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L Schoofs

Publications and source records attributed to L Schoofs.

At least 91 records · Page 5Linked to original sources
PubMed1992

Isolation and primary structure of two sulfakinin-like peptides from the fleshfly, Neobellieria bullata.

1. Two novel insect myotropic peptides termed neosulfakinin-I (Neb-SK-I) and neosulfakinin-II (Neb-SK-II) were isolated from the heads of 42 thousand fleshflies, Neobellieria bullata (Diptera, Sarcophagidae). 2. A series of four, high-performance liquid chromatographic (HPLC), fractionations performed on columns with different characteristic features yielded two purified biologically active, hindgut motility stimulating fractions, suitable for amino acid sequence analysis. 3. The proposed sequences for the two peptides are: Phe-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-(NH2), (Neb-SK-I) and X-X-Glu-Glu-Gln-Phe-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-(NH2), (Neb-SK-II). 4. These sulfakinins exhibit very high homology to putative drosulfakinin sequences which, however, have not yet been isolated, but were deduced from a cloned Drosophila gene encoding these peptides. 5. Here we provide the first evidence for the expression of such peptides present in Dipterans. 6. Insect sulfakinins show structural identities with the hormonally-active portion of vertebrate gastrin II-, cholecystokinin- and caerulin-related peptides and they share common carboxy terminal sequences with invertebrate/vertebrate peptides of the FMRFamide peptide family.

Amino Acid Sequence↗
PubMed1991

Isolation, identification and synthesis of locustamyoinhibiting peptide (LOM-MIP), a novel biologically active neuropeptide from Locusta migratoria.

A novel peptide termed locustamyoinhibiting peptide (LOM-MIP) was isolated from brain-corpora cardiaca-corpora allata-suboesophageal ganglion extracts of the locust, Locusta migratoria. The primary structure of this nonapeptide has been determined Ala-Trp-Gln-Asp-Leu-Asn-Ala-Gly-Trp-NH2. LOM-MIP suppresses the spontaneous contractions of the hindgut and oviduct of Locusta migratoria and of the hindgut of Leucophaea maderae. This novel peptide is, however, structurally different from leucomyosuppressin, a hindgut suppressing peptide isolated from Leucophaea maderae heads. LOM-MIP has a Gly-TrpNH2 carboxy-terminal in common with APGWamide, a penis retractor muscle inhibiting peptide isolated from the snail, Lymnea stagnalis. In addition, it shows carboxy-terminal sequence similarities with locust AKH II which ends in AGWamide. No sequence similarities were found with other vertebrate or invertebrate peptides. Synthetic LOM-MIP showed biological as well as chemical characteristics indistinguishable from those of native LOM-MIP.

Amino Acid Sequence↗
PubMed1991

Isolation, primary structure, and synthesis of locustapyrokinin: a myotropic peptide of Locusta migratoria.

A neuropeptide which stimulates the motility of the cockroach hindgut has been isolated from an extract of 9000 brain-corpora cardiaca-corpora allata-subesophageal ganglion complexes of Locusta migratoria. Biological activity was monitored during HPLC purification by observing the myotropic effect of column fractions on the isolated hindgut of Leucophaea maderae. The primary structure of this myotropic peptide was established as a blocked 16-residue peptide: pGlu-Asp-Ser-Gly-Asp-Gly-Trp-Pro-Gln-Gln-Pro-Phe-Val-Pro-Arg-Leu-NH2. This novel locust peptide was designated as locustapyrokinin, or Lom-PK. Lom-PK was synthesized and shown to have chromatographic and biological properties identical to those of the native material. Lom-PK has a Phe-X-Pro-Arg-Leu-NH2 carboxy terminal in common with leucopyrokinin (or Lem-PK), a blocked myotropic neuropeptide isolated from the cockroach hindgut. The constituent amino acids of this C-terminal are important for biological activity on the Leucophaea hindgut. The primary structure of this novel insect peptide is, however, substantially different from Lem-PK at the amino-terminal sequence.

Amino Acid Sequence↗
PubMed1990

Locustatachykinin III and IV: two additional insect neuropeptides with homology to peptides of the vertebrate tachykinin family.

Two myotropic peptides termed locustatachykinin III and IV were isolated from 9000 brain-corpora cardiaca-corpora allata-suboesophageal ganglion extracts of the locust, Locusta migratoria. The primary structures of Lom-TK III and IV were established as amidated decapeptides: Ala-Pro-Gln-Ala-Gly-Phe-Tyr-Gly-Val-Arg-NH2 (Lom-TK III) and Ala-Pro-Ser-Leu-Gly-Phe-His-Gly-Val-Arg-NH2 (Lom-TK IV). The locustatachykinins were synthesized and shown to have chromatographic and biological properties identical with those of the native materials. They stimulate visceral muscle contractions of the oviduct and the foregut of Locusta migratoria and of the hindgut of Leucophaea maderae. Both peptides exhibit sequence homologies with the vertebrate tachykinins. Sequence similarity is greater with the fish and amphibian tachykinins (up to 40%) than with the mammalian tachykinins. In addition, the intestinal and oviducal myotropic activity of the locustatachykinins is analogous to that of vertebrate tachykinins. Both chemical and biological similarities of vertebrate and insect tachykinins substantiates the evidence for a long evolutionary history of the tachykinin peptide family.

Amino Acid Sequence↗
PubMed1990

Locustatachykinin I and II, two novel insect neuropeptides with homology to peptides of the vertebrate tachykinin family.

Two myotropic peptides termed locustatachykinin I (Gly-Pro-Ser-Gly-Phe-Tyr-Gly-Val-Arg-NH2) and locustatachykinin II (Ala-Pro-Leu-Ser-Gly-Phe-Tyr-Gly-Val-Arg-NH2) were isolated from brain-corpora cardiaca-corpora allata-suboesophageal ganglion extracts of the locust, Locusta migratoria. Both peptides exhibit sequence homologies with the vertebrate tachykinins. Sequence homology is greater with the fish and amphibian tachykinins (up to 45%) than with the mammalian tachykinins. In addition, the intestinal myotropic activity of the locustatachykinins is analogous to that of vertebrate tachykinins. The peptides discovered in this study may just be the first in a whole series of substances from arthropod species to be identified as tachykinin family peptides. Moreover, both chemical and biological similarities of vertebrate and insect tachykinins substantiate the evidence for a long evolutionary history of the tachykinin peptide family.

Amino Acid Sequence↗
PubMed1990

Homologies between the amino acid sequences of some vertebrate peptide hormones and peptides isolated from invertebrate sources.

1. The 4K-prothoracicotropic hormone (PTTH) or bombyxin and the melanization-reddish coloration hormone of the silkworm Bombyx mori resemble insulin and insulin-like growth factors. 2. The family of adipokinetic/red pigment concentrating hormones has some similarity with glucagon. 3. Members of the FMRFamide family are found in vertebrates as well as in invertebrates. 4. In Locusta, a molecule immunologically and biologically related to amphibian melanophore stimulating hormone has been partially characterized. 5. Enkephalins and enkephalin-related peptides occur in insects and other invertebrates. 6. Peptides belonging to the tachykinin family have been isolated from molluscan (Octopus) salivary glands and from insect nervous tissue (Locusta migratoria). 7. Invertebrate arginine-vasotocin homologs have been isolated from an insect (Locusta migratoria) and from a mollusc (Conus). 8. In Leucophaea, Locusta and Drosophila, peptides resembling those of the vertebrate gastrin/cholecystokinin family have been identified. 9. As the number of different neuro-/gut peptides with possible function(s) as hormone, neurotransmitter or neuromodulator is now estimated to be of the order of a few hundred, more similarities will probably show up in the near future.

Amino Acid Sequence↗
PubMed1988

Coexistence of melanin-concentrating hormone and alpha-melanocyte-stimulating hormone immunoreactivities in the central nervous system of the locust, Locusta migratoria.

The distribution of melanin concentrating hormone (MCH) in the central nervous system of the locust Locusta migratoria was studied by the indirect immunofluorescence technique, using antibodies against salmon MCH. Most MCH-immunoreactive perikarya were found in the optic lobes at both sides of the brain, dorsally with respect to the lamina ganglionaris. The same neurons also contain alpha-melanocyte-stimulating hormone (alpha-MSH)-like material. In addition, a moderate number of MCH-like neurons, which were devoid of alpha-MSH-immunoreactive substances, was observed in the pars intercerebralis. Bright immunofluorescent fibers were visualized in various regions of the central nervous system of the locust: the optic lobes, the ocelli, the proto-and deuterocerebrum, the subesophageal connectives and the corpora cardiaca. In the ventral nerve cord and the subesophageal ganglion, where alpha-MSH-like cell bodies were encountered, MCH immunoreactive perikarya were absent and immunoreactive fibers were scarce. The coexistence of MCH and alpha-MSH-immunoreactive material within the same specific neurons might indicate an evolutionary relationship of both peptides.

Animals↗
PubMed1988

Methionine-enkephalin immunoreactivity in the gonads and nervous system of two insect species: Locusta migratoria and Sarcophaga bullata.

Methionine(met)-enkephalin immunoreactivity as visualized by the peroxidase-antiperoxidase procedure, is present in spermatogonia, spermatocytes, spermatids, and young ovarian follicles of Locusta (panoistic type) and Sarcophaga (polytrophic type). Follicle cells and mature spermatozoa are always immunonegative as are locust vitellogenic follicles. In oocytes and in trophocytes, the met-enkephalin-like material first appears around the nucleus and is then dispersed throughout the cytoplasm. Later, it is present only in the periphery. In the ovary of both insects, no immunoreactivity is found with antisera against adrenocorticotrophic hormone, melanophore stimulating hormone, beta-endorphin, corticotropin releasing factor, or leucine-enkephalin. All these antisera yield a positive reaction when applied to the central nervous system as does the met-enkephalin antiserum. This study indicates that the met-enkephalin-like peptide may play a role in reproductive physiology.

Animals↗
PubMed1988

Biological, chromatographical, and radioimmunological evidence for a melanotropin-like peptide in the central nervous system of Locusta migratoria.

Our recent immunocytochemical study has demonstrated the existence of alpha-melanocyte stimulating hormone (alpha-MSH)-like material in the locust central nervous system. The aim of the present study was to further characterize alpha-MSH in the locust brain by its biological effect on frog skin and by high-pressure liquid chromatography in combination with radioimmunological and biological detection methods. Parallel radioimmunoassay (RIA) curves of crude nervous tissue extracts coupled with bioactivity in a very specific bioassay suggest similarity between the locust alpha-MSH-like substance and synthetic alpha-MSH. The highest concentration of alpha-MSH immunoreactive material in the central nervous system was found in the optic lobes, where alpha-MSH immunoreactive cell bodies are localized, as was previously shown by immunocytochemistry. High concentrations of alpha-MSH immunoreactive material were also detected in the thoracic ganglia of the locust ventral nervous system. The application of locust brain extracts to gel permeation HPLC resulted in a similar elution profile of the bioactive and immunologically active substances, both coeluting with synthetic alpha-MSH. As is the case for vertebrate brain material, reverse-phase HPLC revealed four alpha-MSH immunoreactive peaks. One of the peaks coelutes with monoacetyl-alpha-MSH and other RIA-positive material elutes at times close (but not identical) to the methionine sulfoxide forms of alpha-MSH. Peak three, however, elutes in a very different position from desacetyl-alpha-MSH. Peaks are absent in the position of desacetyl-alpha-MSH. Similarity between the locust alpha-MSH-related substance and authentic alpha-MSH is discussed.

Animals↗
PubMed1987

Localization of melanotropin-like peptides in the central nervous system of two insect species, the migratory locust, Locusta migratoria, and the fleshfly, Sarcophaga bullata.

By use of well characterized antisera in the peroxidase-antiperoxidase method, we were able to demonstrate alpha MSH and beta MSH immunoreactive cells and nerve fibres within the nervous system of adults and larvae of Locusta migratoria and 3-, 5- and 8-day-old adult Sarcophaga bullata. In neither of these insect species, any immunoreaction was obtained with a gamma 3MSH-antiserum. Double immunohistochemical stainings revealed that alpha MSH-like and beta MSH-like substances are located in different cells. These cells show no immunoreactivity to a number of antisera against other POMC-derivatives (anti-beta lipotropin, anti beta endorphin, anti-ACTH1-24); thus they appear to contain alpha MSH- or beta MSH-like material in a specific way. The function of the immunologically detected peptides remains to be demonstrated. The distribution of the immunoreactive material suggests that, like in amphibians and other lower vertebrates, the synthesis or release of melanotropins might be under the influence of external stimuli. The present observations support the recently developed concept that even some of the smallest neuropeptides, the melanotropins, have been highly conserved during a long period of evolution.

Animals↗
PubMed1986

Polyploidization and localisation of poly(A)+ RNA in the different cell types of the vitellogenic meroistic ovary of the fleshfly, Sarcophaga bullata.

The degree of polyploidization, the level of transcriptional activity and the volume of the different cell types present in the meroistic ovary of Sarcophaga bullata were measured during different vitellogenic stages. The nurse cells and the germinal vesicle exhibited very pronounced differences with regard to DNA content and mRNA synthesis, even though they are genetically identical. During the 4C stage (late vitellogenesis), we observed different degrees of polyploidy in follicle cells adjacent to the oocyte and those surrounding the nurse cells. Although the chromatin of the germinal vesicle is condensed into a karyosome, in situ hybridisation revealed the presence of transcriptional activity. The volume of the germinal vesicle, which contains only 4C DNA, is big enough to contain 2048C DNA. The meroistic ovary is a highly polarized differentiating system. Our results are discussed in the light of the fact that the polytrophic ovary is a miniature electrophoresis chamber.

Animals↗
PubMed1986

A new alternative for simultaneous immunohistochemical screening of 96 hybridoma clones for tissue-specific antibody productions selects a monoclonal antibody to insect corpus cardiacum.

In the current search for the elucidation of the true structure of hitherto unidentified 'new' insect neuropeptides we designed a novel screening method to facilitate the primary detection of neurone-specific antibody secreting mouse-mouse hybridoma clones obtained after immunization with neuronal tissue homogenates. The present procedure is principally adapted from a conventional immunohistological test and enables one to rapidly screen 96 (and even more) clones at one time for potential secretion of specific antibodies to different tissue compounds, without the necessity of having a purified antigen. It has proved to be sensitive, rapid, practical and reproducible. As such it promises to be very useful to discriminate amongst the wide range of antibodies to various kinds of materials produced by hybridomas by detecting monoclonal antibodies directed against factors contained in well-defined tissues in which one is interested. This paper also reports the successful application of this method to a primary screening of clones producing murine monoclonal antibodies to substances of insect corpora cardiaca (CC), after immunization with crude antigen preparations.

Animals↗
PubMedDate not supplied

NPY-like peptides occur in the nervous system and midgut of the migratory locust, Locusta migratoria and in the brain of the grey fleshfly, Sarcophaga bullata.

The distribution of the NPY-like substances in the nervous system and the midgut of the migratory locust, Locusta migratoria and in the brain of the grey fleshfly, Sarcophaga bullata was determined by immunocytochemistry using an antiserum directed against synthetic porcine NPY. The peroxidase-antiperoxidase procedure revealed that NPY immunoreactive cell bodies and nerve fibers were observed in the brain, optic lobes, corpora cardiaca, suboesophageal ganglion and ventral nerve cord of the locust and in the brain, optic lobes and suboesophageal ganglion of the fleshfly. In the locust midgut, numerous endocrine cells and nerve fibers penetrating the outer musculature contained NPY-like immunoreactivity. The concentrations of NPY immunoreactive material in acetic acid extracts of locust brain, optic lobes, thoracic ganglia, ovaries and midguts was measured using a specific radioimmunoassay technique. The dilution curves of the crude tissue extracts were parallel to the standard curve. The highest amount of NPY-like immunoreactivity was found in the locust ovary and midgut. Reverse-phase high-performance liquid chromatography (RP-HPLC) and radioimmunoassay were used to characterize the NPY-like substances in the locust brain and midgut. HPLC-analysis revealed that NPY-immunoreactivity in the locust brain eluted as three separate peaks. The major peak corresponded to a peptide less hydrophobic than synthetic porcine NPY. RP-HPLC analysis of midgut extracts revealed the presence of an additional NPY-immunoreactive peak which had a retention time similar to the porcine NPY standard. The present data show the existence of a widespread network of NPY immunoreactive neurons in the nervous system of the locust and the fleshfly. Characterization of the immunoreactive substances indicates that peptides similar but not identical to porcine NPY are present in the central nervous system and midgut of insects.

Animals↗
PubMedDate not supplied

Isolation, identification and synthesis of locustamyotropin (Lom-MT), a novel biologically active insect peptide.

A peptide that stimulates the spontaneous contractions of the hindgut of Leucophaea maderae has been purified from extracts of brain-corpora cardiaca/corpora allata-subesophageal ganglion complexes of 9000 adult Locusta migratoria and was designated locustamyotropin or Lom-MT. The primary structure of this 12 residue peptide has been determined Gly-Ala-Val-Pro-Ala-Ala-Gln-Phe-Ser-Pro-Arg-Leu-NH2. The C-terminal sequence (Phe-Ser-Pro-Arg-Leu-NH2) is identical to the C-terminal pentapeptide of the pheromone biosynthesis activating neuropeptide, recently isolated from Heliothis zea, and is also similar to the C-terminal of leucopyrokinin of Leucophaea. Synthetic Lom-MT showed biological as well as chemical characteristics, indistinguishable from those of native Lom-MT. In locust preparations, Lom-MT provoked an increase in frequency, amplitude and tonus of contractions of the oviduct, but was inactive in the same conditions on the locust hindgut preparation.

Amino Acid Sequence↗