Biomedical subjects

A Thorpe

Publications and source records attributed to A Thorpe.

At least 37 records · Page 2Linked to original sources

PubMed1997

Identification, tissue localisation and physiological effect in vitro of a neuroendocrine peptide identical to a dipteran Leu-callatostatin in the codling moth Cydia pomonella (Tortricidae: Lepidoptera).

A neuroendocrine peptide of the Leu-callatostatin family, LPVYNFGL-NH2, has been isolated from tissue extracts of 5th instar larvae of the codling moth, Cydia pomonella (Lepidoptera). It is identical to a peptide previously isolated from the blowfly, Calliphora vomitoria (Diptera). The distribution of this peptide within the tissues of C. pomonella has been mapped by immunocytochemistry using antisera raised against LPVYNFGL-NH2. Midgut endocrine cells contain Leu-callatostatin immunoreactivity, as do several paired Leu-callatostatin neurones in the brain and ventral nerve cord. Within the visceral nervous system, the frontal ganglion contains four Leu-callatostatin neurones. Axons from these cells combine with others originating from neurones in the brain and project within the nervi cardiostomatogastrici to innervate the tissues of the foregut. In particular, the oesophageal valve has a prominent ring of Leu-callatostatin-immunoreactive fibres. The synthetic peptide, LPVYNFGL-NH2, has a potent reversible inhibitory effect in vitro on all visible forms of spontaneous contractile activity of the foregut, including closure of the oesophageal valve. Complete myoinhibition is observed at peptide concentrations from 10(-10 )to 10(-16) M. These results, in conjunction with the results of similar studies on cockroaches, crickets and flies, suggest that the Leu-callatostatins are a ubiquitous family of insect neuroendocrine peptides with an important role in the control of gut motility.

Animals↗

PubMed1997

Lepidopteran peptides of the allatostatin superfamily.

Peptides of the allatostatin superfamily with the C-terminal amino acid sequence -YXFGL-NH2 have been isolated and identified from the lepidopterans, the codling moth, Cydia pomonella (Tortricidae) and the bollworm, Helicoverpa armigera (Noctuidae). The peptides, designated cydiastatins and helicostatins respectively, were monitored during purification with radioimmunoassays based on the callatostatins of the blowfly Calliphora vomitoria. The eight peptides from each of the two species appear to form an homologous series with four identical and three that differ by a single amino acid. This study demonstrates the ubiquitous nature of this family of peptides in insects.

Amino Acid Sequence↗

PubMed1996

Identification of the dipteran Leu-callatostatin peptide family: the pattern of precursor processing revealed by isolation studies in Calliphora vomitoria.

Information from the Leu-callatostatin gene sequences of the blowflies Calliphora vomitoria and Lucilia cuprina was used to develop antisera specific for the variable post-tyrosyl amino-acid residues Ser, Ala and Asn of the common Leu-callatostatin C-terminal pentapeptide sequence -YXFGL-NH2. Radioimmunoassays based on these antisera were used to purify peptides from an extract of 40000 blowfly heads. Five neuropeptides of the Leu-callatostatin family were identified. Three have a seryl residue in the post-tyrosyl position. Two of these are octapeptides that differ only at the N-terminal residue; NRPYSFGL-NH2 and ARPYSFGL-NH2, whilst the third is the heptapeptide derived by N-terminal trimming; RPYSFGL-NH2. Two octapeptides in which X is Ala and Asn were also identified; VERYAFGL-NH2 and LPVYNFGL-NH2. The latter peptide is derived by processing at the internal dibasic site of a putative heneicosapeptide encoded by the DNA. These findings stress the necessity to have putative structures verified at the peptide level. Potent, reversible inhibitory effects on the spontaneous contractile activity of the blowfly rectum were recorded for ARPYSFGL-NH2 (monophasic dose-response curve with an IC50 = 10 fM) and for LPVYNFGL-NH2 (biphasic dose-response curve with IC50 values of approximately 1 fM and 1 nM). It is suggested that regulation of gut motility in insects, rather than an allatostatic function, may represent an ancestral and universal function of the allatostatins. One of the reasons for the large number of members of the Leu-callatostatin family appears to be in the provision of an integrated form of gut motility control, with different peptides controlling specific regions of the gut.

Amino Acid Sequence↗

PubMed1996

Identification of the dipteran Leu-callatostatin peptide family: characterisation of the prohormone gene from Calliphora vomitoria and Lucilia cuprina.

The prohormone gene encoding the Leu-callatostatin peptides has been isolated from a Calliphora vomitoria genomic DNA library and its homologue was cloned from genomic and cDNA libraries of another blowfly species, Lucilia cuprina. Gene and prohormone structure and organisation are essentially identical in the two species. The Leu-callatostatin gene consists of at least 3 exons. The prohormone is encoded on exons two and three and the two blocks of putative Leu-callatostatin peptides are carried on separate exons. It is 180 amino-acids long, begins with a short signal peptide and contains two blocks of tandemly arranged Leu-callatostatin peptides separated by an acidic spacer region. The prohormone contains 5 copies of the C-terminal sequence -YX FGL characteristic of the Leu-callatostatin family. Complete endoproteolytic processing at all possible pairs of basic amino acids would generate 5 different Leu-callatostatin octapeptides. Two larger Leu-callatostatins could be released if processing was not complete at two of the sites. None of the 3 peptides encoded in the first block was identified in previous purification studies of the callatostatin peptides. The second block, located at the carboxyl end of the prohormone, contains two peptide sequences identical to the previously isolated Leu-callatostatins 1 and 4. The absence of independent copies of Leu-callatostatins 2 and 3 on the prohormone establishes that endoproteolytic cleavage of the precursor does not invariably proceed to completion and that Leu-callatostatin 2 must be derived by N-terminal processing of the parent peptide Leu-callatostatin 1. Reverse transcriptase PCR analysis of mRNA from brain and midgut, the two major sites of Leu-callatostatin expression, shows that the prohormone sequence at these two sites is identical, ruling out the possibility that different populations of peptides are expressed in these two tissues as a result of alternative RNA splicing.

Amino Acid Sequence↗

PubMed1996

Immortalized neural cells from trisomy 16 mice as models for Alzheimer's disease.

The trisomy 16 mouse (Ts16) is a general accepted animal model for both Downs syndrome (DS) and Alzheimer's Disease (AD). However, the efficacy of this model is severely hampered by the fact that Ts16 is lethal after about 18-20 days of gestation. Chimeras, long-term tissue culture and neural transplantation of Ts16 material have previously been used to overcome this limitation presented by death in utero of the Ts16. In this paper we describe a new strategy to overcome this limitation, i.e. immortalization of primary cells from Ts16 mice with retrovirus-mediated gene transfer of a temperature sensitive immortalizing oncogene. By this method we have obtained a total of 21 stable cell lines from Ts16 hippocampus, Ts16 cortex, normal hippocampus, and normal cortex. So far, two of the cell lines have been karyotyped and as expected, the cell line immortalized from Ts16 embryos has retained three copies of chromosome 16. We are currently characterizing these cell lines with respect to expression of APP, T-antigen, Nestin, GFAP, NF and Map-2. Moreover, the processing and secretion of APP fragments are being investigated by immunoblotting. In summary, we have immortalized CNS cells from Ts16 mice and we expect that these cell lines will be useful as in vitro and in vivo models for studying various aspects of the pathology of Alzheimer's disease.

Alzheimer Disease↗

PubMed1996

Electret-based passive dust sampler: sampling of organic dusts.

Passive samplers are light, convenient and cheap. However, the sample size tends to be small and a correlation exercise between the results of a passive sampler and a conventional sampler must be carried out. The design principles and mode of action of an electret-based passive dust sampler are described. The device captures dust particles at a rate independent of the velocity of air except when this is very low but dependent on the electrical properties of the dust being sampled. Experimental results are presented of measurements made in bakeries, pig farms, a dairy farm, an arable farm and a rubber-manufacturing plant. Correlation between measurements made with the passive sampler and measurements of inhalable dust performed by other means are reasonable. The results are interpreted in terms of the physical properties of the dust being sampled.

Agriculture↗

PubMed1995

The sulfakinins of the blowfly Calliphora vomitoria. Peptide isolation, gene cloning and expression studies.

The nonapeptide, Phe-Asp-Asp-Tyr(SO3)-Gly-His-Met-Arg-Phe-NH2 was isolated from heads of the blowfly Calliphora vomitoria. Designated callisulfakinin I, the peptide is identical to the earlier known drosulfakinin I of Drosophila melanogaster and to neosulfakinin I of Neobellieria bullata. It belongs to the sulfakinin family, all known members of which (from flies, cockroaches and locusts) have the C-terminal heptapeptide sequence Asp-Tyr(SO3)-Gly-His-Met-Arg-Phe-NH2. The callisulfakinin gene of C. vomitoria was cloned and sequenced. In addition to callisulfakinin I, the DNA revealed a coding sequence for the putative tetradecapeptide. Gly-Gly-Glu-Glu-Gln-Phe-Asp-Asp-Tyr-Gly-His- Met-Arg-Phe-NH2, callisulfakinin II. However, this peptide was not identified in the fly head extracts. Confocal laser scanning immunocytochemical studies with antisera raised against the synthetic undecapeptide C-terminal fragment of drosulfakinin II from D. melanogaster, Asp-Gln-Phe-Asp-Asp-Tyr(SO3)- Gly-His-Met-Arg-Phe-NH2, revealed only four pairs of sulfakinin neurones in the brain of C. vomitoria and no others anywhere else in the neural, endocrine or gut tissues. In situ hybridisation studies with a digoxigenin-labelled sulfakinin gene probe (from the blowfly Lucilia cuprina) also revealed only four pairs of neurones in the brain. The perikarya of two pairs of cells are situated medially in the caudo-dorsal region, close to the roots of the ocellar nerve. The other perikarya are slightly more posterior and lateral. Although it has been suggested by several authors that the insect sulfakinins are homologous to the vertebrate peptides gastrin and cholecystokinin, such arguments (based essentially on C-terminal structural similarities) do not take account of important differences in the C-terminal tetrapeptide. His-Met-Arg-Phe-NH2 in the sulfakinins, compared with Trp-Met-Asp-Phe-NH2 in gastrin and cholecystokinin. Furthermore, whereas the sulfakinin neurons of C. vomitoria are small in number and have a very specialised location, a greater number of cells throughout the nervous system react positively to gastrin/cholecystokinin antisera. Chromatographic profiles of the present study also revealed peaks of gastrin/cholecystokinin-immunoreactive material separate from the sulfakinin peptides. This evidence suggests that the insect and vertebrate peptides may not necessarily be homologous.

Amino Acid Sequence↗

PubMed1995

Isolation, identification and functional significance of [Hyp2]Met-callatostatin and des Gly-Pro Met-callatostatin, two further post-translational modifications of the blowfly neuropeptide Met-callatostatin.

Two post-translationally modified neuropeptides of the Met-callatostatin (Gly-Pro-Pro-Tyr-Asp-Phe-Gly-Met-NH2) family have been identified from head extracts of the blowfly Calliphora vomitoria. They are the octapeptide, [Hyp2]Met-callatostatin, (Gly-Hyp-Pro-Tyr-Asp-Phe-Gly-Met-NH2) and the truncated hexapeptide, des Gly-Pro Met-callatostatin (Pro-Tyr-Asp-Phe-Gly-Met-NH2). The existence of the [Hyp2]Met-callatostatin variant, in addition to the previously identified [Hyp3]Met-callatostatin peptide, suggests that the motif for prolyl hydroxylation in C. vomitoria is more variable than those known from mammalian and other invertebrate studies where, in those regulatory peptides containing a pair of adjacent prolyl residues so far studied, e.g., bradykinin, and the mosquito peptide Aea HP-I, only one of the pair (the second) is known to undergo hydroxylation. The truncated hexapeptide, des Gly-Pro Met-callatostatin could be produced as a result of the action of a dipeptidyl peptidase II type of enzyme which is known from mammalian studies to be unique in its ability to cleave between the two prolyl residues of an Xaa-Pro-Pro- sequence, where Xaa is any unprotected NH2-terminal amino acid. This enzyme is, however, considered unlikely to be able to cleave the Gly-Hyp-Pro-sequence, which would suggest a functional significance for such a post-translational modification. For this reason, it is of interest that [Hyp2]Met-callatostatin (and earlier, [Hyp3]Met-callatostatin) have been shown to be potent inhibitors of the spontaneous contractions of the hindgut of C. vomitoria (biphasic dose-response curve with IC50 values of 10(-14) M and 10(-7) M).(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1995

Leu-callatostatin gene expression in the blowflies Calliphora vomitoria and Lucilia cuprina studied by in situ hybridisation: comparison with Leu-callatostatin confocal laser scanning immunocytochemistry.

In situ hybridisation studies using a digoxigenin-labelled DNA probe encoding the Leu-callatostatin prohormone of the blowflies Calliphora vomitoria and Lucilia cuprina have revealed a variety of neurones in the brain and thoracico-abdominal ganglion, peripheral neurosecretory neurones, and endocrine cells of the midgut. With two exceptions, the hybridising cells are the same as those previously identified in immunocytochemical studies of sections and whole-mounts using Leu-callatostatin COOH-terminal-specific antisera. Within the brain and suboesophageal ganglion, there is a variety of neurones ranging from a single pair of large cells situated in the dorsal protocerebrum, to the several pairs of neurones in the tritocerebrum, some of which, in immunocytochemical preparations, can be seen to project via axons in the cervical connective to the thoracico-abdominal ganglion. In the medulla of the optic lobes, numerous small interneurones hybridise with the probe, as do clusters of similar-sized neurones close to the roots of the ocellar nerves. These results indicate that the Leu-callatostatin neuropeptides of the brain play a variety of roles in neurotransmission and neuromodulation. There are only three pairs of Leu-callatostatin-immunoreactive neurones in the thoracico-abdominal ganglion, at least two pairs of which project axons along the median abdominal nerve to provide extensive innervation of the hindgut. The Leu-callatostatin peripheral neurosecretory cells are located in close association with both nerve and muscle fibres in the thorax. In addition to neuronal Leu-callatostatin, the presence of the peptide and its mRNA has been demonstrated in endocrine cells in the posterior part of the midgut. These observations provide an example of a named brain/gut peptide in an insect.

Amino Acid Sequence↗

PubMed1995

Conformational preferences of the calliFMRFamides and their free-acid analogues.

A molecular dynamics study was undertaken to determine the conformational basis for the differing activities of the insect neuropeptide hormones calliFMRFamide 3 (SPSQDFMRF-NH2). calliFMRFamide 5 (APGQDFMRF-NH2) and their corresponding free-acid analogues (SPSQDFM-RF-OH and APGQDFMRF-OH) in two insect bioassays. A simulated annealing protocol was used to determine the range of conformers available to the linear peptides. Analysis of the conformers obtained indicated that all the peptides exhibited distinct secondary structure preferences. These, when correlated with their biological activities, enabled the formulation of putative conformation-activity relationships for the peptides.

Amino Acid Sequence↗

PubMed1994

Allatostatic neuropeptides from the cockroach Blattella germanica (L.) (Dictyoptera, Blattellidae). Identification, immunolocalization and activity.

Four allatostatic neuropeptides were isolated from extracts of the brain of the cockroach Blattella germanica. The primary structures of these peptides were assigned as Leu-Tyr-Asp-Phe-Gly-Leu-NH2 (BLAST-1), Asp-Arg-Leu-Tyr-Ser-Phe-Gly-Leu-NH2 (BLAST-2), Ala-Gly-Ser-Asp-Gly-Arg-Leu-Tyr-Ser-Phe-Gly-Leu-NH2 (BLAST-3) and Ala-Pro-Ser-Ser-Ala-Gln-Arg-Leu-Tyr-Gly-Phe-Gly-Leu-NH2 (BLAST-4). Each of the peptides showed C-terminal amino acid sequence similarity to cockroach allatostatins and blowfly callatostatins. The four peptides inhibited in vitro juvenile hormone production by corpora allata from virgin females of B. germanica. Immunoreactivity against allatostatins was seen in the lateral neurosecretory neurons and in the axonal pathway leading to the corpora allata.

Amino Acid Sequence↗

PubMed1994

[Hyp3]Met-callatostatin. Identification and biological properties of a novel neuropeptide from the blowfly Calliphora vomitoria.

A novel, hydroxyproline-containing neuropeptide, Gly-Pro-Hyp-Tyr-Asp-Phe-Gly-Met-NH2, designated [HYP3]Met-callatostatin, has been identified from extracts of heads of the blowfly Calliphora vomitoria. The peptide is a naturally occurring hydroxylate analogue of Met-callatostatin, a previously identified allatostatin-like peptide, and is present to the extent of 20% of the nonhydroxylated form. In bioassays, both forms of the peptide show allatostatic activity by inhibiting juvenile hormone synthesis and release in the cockroaches Periplaneta americana, Diploptera punctata, and Blattella germanica (IC50 = 100 pM-10 nM). They do not, however, influence juvenile hormone bisepoxide synthesis and release in the blowfly. In flies, [Hyp3]Met-callatostatin inhibits the peristaltic movements of the hindgut, showing a biphasic response (IC50 = 0.5 pM and 0.5 microM) compared with the monophasic response of Met-callatostatin (IC50 = 100 nM). Immunocytochemical studies with Met-callatostatin antisera provide the cytological basis for a myoinhibitory role in the gut since the axons of immunoreactive neurons in the abdominal ganglion project to the ileum. There are also endocrine cells in the midgut that, by releasing the peptides into the hemolymph, would allow the Met-callatostatins to fulfill a neurohormonal role on muscles of the gut and heart. In contrast, there are no Met-callatostatin neural pathways from the brain to the corpus allatum, the gland that produces juvenile hormone. NH2-terminal degradation of Met-callatostatins incubated with the hemolymph of P. americana results in cleavage of the Pro-Tyr bond giving the pentapeptide Tyr-Asp-Phe-Gly-Met-NH2 as a degradation product. In contrast, the Hyp-Tyr bond resists cleavage. With hemolymph from C. vomitoria, no immunoassayable degradation product has been observed with either peptide.

Amino Acid Sequence↗

PubMed1994

Localisation of sulfakinin neuronal pathways in the blowfly Calliphora vomitoria.

The distribution of neurones immunoreactive to antisera raised against the undecapeptide C-terminal fragment of drosulfakinin II (DrmSKII), Asp-Gln-Phe-Asp-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-NH2, has been studied in the blowfly Calliphora vomitoria. Antisera were preabsorbed with combinations of the parent antigen, the tetrapeptide Phe-Met-Arg-Phe-NH2 and cholecystokinin, the vertebrate sulfated octapeptide (CCK-8), Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2, in order to ensure specificity for the sulfakinin peptides of C. vomitoria (the nonapeptide callisulfakinin I is identical to drosulfakinin I and callisulfakinin II differs from DrmSK II only by the presence of -Glu3-Glu4- in place of -Asp3-Asp4-). Only four pairs of sulfakinin-immunoreactive neurons have been visualised in the entire nervous system. These occur in the brain: two pairs of cells situated medially in the caudo-dorsal region close to the roots of the ocellar nerve and two other pairs at the same level but positioned more laterally. Despite the small number of sulfakinin-immunoreactive cells, there are extensive projections to many areas of neuropile in the brain and the thoracic ganglion. The pathway of the medial sulfakinin cells extends into each of the three thoracic ganglia and a metameric arrangement of sulfakinin neuronal projections is also seen in the abdominal ganglia. Neither the dorsal neural sheath of the thoracic ganglion, nor the abdominal nerves contain sulfakinin-immunoreactive material. These observations suggest that the sulfakinins of the blowfly function as neurotransmitters or neuromodulators. They do not appear to have a direct role in gut physiology, as has been shown by in vitro bioassays for the sulfakinins of orthopterans and blattodeans. In addition to the neurones that display specific sulfakinin immunoreactivity, other cells within the brain and thoracic ganglion are immunoreactive to cholecystokinin/gastrin antisera. There are, therefore, at least two types of dipteran neuropeptides with amino acid sequences that are similar to the vertebrate molecules cholecystokinin and gastrin.

Amino Acid Sequence↗

PubMed1994

Distribution and functional significance of Leu-callatostatins in the blowfly Calliphora vomitoria.

The Leu-callatostatins are a series of four neuropeptides isolated from nervous tissues of the blowfly Calliphora vomitoria that show C-terminal sequence homology to the allatostatins of cockroaches. The allatostatins have an important role in the reproductive processes of insects as inhibitors of the synthesis and release of juvenile hormone from the corpus allatum. In this study, the distribution of the Leu-callatostatin-immunoreactive neurones and endocrine cells has been mapped in C. vomitoria and, in contrast to the cockroach allatostatins, it has been shown that there is no cytological basis to suggest that the dipteran peptides act as regulators of juvenile hormone. Although occurring in various neurones in the brain and thoracico-abdominal ganglion, there is no evidence of Leu-callatostatin-immunoreactive pathways linking the brain to the corpus allatum, or of immunoreactive terminals in this gland. Three different types of functions for the Leu-callatostatins are suggested by the occurrence of immunoreactive material in cells and by the pathways that have been identified. (1) A role in neurotransmission or neuromodulation appears evident from immunoreactive neurones in the medulla of the optic lobes, and from immunoreactive material in the central body and in descending interneurones in the suboesophageal ganglion that project to the neuropile of the thoracico-abdominal ganglion. (2) Leu-callatostatin neurones directly innervate muscles of the hindgut and the heart. Immunoreactive fibres from neurones of the abdominal ganglion pass by way of the median abdominal nerve to ramify extensively over several areas of the hindgut. Physiological experiments with synthetic peptides show that the Leu-callatostatins are potent inhibitors of peristaltic movements of the ileum. Leu-callatostatin 3 is active at 10(-16) to 10(-13) M. This form of regulatory control over gut motility appears to be highly specific since the patterns of contraction in other regions are unaffected by these peptides. (3) Evidence that the Leu-callatostatins act as neurohormones comes from the presence of varicosities in axons passing through the corpus cardiacum (but not the corpus allatum) and also from material in extraganglionic neurosecretory cells in the thorax. Fibres from these peripheral neurones are especially prominent over the large nerve bundles supplying the legs. There are also a considerable number of Leu-callatostatin-immunoreactive endocrine cells in a specific region of the midgut. The conclusion from this study is that although conservation of the structure of the allatostatin-type of peptides is evident through a long period of evolution it cannot be assumed that all of their functions have also been conserved.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗

PubMed1994

Measurements of the effectiveness of dust extraction systems of hand sanders used on wood.

An investigation has been made of the production of dust by hand sanders when used without dust extraction, with integral dust extraction and with external dust extraction. The apparatus used for the measurement was designed to carry out sanding in a repeatable manner, simulating normal working practice. The geometry of the wood sanded affects the dust concentration critically, whereas the effects of the sandpaper grade and of the filtration efficiency of the collection system are small. Belt sanders produce high dust levels in all situations, but they are very efficient in removing wood, which means that they need to be used for only a short period. The integral systems of orbital sanders give good dust control on flat wood but not on edges. The high air extraction rate of external systems results in much better dust control during the sanding of edges, though the performance of the two extraction systems on flat wood is broadly similar. The size distribution of the dust clouds produced by the sanding is relatively constant, but that produced by rotary sanders tends to be coarser than that produced by orbital sanders, consistent with the smoother finish given by the latter. The electric charge on the dust produced by sanding is high.

Air Pollutants, Occupational↗

PubMed1993

Callatostatins: neuropeptides from the blowfly Calliphora vomitoria with sequence homology to cockroach allatostatins.

Five neuropeptides with C-terminal amino acid sequence homology to cockroach allatostatins have been identified in the blowfly Calliphora vomitoria. Three have the same pentapeptide C-terminal amino acid sequence as allatostatin 1 of the cockroach Diploptera punctata. A hexadecapeptide designated callatostatin 1, isolated from thoracic ganglia, brains, and heads, has the sequence Asp-Pro-Leu-Asn-Glu-Glu-Arg-Arg-Ala-Asn-Arg-Tyr-Gly-Phe-Gly-Leu-NH2. Callatostatins 2 and 3 have been isolated from heads and thoracic ganglia, respectively; they comprise the last 14 and 8 residues of callatostatin 1. Callatostatin 4, isolated from thoracic ganglia, has the sequence Xaa-Arg-Pro-Tyr-Ser-Phe-Gly-Leu-NH2, where Xaa is either Asp or Asn. This peptide, with a serine substitution for glycine at position 5, has a C-terminal pentapeptide sequence identical to that of allatostatins 3 and 4 of D. punctata. Callatostatin 5, with the sequence Gly-Pro-Pro-Tyr-Asp-Phe-Gly-Met-NH2, was identified from whole flies. All five peptides inhibit juvenile hormone production by the corpora allata of D. punctata in vitro. Callatostatin 5 was the most potent allatostatin so far tested in this species, with maximum inhibition occurring at 1 nM. In contrast, none of the callatostatins or the allatostatins showed allatostatic activity in mature female C. vomitoria when tested at concentrations of 100 to 0.1 microM. In accordance with these results, immunoreactivity to an antiserum directed against the common C terminus of callatostatin 1 and allatostatin 1 was observed in the corpora allata of D. punctata but not in the corpus allatum of C. vomitoria, despite its presence in neurons of the brain. Neurons in the thoracic ganglion of C. vomitoria that are immunoreactive against this antiserum project to the hindgut, rectum, rectal papillae, and oviduct, suggestive of a function different from that of a true allatostatin.

Amino Acid Sequence↗

PubMed1993

Spectral transmission and short-wave absorbing pigments in the fish lens--I. Phylogenetic distribution and identity.

Fish lens transmission was found to vary depending on the type and concentration of short-wave absorbing compounds present within the lens. Pigments extracted from lenses of ten species were identified as mycosporine-like amino acids (mainly palythine, palythene and asterina-330, lambda maxs around 320-360 nm) which are also thought to be present in the majority of the 120 species examined here. A novel mycosporine-like pigment with lambda max 385 nm was isolated from the lens of the flying fish, Exocoetus obtusirostris, while lenses of several closely related tropical freshwater species were found to have high concentrations of the tryptophan catabolite 3-hydroxykynurenine (lambda max 370 nm). The type of lens pigment a species possesses and its concentration depends upon both the animal's phylogenetic group and its "optical niche".

Animals↗

PubMed1993

Spectral transmission and short-wave absorbing pigments in the fish lens--II. Effects of age.

Examination of the spectral transmission and pigments present in lenses of sixteen species of fish revealed that changes in lens pigment type and/or concentration often occur with age. Age-related changes in lens transmission for all species could be fitted to a common framework composed of three stages: an initial rapid accumulation of lens pigments producing a large increase in the wavelength of 50% transmission, followed by a reduction in the rate of pigment deposition which results in a levelling of the 50% transmission and a final stage after pigment accumulation ceases producing a drop in the wavelength of 50% transmission.

Aging↗