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Michael Locke - One of the best experts on this subject based on the ideXlab platform.
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The characterization of ferritin in an insect
Insect Biochemistry, 2003Co-Authors: Helen Nichol, Michael LockeAbstract:Abstract In mammals, the iron storage protein ferritin is predominantly synthesized on free polysomes and accumulates in the cytosol but some is secreted and circulates in the blood as serum ferritin. In insect tissues, on the other hand, iron-containing holoferritin accumulates in the vacuolar system and can be secreted through the Golgi complex. The midgut can secrete it to the gut lumen and other tissues to the hemolymph. Ferritin was isolated from the midgut and hemolymph of fifth instar larvae of Calpodes ethlius , Lepidoptera, Hesperiidae. This holoferritin is stable to heat (75°C) or in the presence of SDS, proteinase K, or urea, has an Mr above 600,000, contains iron and resembles mammalian ferritins in appearance by electron microscopy. Calpodes ferritin is a glycoprotein having N-linked high-mannose oligosaccharides. It is not antigenically related to horse ferritin but is related to that from Manduca sexta , Lepidoptera, Sphingidae. In its native form, Calpodes ferritin has only 3 isoforms with a pI 6.5–7 suggesting a more uniform subunit composition than that in vertebrates. It has two principle subunits, with relative Mrs of 24,000 (L) and 31,000 (G) and two minor subunits with Mrs of 26,000 and 28,000 all of which cross-react with antibody to Manduca ferritin. The 24 kDa subunit is the only one that is not glycosylated. Iron injections induce an increase in the proportion of the 24 kDa subunit. We conclude that Calpodes has ferritin and that it is glycosylated like mammalian serum ferritin.
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Secreted ferritin subunits are of two kinds in insects molecular cloning of cDNAs encoding two major subunits of secreted ferritin from Calpodes ethlius.
Insect Biochemistry and Molecular Biology, 1999Co-Authors: Helen Nichol, Michael LockeAbstract:Abstract In insects, holoferritin is easily visible in the vacuolar system of tissues that filter the hemolymph and, at least in Lepidoptera, is abundant in the hemolymph. Sequences reported for insect secreted ferritins from Lepidoptera and Diptera have high sequence diversity. We examined the nature of this diversity for the first time by analyzing sequences of cDNAs encoding two ferritin subunits from one species, Calpodes ethlius (Lepidoptera, Hesperiidae). We found that insect secreted ferritin subunits are of two types with little resemblance to each other. Ferritin was isolated from iron loaded hemolymph of C. ethlius fifth instar larvae by differential centrifugation. The N-terminal amino acid sequences for the nonglycosylated subunit with Mr 24,000 (S) and the largest glycosylated subunit with Mr 31,000 (G) were determined. The N-termini of the two subunits were different and were used to construct degenerate PCR primers. The same cDNA products were amplified from cDNA libraries from the midgut which secretes holoferritin and from the fat body which secretes iron-poor apoferritin. The G subunit most closely resembles the glycosylated ferritin subunit from Manduca sexta and the S subunit resembles the Drosophila small subunit. The S and G subunits from Calpodes were dissimilar and distinct from the cytosolic ferritins of vertebrates and invertebrates. Additional sequences were obtained by 5′ and 3′ RACE from separate fat body and midgut RACE libraries. cDNAs encoding both subunits had a consensus iron responsive element (IRE) in a conserved cap-distal location of their 5′ UTR. An integrin-binding RGD motif found in the G subunit and conserved in Manduca may facilitate iron uptake through a calreticulin (mobilferrin)/integrin pathway. Calpodes and other insect ferritins have conserved cysteine residues to which fatty acids can be linked. Dynamic acylation of ferritin may slow but not prevent its passage out of the ER.
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The origin, transport and cleavage of the molt-associated cuticular protein CECP22 from Calpodes ethlius (Lepidoptera, Hesperiidae).
Journal of Insect Physiology, 1999Co-Authors: Oana Marcu, Michael LockeAbstract:CECP22 (Calpodes ethlius Cuticular Protein 22 kDa) is a molt associated protein found in the cuticle of C. ethlius larvae and pupae. The mRNA for the CECP22 cuticular protein is expressed in the epidermis and fat body during the intermolt. The protein itself accumulates in intermolt hemolymph, but at molting, when the cuticle is being digested, it is also found in the cuticle of surface integument, tracheae, foregut and hindgut and in the molting fluid. CECP22 exists in two forms. The large form (19.17 kDa, pI 6.2) becomes smaller (16.1 kDa, pI 7.4) by cleavage at the proteolytic cleavage site (position 170) with amidation of the C-terminal. The small, more basic peptide, appears only at molting, first in the cuticle and then in the molting fluid. It is presumed to be the active form of an amidase involved in the earliest stages of cuticle degradation. The inactive form accumulates in the hemolymph during the long intermolt and probably represents an abundant source of precursor enzyme that can be provided to all cuticle containing organs for a precise initiation of cuticle degradation.
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A cuticular protein from the moulting stages of an insect
Insect Biochemistry and Molecular Biology, 1998Co-Authors: Oana Marcu, Michael LockeAbstract:A 22 kDa peptide was purified from prepupal cuticles of 5th instar Calpodes ethlius caterpillars. It was absent earlier in the stadium and from the egg and adult, i.e. it is related to cuticle turnover rather than cuticle structure. It was present at larval and metamorphic moults, showing that it is related to moulting not just metamorphosis. The cDNA corresponding to the 22 kDa peptide was isolated by antibody screening of an epidermal cDNA expression library. Hybridization to Calpodes genomic DNA showed that the gene was present as a single copy. The deduced amino acid sequence is not like any of the sequences of cuticular structural proteins that have been published, but has a 47 amino acid sequence similar to bacteriophage T7 N-acetylmuramoyl-L-alanine amidase (34% identical, 51% similar). The amino acid sequence, the timing of expression in development, and the similarity between the substrate of the bacteriophage amidase and components of insect cuticle, all suggest that the 22 kDa protein may have a role in cleaving chitin-peptide bonds as a prerequisite for digestion of the cuticle by chitinases and proteases.
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Integument and hemocyte peptides
Journal of Insect Physiology, 1994Co-Authors: Miklós Sass, Agnes Kiss, Michael LockeAbstract:Abstract There are four routing classes of integument peptide in the caterpillar of Calpodes ethlius. The epidermis secretes peptides apically into the cuticle (C), basally into the hemolymph (H) and in both directions (BD). Peptides in a 4th class (T), are presumed to be transported across the epidermis, because the epidermis does not synthesize them although they occur in both cuticle and hemolymph. In a search for the origin of the presumed transepidermal peptides we found that hemocytes contain some peptides from all four routing classes. Peptides prepared from washed hemocytes reacted in immunoblots to antibodies against integument peptides prepared from hemolymph and cuticle. These peptides are probably synthesized by hemocytes because they matched those from medium containing [35S]methionine in which hemocytes had been incubated. Calpodes hemolymph contains four hemocyte types. Immunogold labelling localized integument peptides in the secretory pathway of granulocytes and spherulocytes and in the cytosol of oenocytoids but not in plasmatocytes. Each peptide was localized in a particular kind or kinds of hemocyte. Granulocyte secretory vesicles reacted with antibodies to C180, C55 and BD82 kDa peptides. Spherulocytes secretory vesicles reacted with antibodies to C180, C55, BD89, BD82 and a 78 kDa peptide presumed to be the precursor of T66. Oenocyotoids reacted with antibodies to H45, 38, 32, 23 and BD89 kDa peptides. Spherulocytes were the only tissue to react with antibodies to the T66 kDa peptide that is found abundantly in cuticle and hemolymph. Spherulocytes are therefore presumed to secrete the 66 kDa peptide into the hemolymph from where it is transported to the cuticle. The C180 and C55 kDa peptides do not occur in hemolymph. Their presence in granulocytes and spherulocytes may be associated with hemocyte functions such as basal lamina formation, since immunogold localized them in that part of the basal lamina next to the hemolymph, as would be expected if hemocytes deposited components onto the exposed hemolymph surface. The presence of hemolymph peptides in oenocytoids is more difficult to interpret, since the antigenic reactions are localized in the cytosol rather than in the secretory pathway expected for exported proteins. We conclude that integument peptides are not secreted only by the epidermis, nor is the cuticle their only destination.
Stanley Caveney - One of the best experts on this subject based on the ideXlab platform.
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Unusual Life History Characteristics of Elachertus scutellatus Howard (Hymenoptera: Eulophidae), a Koinobionic Ectoparasitoid
Environmental Entomology, 2004Co-Authors: Kimberley E. Macdonald, Stanley CaveneyAbstract:Elachertus scutellatus Howard is a synovigenic, koinobionic ectoparasitoid that preys on the Brazilian skipper caterpillar, Calpodes ethlius (Stoll) (Lepidoptera: Hesperiidae). This wasp exhibits a rare combination of life history strategies, some associated with being a koinobiont and others with being ectoparasitic. The female wasp lays large, inflexible, anhydropic eggs that are passed externally down the ovipositor. This process is uncommon and is considered the morphological intermediate between the use of the ovipositor as an egg-laying device and a stinger. The average clutch size and the oviposition frequency of E. scutellatus females are comparable with other wasps in the Eulophidae. Female wasps were observed to be nonconcurrent host-feeders. The sex ratios of E. scutellatus broods were consistently female biased. Adult male wasps lived longer than female wasps, which may have been a result of host size or the rearing technique used. E. scutellatus has potential as a biocontrol agent because of its female-biased sex ratios, destructive host-feeding, and synovigeny.
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EXTERNAL MORPHOLOGY AND DEVELOPMENT OF IMMATURE STAGES OF ELACHERTUS SCUTELLATUS (HYMENOPTERA: EULOPHIDAE) IN FLORIDA: THE FIRST NORTH AMERICAN RECORD
Florida Entomologist, 2004Co-Authors: Kimberley E. Macdonald, Stanley CaveneyAbstract:The first North American record for Elachertus scutellatus, a parasitoid of Calpodes ethlius Stoll, occurred August 1999, in Florida. A simple rearing protocol was established to allow the morphology and development of this wasp to be examined. The egg and larval morphology and development of E. scutellatus resemble other Elachertus species. The freshly-ecdysed pupa, on the other hand, is rare among parasitoids in that it secretes a fluid from its anus which, when dry, fastens the pupa to its substrate. The death of the colony after eight months has many possible explanations including a laboratory-induced castration, inappropriate food source(s), and pathogenic infection.
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Insecticidal activity of glufosinate through glutamine depletion in a caterpillar.
Pest Management Science, 2001Co-Authors: Nicole J Kutlesa, Stanley CaveneyAbstract:The herbicide glufosinate-ammonium (GLA) is a competitive inhibitor of glutamine synthetase (GS), an enzyme converting glutamate to glutamine in both plants and animals. Because GS is essential for ammonia detoxification in plants, GLA treatment disrupts photorespiration by causing a build-up of ammonia and a loss of glutamine in plant tissues. This study reports that GLA applied to leaf surfaces is also toxic to 5th-instar caterpillars of the skipper butterfly Calpodes ethlius (LD50 = 400 mg kg-1). After ingesting GLA, caterpillars stopped feeding and became dehydrated through a loss of rectal function. Caterpillars showed symptoms of neurotoxicity, such as proleg tremors, body convulsions and complete paralysis before death. Incubation of several tissues isolated from normal feeding-stage caterpillars with the GS substrates glutamate and ammonium showed that GLA inhibited GS activity in vitro. Within 24 h of ingesting GLA, caterpillars had a greatly reduced glutamine content and the ammonium ion levels had more than doubled. Injection of ammonium chloride into non-GLA-treated caterpillars had no deleterious effect, suggesting that glutamine depletion, and not a rise in body ammonium, was the primary cause of GLA toxicity following GS inhibition. This was supported by the observation that the onset of the symptoms of GLA poisoning could be postponed by giving GLA-fed caterpillars several subsequent daily injections of glutamine. The effective GLA dose fed to 5th-instar caterpillars in this study was comparable to the amount that might realistically by acquired from feeding on GLA-treated crops.
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l glutamate retrieved with the moulting fluid is processed by a glutamine synthetase in the pupal midgut of Calpodes ethlius
Journal of Insect Physiology, 2000Co-Authors: C Yarema, H Mclean, Stanley CaveneyAbstract:From apolysis until pupal ecdysis, the pharate pupa of the Brazilian Skipper (Calpodes ethlius) lies wrapped in a prepupal shell composed of the larval cuticle and an ecdysial space (ES) filled with enzyme-rich moulting fluid (MF). In the 4h before ecdysis the pharate pupa drinks the moulting fluid through its mouth and anus, and transfers the cuticular degradation products to its midgut (MG). At the same time, extra fluid passes across the body wall of the pharate pupa and flushes out the ES. The MF is recovered at an overall rate of 70µl/h and reabsorbed across the pharate pupal midgut at about 26µl/h. L-Glutamate was found to be the dominant amino acid in the moulting fluid. Total MF glutamate peaked at 850nmol about 8h before pupal ecdysis (P-8), but by ecdysis it had dropped to nearly zero as the MF became diluted with new fluid and was consumed. The drop in glutamate in the ES coincided with a rise in the glutamine content of the fluid in the midgut lumen. The highest rate of glutamine synthesis occurred in midguts isolated from pharate pupae actively drinking MF (Psynthetase (GS) was found to be active in glutamate metabolism in the pharate pupal midgut. Glutamine synthesis in the midgut was L-glutamate-dependent and inhibited by two selective competitive inhibitors of GS activity, L-methionine sulfoximine (MSO) and glufosinate ammonium (GLA). Injection of GS inhibitors into the prepupal ES greatly reduced the glutamine content of the midgut epithelium by P+24. Although a corresponding increase in midgut glutamate levels was not seen, midgut serine levels in treated animals rose, suggesting that GS inhibitors shunted the MF-derived glutamate along an alternative metabolic pathway. GLA was much more toxic to pupae than MSO. Midgut GS appears to play a central role in the recycling of L-glutamate across the pupal MG epithelium at pupation.
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l-Glutamate retrieved with the moulting fluid is processed by a glutamine synthetase in the pupal midgut of Calpodes ethlius
Journal of Insect Physiology, 2000Co-Authors: C Yarema, H Mclean, Stanley CaveneyAbstract:From apolysis until pupal ecdysis, the pharate pupa of the Brazilian Skipper (Calpodes ethlius) lies wrapped in a prepupal shell composed of the larval cuticle and an ecdysial space (ES) filled with enzyme-rich moulting fluid (MF). In the 4h before ecdysis the pharate pupa drinks the moulting fluid through its mouth and anus, and transfers the cuticular degradation products to its midgut (MG). At the same time, extra fluid passes across the body wall of the pharate pupa and flushes out the ES. The MF is recovered at an overall rate of 70µl/h and reabsorbed across the pharate pupal midgut at about 26µl/h. L-Glutamate was found to be the dominant amino acid in the moulting fluid. Total MF glutamate peaked at 850nmol about 8h before pupal ecdysis (P-8), but by ecdysis it had dropped to nearly zero as the MF became diluted with new fluid and was consumed. The drop in glutamate in the ES coincided with a rise in the glutamine content of the fluid in the midgut lumen. The highest rate of glutamine synthesis occurred in midguts isolated from pharate pupae actively drinking MF (P
C Yarema - One of the best experts on this subject based on the ideXlab platform.
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l glutamate retrieved with the moulting fluid is processed by a glutamine synthetase in the pupal midgut of Calpodes ethlius
Journal of Insect Physiology, 2000Co-Authors: C Yarema, H Mclean, Stanley CaveneyAbstract:From apolysis until pupal ecdysis, the pharate pupa of the Brazilian Skipper (Calpodes ethlius) lies wrapped in a prepupal shell composed of the larval cuticle and an ecdysial space (ES) filled with enzyme-rich moulting fluid (MF). In the 4h before ecdysis the pharate pupa drinks the moulting fluid through its mouth and anus, and transfers the cuticular degradation products to its midgut (MG). At the same time, extra fluid passes across the body wall of the pharate pupa and flushes out the ES. The MF is recovered at an overall rate of 70µl/h and reabsorbed across the pharate pupal midgut at about 26µl/h. L-Glutamate was found to be the dominant amino acid in the moulting fluid. Total MF glutamate peaked at 850nmol about 8h before pupal ecdysis (P-8), but by ecdysis it had dropped to nearly zero as the MF became diluted with new fluid and was consumed. The drop in glutamate in the ES coincided with a rise in the glutamine content of the fluid in the midgut lumen. The highest rate of glutamine synthesis occurred in midguts isolated from pharate pupae actively drinking MF (Psynthetase (GS) was found to be active in glutamate metabolism in the pharate pupal midgut. Glutamine synthesis in the midgut was L-glutamate-dependent and inhibited by two selective competitive inhibitors of GS activity, L-methionine sulfoximine (MSO) and glufosinate ammonium (GLA). Injection of GS inhibitors into the prepupal ES greatly reduced the glutamine content of the midgut epithelium by P+24. Although a corresponding increase in midgut glutamate levels was not seen, midgut serine levels in treated animals rose, suggesting that GS inhibitors shunted the MF-derived glutamate along an alternative metabolic pathway. GLA was much more toxic to pupae than MSO. Midgut GS appears to play a central role in the recycling of L-glutamate across the pupal MG epithelium at pupation.
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l-Glutamate retrieved with the moulting fluid is processed by a glutamine synthetase in the pupal midgut of Calpodes ethlius
Journal of Insect Physiology, 2000Co-Authors: C Yarema, H Mclean, Stanley CaveneyAbstract:From apolysis until pupal ecdysis, the pharate pupa of the Brazilian Skipper (Calpodes ethlius) lies wrapped in a prepupal shell composed of the larval cuticle and an ecdysial space (ES) filled with enzyme-rich moulting fluid (MF). In the 4h before ecdysis the pharate pupa drinks the moulting fluid through its mouth and anus, and transfers the cuticular degradation products to its midgut (MG). At the same time, extra fluid passes across the body wall of the pharate pupa and flushes out the ES. The MF is recovered at an overall rate of 70µl/h and reabsorbed across the pharate pupal midgut at about 26µl/h. L-Glutamate was found to be the dominant amino acid in the moulting fluid. Total MF glutamate peaked at 850nmol about 8h before pupal ecdysis (P-8), but by ecdysis it had dropped to nearly zero as the MF became diluted with new fluid and was consumed. The drop in glutamate in the ES coincided with a rise in the glutamine content of the fluid in the midgut lumen. The highest rate of glutamine synthesis occurred in midguts isolated from pharate pupae actively drinking MF (P
Dolder H. - One of the best experts on this subject based on the ideXlab platform.
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Sperm Morphology And Arrangement Along The Male Reproductive Tract Of The Butterfly Euptoieta Hegesia (insecta: Lepidoptera)
2015Co-Authors: Mancini K., Dolder H.Abstract:The present study was undertaken to describe the morphological and organizational modifications that occur in apyrene and eupyrene spermatozoa along the male adult reproductive tract of the butterfly, Euptoieta hegesia. Testis, vas deferens, vesicula seminalis and ductus ejaculatorius were studied by transmission electron microscopy. In the testis, both sperm types are organized into cysts; apyrene sperm are devoid of extracellular structures while eupyrene ones have lacinate and reticular appendages. In the testis basal region, both sperm pass through an epithelial barrier and lose their cystic envelope. The eupyrene morphological and organizational modifications are more drastic than the apyrene ones. From the vas deferens to the ductus ejaculatorius, apyrene sperm are dispersed in the lumen and acquire several concentric layers that are formed by the folding of their abundant cell membrane. The apyrene distribution observed here suggests that their functions include eupyrene transportation. Eupyrene sperm, however, remain aggregated along the tract. In the vas deferens, they are covered by a filamentous material that develops into a homogeneous matrix surrounding the spermatozoa coat in the vesicula seminalis and the ductus ejaculatorius. Eupyrene sperm undergo complex morphological changes that include the loss of lacinate appendages and the formation of a dense and heterogeneous extracellular coat. The formation of the matrix and the coat in eupyrene extratesticular sperm is related to the loss of lacinate appendages. These changes are in general extracellular and are probably important for sperm maturation.4402/03/15107117Bebas, P., Cymborowski, B., Giebultowicz, J.M., Circadian rhythm of sperm release in males of the cotton leafworm, Spodoptera littoralis: In vivo and in vitro studies (2001) J. 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Morphol., 138, pp. 121-129Friedlander, M., Jeshtadi, A., Reynolds, S.E., The structural mechanism of trypsin-induced intrinsic motility in Manduca sexta spermatozoa in vitro (2001) J. Insect Physiol., 47, pp. 245-255Friedländer, M., Miesel, S., Spermatid enucleation during the normal atypical spermiogenesis of the warehouse moth Ephestia cautella (1977) J. Submicrosc. Cytol., 9, pp. 173-185Garvey, L.K., Gutierrez, G.M., Krider, H.M., Ultrastructure and morphogenes is of the apyrene and eupyrene spermatozoa in the Gypsy moth (Lepidoptera: Lymantriidae) (2000) Ann. Entomol. Soc. Am., 93, pp. 1147-1155Giebultowicz, J.M., Bell, R.A., Imberski, R.B., Circadian rhythm of sperm movement in the male reproductive tract of the gypsy moth, Lymantria dispar (1988) J. Insect Physiol., 34, pp. 527-532Giebultowicz, J.M., Blackburn, M.B., Thomas-Laemont, P.A., Weyda, F., Raina, A.K., Daily rhythm in myogenic contractions of vas deferens associated with sperm release cycle in a moth (1996) J. Comp. 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Develop., 34, pp. 259-269LaChance, L.E., Richard, R.D., Ruud, R.L., Movement of eupyrene sperm bundles from the testis and storage in the ductus ejaculatorius duplex of the male pink bollworm: Effects of age, strain, irradiation, and light (1977) Ann. Entomol. Soc. Am., 70, pp. 647-651Lai-Fook, J., Structural comparison between eupyrene and apyrene spermiogenesis in Calpodes ethlius (Hesperiidae: Lepidoptera) (1982) Can. J. Zool., 60, pp. 1216-1230Lai-Fook, J., The vasa deferentia of the male reproductive system of Calpodes ethlius (Hesperiidae: Lepidoptera) (1982) Can. J. 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Anat., 56, pp. 553-606Osanai, M., Kasuga, H., Aigaki, T., Physiological role of apyrene spermatozoa of Bombyx mori (1987) Experientia, 43, pp. 593-596Osanai, M., Kasuga, H., Aigaki, T., Spermatophore and its structural changes with time in bursa copulatrix of the silkworm, Bombyx mori (1987) J. Morphol., 193, pp. 1-11Phillips, D.M., Insect sperm: Their structure and morphogenesis (1970) J. Cell Biol., 44, pp. 243-277Phillips, D.M., Morphogenesis of the lacinate appendages of Lepidopteran spermatozoa (1971) J. Ultrastruct. Res., 34, pp. 567-585Riemann, J.G., Metamorphosis of the cabbage looper Trichoplusia ni during passage from the testis to the female spermatheca (1970) Comparative Spermatology, pp. 321-331. , B. Baccetti (ed.), Academic Press, New YorkRiemann, J.G., Gassner, G., Ultrastructure of Lepidopteran sperm within spermathecae (1973) An. Entomol. Soc. Am., 66, pp. 154-159Riemann, J.G., Giebultowicz, J.M., Secretion in the upper vas deferens of the gypsy moth correlated with the circadian rhythm of sperm release from the testes (1991) J. Insect Physiol., 37, pp. 53-62Riemann, J.G., Giebultowicz, J.M., Sperm maturation in the vasa deferentia of the gypsy moth, Lymantria dispar L. (Lepidoptera: Lymantriidae) (1992) Int. J. Insect Morphol. Embryol., 21, pp. 271-284Riemann, J.G., Ruud, R.L., Mediterranean flour moth: Effects of continuous light on the reproductive capacity (1974) Ann. Entomol. Soc. Am., 67, pp. 857-860Riemann, J.G., Thorson, B.J., Sperm maturation in the male and female genital tracts of Anagasta kuhniella (Lepidoptera: Pyralididae) (1971) Int. J. Insect Morphol. Embryol., 1, pp. 11-19Riemann, J.G., Thorson, B.J., Ultrastructure of the vasa deferentia of the Mediterranean flour moth (1976) J. Morphol., 129, pp. 483-506Riemann, J.G., Thorson, B.J., Ruud, R.L., Daily cycle of release of sperm from the testes of Mediterranean flour moth (1974) J. Insect Physiol., 20, pp. 195-207Scott, J.E., Haigh, M., Nusgens, B., Lapière, C.M., Proteoglycan: Collagen interactions in dermasparacti skin and tendon. An electron histochemical study using cupromeronic blue in a critical electrolyte concentration method (1989) Matrix, 9, pp. 437-442Seth, R.K., Rao, D.K., Reynolds, S.E., Movement of spermatozoa in the reproductive tract of adult male Spodoptera litura: Daily rhythm of sperm descent and the effect of light regime on male reproduction (2002) J. Insect Physiol., 48, pp. 119-131Silberglied, R.E., Shepherd, J.G., Dickinson, J.L., Eunuchs: The role of apyrene sperm in lepidoptera? (1984) Am. Nat., 123, pp. 255-265Snook, R.R., Is the production of multiple sperm types adaptive? (1997) Evolution, 51, pp. 797-808Snook, R.R., The risk of sperm competition and the evolution of sperm heteromorphism (1998) Anim. Behav., 56, pp. 1497-1507Sonnenschein, M., Hauser, C.L., Presence of only eupyrene spermatozoa in adult males of the genus Micropteryx Hubner and its phylogenetic significance (1990) Int. J. Insect Morphol. Embryol., 19, pp. 269-276Wedell, N., Cook, P.A., Butterflies tailor their ejaculate in response to sperm competition risk and intensity (1999) Proc. Royal Soc. London B, 266, pp. 1033-1039Zylberberg, L., Contribution a l'étude de la double spermatogenèse chez un lépdoptère (Pieris brassicae L., Pieridae) (1969) Ann. Sci. Nat., Zool., 11, pp. 569-62
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Ultrastructure Of Apyrene And Eupyrene Spermatozoa From The Seminal Vesicle Of Euptoieta Hegesia (lepidoptera: Nymphalidae)
2015Co-Authors: Mancini K., Dolder H.Abstract:The ultrastructure of the seminal vesicle's spermatozoa of the butterfly Euptoieta hegesia was analyzed. The apyrene spermatozoa measure about 300 μm in length and swim freely in a secretion. The anterior end consists in a cap with a cylindrical extension and a globular structure. The flagellum has a 9+9+2 axoneme, two mitochondrial derivatives with paracrystalline matrices and an external coat formed by concentric layers. The eupyrene spermatozoa measure about 550 μm in length and are grouped into bundles. The anterior end consists in an amorphous globule. Posterior to this globule, a coat with a dense material covers the spermatozoon where an acrosome and a nucleus appear. The flagellum has a 9+9+2 axoneme and two mitochondrial derivatives. External to the coat and attached to the dense material, there is a reticular appendage, which has a paracrystalline core and extends to the distal tip of the spermatozoon. © 2001 Harcourt Publishers Ltd.333301308Behnke, O., Forer, A., Evidence for four classes of microtubules in individual cells (1967) J. Cell Sci., 2, pp. 169-192Cook, P.A., Wedell, N., Non-fertile sperm delay female remating (1999) Nature, 397, p. 486Dallai, R., Afzelius, B.A., Microtubular diversity in insect spermatozoa: Results obtained with a new fixative (1990) J. Struct. Biol., 103, pp. 164-179Friedländer, M., Phylogenetic branching of trichoptera and lepidoptera - An ultrastructural analysis on comparative spermatology (1983) J. Ultrastruct. Res., 83, pp. 141-147Friedländer, M., Gitay, H., The fate of the normal anucleated spermatozoa in inseminated female of the silkworm Bombyx mori (1972) J. Morphol., 138, pp. 121-129Friedländer, M., Miesel, S., Spermatid anucleation during the normal atypical spermiogenesis of the warehouse moth Ephestia cautella (1977) J. Submicrosc. Cytol., 9, pp. 173-185Gage, M.J.G., Associations between body size, mating pattern, testis size and sperm lengths across butterflies (1994) Proc. R. Soc. Lond. B, 258, pp. 247-254Gatenby, J.B., Tahmisian, T.N., Centriole adjunct, centriole, mitochondria and ergastoplasm in orthopteran spermatogensis. An electron microscopic study (1959) La Cellule, 60, pp. 103-134Jamieson, B.G.M., (1987) The Ultrastructure and Phylogeny of Insect Spermatozoa, , Cambridge University Press, CambridgeJamieson, B.G.M., Dallai, R., Afzelius, B.A., Insects: Their spermatozoa and phylogeny (1999), Science Publishers, Enfield, NHKubo-Irie, M., Irie, M., Nakazawa, T., Mohri, H., Morphological changes in apyrene and eupyrene spermatozoa in the reproductive tract of the male butterfly Atrophaneura alcinous (1998) Klug. Invert. Reprod. Dev., 34, pp. 259-269Lai-Fook, J., Structural comparision between eupyrene and apyrene spermiogenesis in Calpodes ethlius (Hesperiidae: Lepidoptera) (1982) Can. J. Zool., 60, pp. 1216-1230Leviatan, R., Friedländer, M., The eupyrene-apyrene dichotomous spermatogenesis of lepidoptera. I. The relationship with postembryonic development and the role of the decline in juvenile hormone titer toward pupation (1979) Develop. Biol., 68, pp. 515-524Lino-Neto, J., Báo, S.N., Dolder, H., Structure and ultrastructure of the spermatozoa of Bephratelloides pomorum (Fabricius) (Hymenoptera: Eurytomidae) (1999) Int. J. Insect Morphol. Embryol., 28, pp. 253-259Lino-Neto, J., Báo, S.N., Dolder, H., Structure and ultrastructure of the spermatozoa of Trichogramma pretiosum riley and Trichogramma atopovirilia Oatman and Platner (Hymenoptera: Trichogrammatidae) (2000) Acta Zool. (Stockh.), 81, pp. 205-211Lino-Neto, J., Báo, S.N., Dolder, H., Sperm ultrastructure of the honey bee (Apis mellifera) (L) (Hymenoptera, Apidae) with emphasis on the nucleus-flagellum transition region (2000) Tissue & Cell, 32, pp. 322-327Medeiros, M., Caracterização ultra-estrutural de espermatozóides eupirenes e apirenes de Alabama argillacea Hübner, 1818 (Lepidoptera: Noctuidae), ao nível dos testículos e das vias genitais de imagos machos e fêmeas até a espermateca (1986), Tese (Mestrado). Instituto de Biologia, Universidade Estadual de CampinasMedeiros, M., Estudo ultra-estrutural da espermiogênese dicotômica de Alabama argillacea Hübner, 1818 (1997), Tese (doutorado). Instituto de Biociências, Universidade Estadual de São PauloMedeiros, M., Silveira, M., Ultrastructural study of apyrene spermatozoa of Alabama argillacea (Insecta, Lepidoptera, Noctuidae) with tannic acid containing fixative (1996) J. Submicros. Cytol. Pathol., 28, pp. 133-140Morrow, E.H., Gage, M.J.G., The evolution of sperm length in moths (2000) Proc. R. Soc. Lond. B, 267, pp. 307-313Phillips, D.M., Insect sperm: Their structure and morphogenesis (1970) J. Cell Biol., 44, pp. 243-277Phillips, D.M., Morphogenesis of the lacinate appendages of lepidopteran spermatozoa (1971) J. Ultrastruct. Res., 34, pp. 567-585Riemann, J.G., Giebultowicz, J.M., Sperm maturation in the vasa deferentia of the gypsy moth, Lymantria dispar L. (Lepidoptera: Lymantriidae) (1992) Int. J. Insect Morphol. & Embriol., 21, pp. 271-284Silberglied, R.E., Shepherd, J.G., Dickinson, J.L., Eunuchs: The role of apyrene sperm in Lepidoptera? (1984) Am. Nat., 123, pp. 255-265Sonnenschein, M., Hauser, C.L., Presence of only eupyrene spermatozoa in adult males of the genus Micropteryx Hübner and its phylogenetic significance (1990) Int. J. Insect Morphol. & Embryol., 19, pp. 269-276Snook, R.R., Is the production of multiple sperm types adaptive? (1997) Evolution, 51, pp. 797-808Snook, R.R., The risk of sperm competition and the evolution of sperm heteromorphism (1998) An. Behav., 56, pp. 1497-1507(1998) Técnicas Básicas de Microscopia Electrônica Aplicada às Ciências Biológicas, , Souza, W., ed.Sociedade Brasileira de MicroscopiaWedell, N., Cook, P.A., Butterflies tailor their ejaculate in response to sperm competition risk and intensity (1999) Proc. R. Soc. Lond. B, 266, pp. 1033-103
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Immunocytochemical Localization Of Tubulins In Spermatids And Spermatozoa Of Euptoieta Hegesia (lepidoptera: Nymphalidae)
2015Co-Authors: Mancini K., Bao S.n., Fernandes A.p., Dolder H.Abstract:A comparative analysis of the distribution of tubulin types in apyrene and eupyrene sperm of Euptoieta hegesia butterflies was carried out, also verifying the presence of tubulin in lacinate appendages of the eupyrene sperm. Ultrathin sections of LR White embedded spermatids and spermatozoa were labeled for alpha, beta, gamma, alpha-acetylated and alpha-tyrosinated tubulins. Apyrene and eupyrene spermatids show the same antibody recognition pattern for tubulins. All tubulin types were detected in axonemal microtubules. Alpha and gamma tubulins were also detected on the cytoplasmic microtubules. However, for beta and tyrosinated tubulins only scattered labeling was detected on cytoplasmic microtubules and acetylated tubulin was not detected. In apyrene and eupyrene spermatozoa only the axoneme labeling was analyzed since cytoplasmic microtubules no longer exist in these cells. Alpha, beta and tyrosinated tubulins were easily detected on the apyrene and eupyrene axoneme; gamma tubulin was strongly marked on eupyrene axonemes but was scattered on the apyrene ones. Acetylated tubulin appeared with scattered labeling on the axoneme of both sperm types. Our results demonstrate significant differences in tubulin distribution in apyrene and eupyrene axonemal and cytoplasmic microtubules. Extracellular structures, especially the lacinate appendages, were not labeled by antibodies for any tubulin. © 2004 Elsevier Ltd. 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H Mclean - One of the best experts on this subject based on the ideXlab platform.
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l glutamate retrieved with the moulting fluid is processed by a glutamine synthetase in the pupal midgut of Calpodes ethlius
Journal of Insect Physiology, 2000Co-Authors: C Yarema, H Mclean, Stanley CaveneyAbstract:From apolysis until pupal ecdysis, the pharate pupa of the Brazilian Skipper (Calpodes ethlius) lies wrapped in a prepupal shell composed of the larval cuticle and an ecdysial space (ES) filled with enzyme-rich moulting fluid (MF). In the 4h before ecdysis the pharate pupa drinks the moulting fluid through its mouth and anus, and transfers the cuticular degradation products to its midgut (MG). At the same time, extra fluid passes across the body wall of the pharate pupa and flushes out the ES. The MF is recovered at an overall rate of 70µl/h and reabsorbed across the pharate pupal midgut at about 26µl/h. L-Glutamate was found to be the dominant amino acid in the moulting fluid. Total MF glutamate peaked at 850nmol about 8h before pupal ecdysis (P-8), but by ecdysis it had dropped to nearly zero as the MF became diluted with new fluid and was consumed. The drop in glutamate in the ES coincided with a rise in the glutamine content of the fluid in the midgut lumen. The highest rate of glutamine synthesis occurred in midguts isolated from pharate pupae actively drinking MF (Psynthetase (GS) was found to be active in glutamate metabolism in the pharate pupal midgut. Glutamine synthesis in the midgut was L-glutamate-dependent and inhibited by two selective competitive inhibitors of GS activity, L-methionine sulfoximine (MSO) and glufosinate ammonium (GLA). Injection of GS inhibitors into the prepupal ES greatly reduced the glutamine content of the midgut epithelium by P+24. Although a corresponding increase in midgut glutamate levels was not seen, midgut serine levels in treated animals rose, suggesting that GS inhibitors shunted the MF-derived glutamate along an alternative metabolic pathway. GLA was much more toxic to pupae than MSO. Midgut GS appears to play a central role in the recycling of L-glutamate across the pupal MG epithelium at pupation.
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l-Glutamate retrieved with the moulting fluid is processed by a glutamine synthetase in the pupal midgut of Calpodes ethlius
Journal of Insect Physiology, 2000Co-Authors: C Yarema, H Mclean, Stanley CaveneyAbstract:From apolysis until pupal ecdysis, the pharate pupa of the Brazilian Skipper (Calpodes ethlius) lies wrapped in a prepupal shell composed of the larval cuticle and an ecdysial space (ES) filled with enzyme-rich moulting fluid (MF). In the 4h before ecdysis the pharate pupa drinks the moulting fluid through its mouth and anus, and transfers the cuticular degradation products to its midgut (MG). At the same time, extra fluid passes across the body wall of the pharate pupa and flushes out the ES. The MF is recovered at an overall rate of 70µl/h and reabsorbed across the pharate pupal midgut at about 26µl/h. L-Glutamate was found to be the dominant amino acid in the moulting fluid. Total MF glutamate peaked at 850nmol about 8h before pupal ecdysis (P-8), but by ecdysis it had dropped to nearly zero as the MF became diluted with new fluid and was consumed. The drop in glutamate in the ES coincided with a rise in the glutamine content of the fluid in the midgut lumen. The highest rate of glutamine synthesis occurred in midguts isolated from pharate pupae actively drinking MF (P
