Peptides in the Nervous Systems of Cnidarians: Structure, Function, and Biosynthesis

Grimmelikhuijzen, Cornelis J.P.; Leviev, Ilia; Carstensen, Klaus

doi:10.1016/s0074-7696(08)61345-5

Cited by 170 publications

(145 citation statements)

References 107 publications

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“…Several peptides are known to affect muscle contraction in Hydra and other cnidarians (Takahashi et al, 1997;Yum et al, 1998b;Grimmelikhuijzen et al, 1996). Hym-355 has been shown to weakly promote the contraction of an isolated retractor muscle of the sea anemone, Anthopleura fuscoviridis (T. Takahashi et al, unpublished observations), but no effect on muscle contraction in Hydra was observed (data not shown).…”

Section: Hym-355 Is Expressed In Neuronsmentioning

confidence: 96%

“…The precursor protein contains a possible signal sequence rich in hydrophobic amino acids at the N-terminal region (von Heijne, 1983) (thinly underlined) and one copy of the unprocessed sequence of Hym-355 (thickly underlined). The unprocessed Hym-355 sequence is preceded by glutamic acid at its N terminus, which is one of the processing sites specifically found for Cnidaria (Grimmelikhuijzen et al, 1996). At its C-terminal flanking region there is a dibasic processing site (KR) preceded by glycine, which serves as an amide group donor.…”

Section: Isolation and Characterization Of The Gene Encoding Hym-355mentioning

confidence: 99%

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A novel neuropeptide, Hym-355, positively regulates neuron differentiation in Hydra

Takahashi¹,

Koizumi²,

Ariura³

et al. 1999

Comparative Biochemistry and Physiology Part A: Molecular &

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During the course of a systematic screening of peptide signaling molecules in Hydra a novel peptide, Hym-355 (FPQSFLPRG-NH2), was identified. A cDNA encoding the peptide was isolated and characterized. Using both in situ hybridization and immunohistochemistry, Hym-355 was shown to be expressed in neurons and hence is a neuropeptide. The peptide was shown to specifically enhance neuron differentiation throughout the animal by inducing interstitial cells to enter the neuron pathway.Further, co-treatment with a PW peptide, which inhibits neuron differentiation, nullified the effects of both peptides, suggesting that they act in an antagonistic manner. This effect is discussed in terms of a feedback mechanism for maintaining the steady state neuron population in Hydra.

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Section: Hym-355 Is Expressed In Neuronsmentioning

confidence: 96%

Section: Isolation and Characterization Of The Gene Encoding Hym-355mentioning

confidence: 99%

A novel neuropeptide, Hym-355, positively regulates neuron differentiation in Hydra

Takahashi¹,

Koizumi²,

Ariura³

et al. 1999

Comparative Biochemistry and Physiology Part A: Molecular &

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“…Since then, FMRFamide and FMRFamide-related peptides have been isolated from a wide variety of invertebrate species, ranging from primitive metazoans, such as cnidarians, to higher invertebrates, such as insects (2)(3)(4)(5). FMRFamide-related peptides occur in all classes of cnidarians, suggesting that these peptides were among the first transmitters used in evolution (6). After their discovery in invertebrates, FMRFamide-related substances have also been purified from mammals and other vertebrates (7)(8)(9), suggesting that these peptides occur in all animals having a nervous system.…”

mentioning

confidence: 99%

“…The preprohormones of the FMRFamide-related peptides in invertebrates are characterized by a large number of FMRFamide peptide copies, ranging from 38 copies (36 identical peptides) in cnidarians (6,10), to 29 copies (28 FMRFamides and one FLRFamide copy) in molluscs (11) and 13 (eight different peptides) in insects (12,13). FMRFamide-related peptides may act excitatory or inhibitory on their target cells (depending on the target cell type) and they are involved in reproduction, feeding, and many other behaviors (3,5,(14)(15)(16)(17)(18).…”

mentioning

confidence: 99%

Molecular cloning and functional expression of the first insect FMRFamide receptor

Cazzamali

Grimmelikhuijzen

2002

Proc. Natl. Acad. Sci. U.S.A.

115

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FMRFamide and FMRFamide-related neuropeptides are extremely widespread and abundant in invertebrates and have numerous important functions. Here, we have cloned a Drosophila orphan receptor, and stably expressed it in Chinese hamster ovary cells. Screening of a peptide library revealed that the receptor reacted with high affinity to FMRFamide (EC50, 6 ؋ 10 ؊9 M). The intrinsic Drosophila FMRFamide peptides are known to be synthesized as a large preprohormone, containing at least 13 related FMRFamide peptides (8 distinct FMRFamides). Screening of these intrinsic Drosophila FMRFamides showed that the receptor had highest affinity to Drosophila FMRFamide-6 (PDNFMRFamide) (EC50, 9 ؋ 10 ؊10 M), whereas it had a somewhat lower affinity to Drosophila FMRFamide-2 (DPKQDFMRFamide) (EC50, 3 ؋ 10 ؊9 M) and considerably less affinity to the other Drosophila FMRFamide-related peptides. To our knowledge, this article is the first report on the molecular identification of an invertebrate FMRFamide receptor.

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“…In contrast, PHM is not glycosylated and is followed by a noncatalytic region (exon A), the second catalytic domain, and a single transmembrane domain that attaches to a cytosolic COOH-terminal domain responsible for localizing PAM in cells (5). Based on studies on Cnidarians, the most primitive organisms with an organized nervous system, the use of amidated peptides for intercellular communication preceded the use of catecholamines (22). DBM and PHM are both found in soluble and membranebound forms, but have adopted different mechanisms for membrane association.…”

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confidence: 99%

Cell Type-specific Storage of Dopamine β-Monooxygenase

Oyarce

Eipper

2000

Journal of Biological Chemistry

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Expression of dopamine ␤-monooxygenase (DBM), the enzyme that converts dopamine into norepinephrine, is limited to adrenal chromaffin cells and a small population of neurons. We studied DBM trafficking to regulated granules by stably expressing rat DBM in AtT-20 corticotrope tumor cells, which contain regulated granules, and in Chinese hamster ovary (CHO) cells, which lack regulated granules. The behavior of exogenous DBM in both cell lines was compared with endogenous DBM in adrenal chromaffin cells. CHO cells secreted active DBM, indicating that production of active enzyme does not require features unique to neuroendocrine cells. Pulse-chase experiments indicated that early steps in DBM maturation followed a similar time course in AtT-20, CHO, and adrenal chromaffin cells. Use of a conformation-sensitive DBM antiserum indicated that acquisition of a folded structure occurred with a similar time course in all three cell types. Cell type-specific differences in DBM trafficking became apparent only when storage in granules was examined. As expected, DBM was stored in secretory granules in chromaffin cells; CHO cells failed to store DBM. Despite the fact that AtT-20 cells have regulated granules, exogenous DBM was not stored in these granules. Thus storage of DBM in secretory granules requires cell type specific factors.

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Peptides in the Nervous Systems of Cnidarians: Structure, Function, and Biosynthesis

Cited by 170 publications

References 107 publications

A novel neuropeptide, Hym-355, positively regulates neuron differentiation in Hydra

A novel neuropeptide, Hym-355, positively regulates neuron differentiation in Hydra

Molecular cloning and functional expression of the first insect FMRFamide receptor

Cell Type-specific Storage of Dopamine β-Monooxygenase

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