locust Schistocerca gregaria.

A quantitative assay for measuring the number of hemocytic nodules formed in response to foreign particles and soluble molecules has been used, in the locust Schistocerca and the cockroach Periplaneta, to investigate the response to transferred hemolymph. Xenogeneic test particles, rabbit neutrophil leukocytes, stimulate formation of nodules when injected into both insect species, compared with saline-injected controls. However, the number of nodules formed in the locust in response to cockroach hemolymph is significantly reduced compared with the response to other xenogeneic cells, and it is suggested that, in view of the strong reactivity of cockroach hemocytes to locust hemolymph and plasma, a graft-versus-host response might be occurring in the recipient locust. Whole hemolymph transferred allogeneically between Periplaneta, or xenogeneically from Blatta to Periplaneta, does not stimulate a response in the recipient. This corresponds well with results from other assays for immunorecognition of transplants and is further confirmation that allogeneic and, in some combinations xenogeneic, recognition is absent in insects.

Animals↗

Transient appearance and localization of a 26-kDa lectin, a novel member of the Periplaneta lectin family, in regenerating cockroach leg.

A lectin consisting of a 26-kDa subunit was purified from the hemolymph of adult American cockroaches (Periplaneta americana) and shown to be a member of the Periplaneta lectin family. Immunoblotting analysis revealed that this lectin appeared transiently in regenerating legs after nymphal legs were amputated. Thus, its mode of appearance was similar to that of regenectin, another member of the Periplaneta lectin family. However, its time of appearance and localization in the regenerates were different from those of regenectin: the 26-kDa lectin appeared in regenerates in the middle stage of regeneration and was localized in the vicinity of the outside of newly formed epidermal cells. These results suggest that this lectin participates in the organization or stabilization of the epidermis during leg regeneration.

Animals↗

The effects of dopamine receptor agonists and antagonists on the secretory rate of cockroach (Periplaneta americana) salivary glands.

The acinar salivary glands of the cockroach, Periplaneta americana, are innervated by dopaminergic and serotonergic nerve fibers. Serotonin stimulates the secretion of protein-rich saliva, whereas dopamine causes the production of protein-free saliva. This suggests that dopamine acts selectively on ion-transporting peripheral cells within the acini and the duct cells, and that serotonin acts on the protein-producing central cells of the acini. We have investigated the pharmacology of the dopamine-induced secretory activity of the salivary gland of Periplaneta americana by testing several dopamine receptor agonists and antagonists. The effects of dopamine can be mimicked by the non-selective dopamine receptor agonist 6,7-ADTN and, less effectively, by the vertebrate D1 receptor-selective agonist chloro-APB. The vertebrate D1 receptor-selective agonist SKF 38393 and vertebrate D2 receptor-selective agonist R(-)-TNPA were ineffective. R(+)-Lisuride induces a secretory response with a slower onset and a lower maximal response compared with dopamine-induced secretion. However, lisuride-stimulated glands continue secreting saliva, even after lisuride-washout. Dopamine-induced secretions can be blocked by the vertebrate dopamine receptor antagonists cis(Z)-flupenthixol, chlorpromazine, and S(+)-butaclamol. Our pharmacological data do not unequivocally indicate whether the dopamine receptors on the Periplaneta salivary glands belong to the D1 or D2 subfamily of dopamine receptors, but we can confirm that the pharmacology of invertebrate dopamine receptors is remarkably different from that of their vertebrate counterparts.

2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-ben↗

Molecular characterization of the ebony gene from the American cockroach, Periplaneta americana.

Biogenic amines are an important class of primary messengers in the central (CNS) and peripheral nervous systems and in peripheral organs. These substances regulate and modulate many physiological and behavioral processes. Various inactivation mechanisms for these substances exist to terminate biogenic amine-mediated signal transduction. In vertebrates, the enzymes monoamine oxidase and/or catechol-O-methyl-transferase are involved in these processes. In insects, however, in which both enzymes are low in abundance or absent, biogenic amines are inactivated mainly by N-acetylation or O-sulphation. In Drosophila, beta-alanyl conjugation mediated by the Ebony protein has recently been shown to be a novel and alternative pathway for biogenic amine inactivation. Here, we report the cloning of ebony cDNA (Peaebony) from a brain-specific cDNA library of the cockroach Periplaneta americana. The open reading frame encodes a protein of 860 amino acid residues (PeaEbony). The PeaEbony polypeptide shares homology to Ebony sequences from Anopheles gambiae, Apis mellifera, and Drosophila melanogaster. In addition, PeaEbony exhibits sequence similarity to a family of microbial non-ribosomal peptide synthetases. The mRNA encoding PeaEbony is highly expressed in the cockroach brain and to a lesser extent in the salivary glands. PeaEbony is, therefore, probably involved in the inactivation of various biogenic amines through beta-alanyl conjugation in the cockroach CNS. Since the salivary glands in Periplaneta are innervated by dopaminergic and serotonergic neurons, PeaEbony probably also biochemically modifies dopamine and serotonin in these acinar glands.

Amino Acid Sequence↗

The nature and development of sex attractant specificity in cockroaches of the genus Periplaneta. IV. electrophysiological study of attractant specificity and its determination by juvenile hormone.

The antennae of male Periplaneta americana acquire a large number of olfactory receptors at the adult stage. Electrophysiological methods (single unit and electroantennogram recording) show that a portion of the receptors added at the adult ecdysis are sex attractant receptors. Sex attractant receptors are not present in large numbers on larval and adult female antennae. The differentiation of pheromone receptors is inhibited during normal larval development by juvenile hormone. Topical application of juvenile hormone-mimic to male antennae during the terminal larval instar inhibits their development. Comparative electrophysiological studies indicate a high degree of cross-reactivity of the P. americana sex attractant among four other species within the genus Periplaneta.

Action Potentials↗

Binding of N-[propionyl-3H]propionylated alpha-bungarotoxin and L-[benzilic-4,4'-3H] quinuclidinyl benzilate to CNS extracts of the cockroach Periplaneta americana.

The nerve cord of the cockroach (Periplaneta americana) contains distinct saturable components of specific binding for the ligands N-[propionyl-3H]propionylated alpha-bungarotoxin and L-[benzilic-4,4'-3H]quinuclidinyl benzilate. N-[Propionyl-3H]propionylated alpha-bungarotoxin bound reversibly to homogenates with a Kd of 4.8 nM and Bmax of 910 fmol mg-1. The association rate constant (1.9 X 10(5) M-1 s-1) and dissociation rate constant (1.2 X 10(-4) s-1) yielded a Kd of 0.6 nM. Nicotinic ligands were found to displace toxin binding most effectively. The binding sites characterized in this way showed many similarities with the properties of the vertebrate neuronal alpha-bungarotoxin binding site. For a range of cholinergic ligands, inhibition constants calculated from toxin binding studies closely corresponded to their effectiveness in blocking the depolarizing response to acetylcholine recorded by electrophysiological methods from an identified cockroach motoneurone. The N-[propionyl-3H]propionylated alpha-bungarotoxin binding component therefore appears to be a constituent of a functional CNS acetylcholine receptor. Binding of L-[benzilic-4,4'-3H]quinuclidinyl benzilate was reversible with a Kd of 8 nM and Bmax of 138 fmol mg-1, determined from equilibrium binding experiments. The Kd calculated from the association rate constant (2.4 X 10(5) M-1 s-1) and dissociation rate constant (1.3 X 10(-4) s-1) was 1.9 nM. Muscarinic ligands were the most potent inhibitors of quinuclidinyl benzilate binding. The characteristics of this binding site resembled those of vertebrate CNS muscarinic cholinergic receptors. In contrast with vertebrate CNS, the nerve cord of Periplaneta americana contains more (approximately X 7) alpha-bungarotoxin binding sites than quinuclidinyl benzilate binding sites.

Animals↗

Measurement of the pyroelectric coefficient and permittivity on Rhododendron and Encephalartos leaves and on the insect Periplaneta americana.

Pyroelectric (PE) voltage responses to single square radiation signals absorbed in epidermal layers of the leaves of Encephalartos villosus and Rhododendron catawbiense and in the integument of the insect Periplaneta americana L. were investigated on dry preparations as well as on whole fresh leaves and live insects. Measurements of the initial slopes of the responses, the rise times, and the peak voltages were carried out with 10 interchangeable load resistors from 5M omega to 10 G omega, connected parallel to the samples. In encephalartos leaves this yielded for the permittivity epsilon and the PE coefficient lambda in the upper/lower epidermis, epsilon = 30/60 and lambda = 2/6 pC/cm2K, respectively, and in rhododendron, epsilon = 60/200 and lambda = 3/15 pC/cm2K. In periplaneta we found epsilon = 300 and lambda = 20 pC/cm2K for the abdomen rings, and epsilon = 1,000 and lambda = 350 pC/cm2K for the thorax of live insects. Generally, dry preparations of leaves, and especially of insects, showed smaller PE responses. The outer epidermis of live plant leaves and the integument of live insects appear to be polar and to exhibit pronounced PE properties.

Animals↗