Immunocytochemical Localization of Glucagon‐Related Peptides in the Cerebral Ganglion of the Protochordate Ascidian, <i>Styela plicata</i>

Pestarino, Mario

doi:10.1111/j.1365-2826.1990.tb00459.x

Cited by 8 publications

(3 citation statements)

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“…In annelids, a sister clade of molluscs, immunoreactive PACAP-like peptides and receptors were identified in the CNS and peripheral nervous system (PNS) (Reglödi et al, 2000;Molnar et al, 2006;Boros et al, 2008Boros et al, , 2010Varhalmi et al, 2008). Similarly, in the bivalve mollusc the Mediterranean mussel (Mytilus galloprovincialis), immunoreactivity for VIP was detected in the mantle and in gastropod molluscs, VIP-like molecules were detected in the nervous system of the sea hare (Aplysia kurodai) and land snail (Helix pomatia) and in innate immune cells of two freshwater snails (Planorbarius corneus and Viviparus ater) (Kuramoto et al, 1985;Ottavianil and Cossarizza, 1990;Ottaviani et al, 1992;Kaufmann et al, 1995;Licata et al, 2003). In the nervous system of the pond snail (Lymnaea stagnalis) two VIP immunoreactive neurons were detected (Schot et al, 1981).…”

Section: Lophotrochozoansmentioning

confidence: 99%

“…In the nervous system of the pond snail (Lymnaea stagnalis) two VIP immunoreactive neurons were detected (Schot et al, 1981). Immunoreactive GCG/GLP and SCT was also detected in immune cells of the two freshwater snails (Ottavianil and Cossarizza, 1990;Ottaviani et al, 1992). In annelids, VIP-like positive cells were detected in the CNS of the leech (Hirudo medicinalis), earthworm (Lumbricus terrestres), oligochaete (Nereis diversicolor) (Sundler et al, 1977;Osborne et al, 1982), and planarian (Schistosoma mansoni) (Gustafsson, 1987).…”

Section: Lophotrochozoansmentioning

confidence: 99%

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Tracing the Origins of the Pituitary Adenylate-Cyclase Activating Polypeptide (PACAP)

2020

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Pituitary adenylate cyclase activating polypeptide (PACAP) is a well-conserved neuropeptide characteristic of vertebrates. This pluripotent hypothalamic neuropeptide regulates neurotransmitter release, intestinal motility, metabolism, cell division/differentiation, and immunity. In vertebrates, PACAP has a specific receptor (PAC 1) but it can also activate the Vasoactive Intestinal Peptide receptors (VPAC 1 and VPAC 2). The evolution of the vertebrate PACAP ligand-receptor pair has been well-described. In contrast, the situation in invertebrates is much less clear. The PACAP ligand-receptor pair in invertebrates has mainly been studied using heterologous antibodies raised against mammalian peptides. A few partial PACAP cDNA clones sharing >87% aa identity with vertebrate PACAP have been isolated from a cnidarian, several protostomes and tunicates but no gene has been reported. Moreover, current evolutionary models of the peptide and receptors using molecular data from phylogenetically distinct invertebrate species (mostly nematodes and arthropods) suggests the PACAP ligand and receptors are exclusive to vertebrate genomes. A basal deuterostome, the cephalochordate amphioxus (Branchiostoma floridae), is the only invertebrate in which elements of a PACAP-like system exists but the peptides and receptor share relatively low sequence conservation with the vertebrate homolog system and are a hybrid with the vertebrate glucagon system. In this study, the evolution of the PACAP system is revisited taking advantage of the burgeoning sequence data (genome and transcriptomes) available for invertebrates to uncover clues about when it first appeared. The results suggest that elements of the PACAP system are absent from protozoans, non-bilaterians, and protostomes and they only emerged after the protostome-deuterostome divergence. PACAP and its receptors appeared in vertebrate genomes and they probably shared a common ancestral origin with the cephalochordate PACAP/GCG-like system which after the genome tetraploidization events that preceded the vertebrate radiation generated the PACAP ligand and receptor pair and also the other members of the Secretin family peptides and their receptors.

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Section: Lophotrochozoansmentioning

confidence: 99%

Section: Lophotrochozoansmentioning

confidence: 99%

Tracing the Origins of the Pituitary Adenylate-Cyclase Activating Polypeptide (PACAP)

2020

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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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Glucagon and Glucagon-like Peptides in Fishes

Plisetskaya

Mommsen

1996

International Review of Cytology

131

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Immunocytochemical Localization of Glucagon‐Related Peptides in the Cerebral Ganglion of the Protochordate Ascidian, Styela plicata

Cited by 8 publications

References 31 publications

Tracing the Origins of the Pituitary Adenylate-Cyclase Activating Polypeptide (PACAP)

Tracing the Origins of the Pituitary Adenylate-Cyclase Activating Polypeptide (PACAP)

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

Glucagon and Glucagon-like Peptides in Fishes

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