Immunohistochemical demonstration of a CCK-like peptide in the nervous system of a marine annelid worm, Nereis diversicolor O.F. M�ller

Engelhardt, R. P.; Dhainaut-Courtois, N.; Tramu, G.

doi:10.1007/bf00210894

Cited by 46 publications

(23 citation statements)

References 34 publications

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“…Note that one of the paired mushroom bodies is only lightly shaded to allow for underlying structures to be seen (ec circumesophageal connective, pa palps, pc prostomial cirri, pn palpal nerve). c Diagram representing the gross distribution of ganglion cell groups in the brain (left dorsal view, right ventral view; modified from Engelhardt et al 1982) extends from dorso-caudal toward ventro-rostral. A fissure divides it into a larger anterior and a smaller posterior cell mass (Fig.…”

Section: Mushroom Bodiesmentioning

confidence: 99%

“…Later, immunocytological techniques were used to investigate the presence and distribution of neuropeptides in N. diversicolor. For example, Engelhardt et al (1982) and Dhainaut-Courtois et al (1985) demonstrated, in the perikaryal clusters, the occurrence and distribution of cholecystokinin-like peptides and a variety of substances immunologically related to vertebrate neuropeptides. The presence of Phe-Met-Arg-Phe-NH2 (FMRFamide) in the central nervous system of N. diversicolor was reported by Porchet and Dhainaut-Courtois (1988).…”

Section: Introductionmentioning

confidence: 99%

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Immunofluorescence analysis of the internal brain anatomy of Nereis diversicolor (Polychaeta, Annelida)

Heuer

Loesel

2007

Cell Tissue Res

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Comparative analyses of neuroanatomical characters can make valuable contributions to the inference of phylogenetic relationships. Whereas investigations in this field are numerous for arthropods, in-depth studies on other protostomes are sparse. Here, we provide a survey of the internal neuroarchitecture of the brain of the aciculate ragworm Nereis diversicolor (Polychaeta, Annelida). Descriptions are based on confocal laser scanning microscope analyses of brain sections labeled with the nuclear marker DAPI and antibodies raised against FMRF-amide, serotonin, and histamine. Autofluorescence of the nervous tissue has been utilized to further elucidate the anatomical structures of the brain. The architecture of two major brain compartments, i.e., the paired mushroom bodies and the central optic neuropil, is described in detail. The findings are compared with existent literature on polychaete neuroanatomy and on arthropod neuroanatomy, and possible phylogenetic implications are outlined.

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Section: Mushroom Bodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immunofluorescence analysis of the internal brain anatomy of Nereis diversicolor (Polychaeta, Annelida)

Heuer

Loesel

2007

Cell Tissue Res

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“…Our data showed that the leech PCSK1 is prominently expressed in the supraoesophageal ganglion, representing the brain of the leech. Given that many invertebrate peptide hormones, including those of the leech, are produced by neurosecretory cells of the brain (Grimmelikhuijzen, et al 1980;Engelhardt, et al 1982;Vigna, et al 1984;Pestarino 1990;van Heumen and Roubos 1990;Gomot, et al 1992;Meester, et al 1992;Sonetti, et al 1992;Kellner-Cousin, et al 1994;Kellner, et al 2002;Wang, et al 2007;Miller and Newmark 2012), these specialized Hau-pcsk1-expressing cells may well be some of the neurosecretory cells of the leech.…”

Section: Invertebrate Pcsk1 Orthologs Have Not Been Characterized In mentioning

confidence: 99%

Diversification of metazoan Kexin-like proprotein convertases: insights from the leechHelobdella

Tao

Cheng

Song

et al. 2019

Preprint

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Intercellular communication is quintessential for multicellularity and often mediated by secreted peptide ligands. In Metazoa, proprotein convertases are a major class of endoproteases partaking in the proteolytic processing of these ligands, which is in turn required for their signaling activities. In vertebrates, the best-studied convertase substrates are neuropeptides, peptide hormones, and members of the TGFβ/BMP-family. Each ligand is processed by a particular subset of convertases. Therefore, the diversification of convertases may have contributed to the growing complexity of cellular communication in metazoan evolution.However, proprotein convertases have not been systematically explored in Metazoa. Here, we sampled the representative metazoan genomes and established that six Kexin-like proprotein convertases were present in the last common ancestor of protostomes and deuterostomes.Among these, we identified a novel PCSKX orthologous group (OG) that was lost in vertebrates. Spiralian protosomes have, in general, maintained all six OGs. Therefore, we characterized the functional divergence of the Kexin-like OGs in the leech Helobdella, an experimentally tractable spiralian. Gene expression patterns suggested that PCSK1 and PCSK2 are specialized for the processing of neuropeptides and peptide hormones in bilaterians and that the newly identified PCSKX is probably functionally similar to furin and PCSK7. Finally, we showed that, distinct from the BMP morphogen in vertebrate embryos, the convertase-mediated proteolytic cleavage is not required for the short-range BMP signaling in the dorsoventral patterning of leech ectoderm. Together, our data revealed the complexity of the Kexin-like proprotein convertase gene family and their roles in generating diverse patterns of cellular communication in Metazoa. 4 each individual convertase has distinct, preferred cleavage sites (Nelsen and Christian 2009), tissue-specific expression of convertase activity may be a critical factor in determining the differing strength and range of TGFβ/BMP signaling between tissue types.While it has been shown that the requirement for and consequence of convertasemediated cleavage differ between BMP ligands and between species (Fritsch, et al. 2012), the diversity in the roles of convertase-mediated cleavage in the regulation of cellular signaling has been largely unexplored. In the leech Helobdella, a novel form of short-range BMP signal patterns the dorsoventral axis of ectoderm (Kuo and Weisblat 2011b). Thus, to investigate the hypothesis that differential expression of selected Kexin-like proprotein convertases contributes to such a non-canonical deployment of this BMP signal, we set out to characterize the genes encoding proprotein convertases in the leech genome.Proprotein convertases have only been studied in a small number of mostly vertebrate model species, and the pre-vertebrate evolutionary history of this gene family is largely unknown. To provide a phylogenetic framework for our studies on the leech proprotein convertases a...

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“…The immunohistochemical method was performed as described previously (Engelhardt et al, 1982). In brief, 8·µm sections were prepared and mounted on chrome alum/gelatin-coated slides and briefly air-dried.…”

Section: Immunohistochemical Proceduresmentioning

confidence: 99%

Stimulation by cadmium of myohemerythrin-like cells in the gut of the annelidNereis diversicolor

Demuynck¹,

Bocquet-Muchembled²,

Deloffre³

et al. 2004

Journal of Experimental Biology

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Trace metals, whether essential such as Cu and Zn or nonessential such as Cd, are taken up by aquatic invertebrates from both food and solutions. After ingestion, the metal is transported around the body, perhaps to be accumulated in particular target organs or even to be excreted (Rainbow, 1998). In most invertebrates, body concentrations of the non-essential metal Cd do not appear to be regulated (Rainbow, 1985;Amiard et al., 1987;Rainbow, 1998). Metal toxicity is often postulated to arise from reactions occurring in the cytosol, through nonspecific binding of the metal to non-thionein ligands, which are physiologically important molecules (metalloenzymes or small peptides such as glutathione) and are inactivated by metal binding (Mason and Jenkins, 1995). Control of intracellular metal toxicity and detoxification of accumulated trace metals is generally achieved via the production of metal-binding ligands that sequester metals. These cellular ligands can be found in the particulate fraction of the cells such as mineral deposits, granules or lysosomes (George, 1990;Mason and Jenkins, 1995) and in the cytosol such as metallothioneins (Engel and Roesijadi, 1987). Metallothioneins, a family of low molecular mass cysteine-rich proteins, have been shown to occur in most zoological taxa (Amiard and Cosson, 1997). However, in polychaetous annelids this type of protein has not yet been isolated.Nereis diversicolor (Hediste diversicolor, recent denomination) is a polychaete living in the mud of estuaries which, in Europe, is routinely contaminated by heavy metals. Previous work (Nejmeddine et al., 1988) showed that in animals exposed to Cd the metal was bound to two pools of proteins of high molecular mass (metalloprotein I, MPI, >67·kDa) and low molecular mass (MPII, of about 20·kDa). MPI is the extracellular hemoglobin of this annelid (Demuynck and Dhainaut-Courtois, 1993). The primary structure of MPII isolated from whole worms was different from that of a metallothionein, consisting of 119 amino acid residues with only one cysteine residue , but shares 80.8% identity with the myohemerythrin isolated by Takagi and Cox (1991) from the same species. MPII is a Cd-binding protein but is not a metallothionein. Metallothioneins are known to be induced by essential (Cu or Zn) and non-essential (Cd) metals and are thought to be important both in the detoxification of trace metals and in the metabolism of intracellular Cu and Zn, as in the scavenging of reactive oxygen species (Palmiter, 1998;Klaassen et al., 1999). However, MPII appeared to correspond to a myohemerythrinlike pigment, known to play a mainly respiratory role and with no known function of detoxification. Immunocytochemical studies showed that MPII is located in granulocytes I Isolated guts of Nereis diversicolor revealed the existence of a cadmium-binding protein, the MPII, belonging to the group of hemerythrins and myohemerythrins. The presence of MPII in the cells of the intestine was demonstrated by immunocytochemistry, using anti-MPII, a monoclonal antibod...

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Immunohistochemical demonstration of a CCK-like peptide in the nervous system of a marine annelid worm, Nereis diversicolor O.F. M�ller

Cited by 46 publications

References 34 publications

Immunofluorescence analysis of the internal brain anatomy of Nereis diversicolor (Polychaeta, Annelida)

Immunofluorescence analysis of the internal brain anatomy of Nereis diversicolor (Polychaeta, Annelida)

Diversification of metazoan Kexin-like proprotein convertases: insights from the leechHelobdella

Stimulation by cadmium of myohemerythrin-like cells in the gut of the annelidNereis diversicolor

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