Seven novel FMRFamide-like neuropeptide sequences from the eyestalk of the giant tiger prawn Penaeus monodon

Sithigorngul, Paisarn; Pupuem, Jirasak; Krungkasem, Chatchadaporn; Longyant, Siwaporn; Chaivisuthangkura, Parin; Sithigorngul, Weerawan; Petsom, Amorn

doi:10.1016/s1096-4959(01)00499-7

Cited by 46 publications

(44 citation statements)

References 21 publications

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“…In the case of FMRFamide-like peptides of the prawn Penaeus monodon, which were found to be components of the SG, the amount of material for purification was 18,000 times higher than in our study (25). On the other hand, enkephalins were postulated to be present in SG of crustacean by cytochemical methods (26), but never found by structural analysis.…”

Section: Discussioncontrasting

confidence: 71%

Identification of Neuropeptides from the Sinus Gland of the Crayfish Orconectes limosus Using Nanoscale On-line Liquid Chromatography Tandem Mass Spectrometry

Bulau

Meisen

Schmitz

et al. 2004

Molecular & Cellular Proteomics

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In this article, a novel and sensitive analytical strategy for direct characterization of neuropeptides from the X-Organ-sinus gland neurosecretory system of the crayfish Orconectes limosus is presented. A desalted extract corresponding to 0.5 sinus gland equivalents was analyzed in a nanoflow liquid chromatography system coupled to quadrupole time-of-flight tandem mass spectrometry (nanoLC-QTOF MS/MS). The existence and structural identity of four crustacean hyperglycemic hormone precursor-related peptide variants and two new genetic variants of the pigment-dispersing hormone, not detected by conventional chromatographic systems, molecular cloning, or immunochemical methods before, was revealed. Studies in crustaceans have demonstrated the X-Organsinus gland neurosecretory system (XO-SG) 1 as a source of various neuropeptides (1, 2). The most relevant progress has been achieved in structure elucidation of a novel family of large peptides from the sinus gland (SG), which includes, according to their first-discovered biological activities, crustacean hyperglycaemic (CHH), moult-inhibiting (MIH) and vitellogenesis/gonad-inhibiting (VIH/GIH) hormones (3, 4). Two subfamilies may be distinguished at the preprohormone level, either containing an associated CHH precursor-related peptide sequence (CPRP), located between the signal peptide and the native hormone sequence, characteristic for the CHH subfamily, or without this CPRP sequence, as determined for the MIH/VIH/GIH subfamily. CPRPs have also been identified in other invertebrate groups such as insects and nematodes (4, 5). These neurohormones are classically considered as major physiological regulators involved in the control of carbohydrate metabolism and in various functions in development such as moult and reproduction (3, 6, 7). Additionally, the chromatophore-regulating hormones, like red pigmentconcentrating hormone (RPCH) and pigment-dispersing hormone (PDH), have been found in the XO-SG system of different crustacean species (8 -11).Different approaches, such as conventional chromatography, molecular cloning, and immunochemical methods, were used previously to investigate sinus gland components (12)(13)(14)(15)(16)(17). The limitations of these established methods to identify and characterize new peptides are the relatively low sensitivity in the case of conventional chromatography, the necessity of sufficient sequence homology in the case of molecular cloning, and the availability of specific antibodies in the case of immunochemical methods. In contrast to this, the combination of nanoscale liquid chromatography and mass spectrometry (MS) capable of tandem MS analysis (nanoLC-MS/MS) is designed for detection and sequencing of known and unknown peptides independent of their sequence homology. This is the first report on the direct analysis of neuropeptides from the neurosecretory XO-SG system using nanoLC-MS/MS.

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Section: Discussioncontrasting

confidence: 71%

Identification of Neuropeptides from the Sinus Gland of the Crayfish Orconectes limosus Using Nanoscale On-line Liquid Chromatography Tandem Mass Spectrometry

Bulau

Meisen

Schmitz

et al. 2004

Molecular & Cellular Proteomics

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“…However, in contrast to the wealth of information on the hormonal contents of insect midgut endocrine cells, nothing is known about the identity of the paracrines/hormones present in the putative midgut epithelial endocrine cells of any decapod species. Here, we have begun an immunohistochemical and mass spectrometric investigation to determine the extent to which crustacean neuropeptide paracrines and hormones are located in and released by midgut epithelial endocrine cells of Cancer species, focusing on the tachykinin-related peptides (TRPs), which are welldocumented brain-gut peptides in insects (reviewed by Nässel, 1999), and the SIFamides, a newly described family of neuropeptides present in both insects and crustaceans (Janssen et al, 1996;Vanden Broeck, 2001;Huybrechts et al, 2003;Sithigorngul et al, 2002;Verleyen et al, 2004;Yasuda et al, 2004;Messinger et al, 2005;Christie et al, 2006). Some of these data have appeared previously in abstract form .…”

Section: Introductionmentioning

confidence: 99%

Midgut epithelial endocrine cells are a rich source of the neuropeptides APSGFLGMRamide (Cancer borealis tachykinin-related peptide Ia) and GYRKPPFNGSIFamide (Gly1-SIFamide) in the crabs Cancer borealis, Cancer magister and Cancer productus

Christie

Kutz-Naber

Stemmler

et al. 2007

Journal of Experimental Biology

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-SIFamide) and APSGFLGMRamide [Cancer borealis tachykinin-related peptide Ia (CabTRP Ia)], respectively, both of which are known neuropeptides of Cancer species. Although the function of these midgut-derived peptides remains unknown, we found that both Gly 1 -SIFamide and CabTRP Ia were released when the midgut was exposed to highpotassium saline. In addition, CabTRP Ia was detectable in the hemolymph of crabs that had been held without food for several days, but not in that of fed animals, paralleling results that were attributed to TRP release from midgut endocrine cells in insects. Thus, one function that midgutderived CabTRP Ia may play in Cancer species is paracrine/hormonal control of feeding-related behavior, as has been postulated for TRPs released from homologous cells in insects.

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“…Sample selection and preparation: The SGs were excised from crayfish and the naturally peptides crude extract were extracted according to Sithigorngul et al (2002). Briefly, eyestalks were cut-off near the base with a scalpel.…”

Section: Methodsmentioning

confidence: 99%

Identification of peptides from sinus gland extracts in the red swampcrayfish Procambarus clarkii by mass spectrometry

Zhou

2016

IJAR

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Crustacean sinus gland (SG) is a well-defined neuroendocrine organ that controls the secretion of various neuropeptides which regulate many physiological activities. The red swamp crayfish Procambarus clarkii is a decapod crustacean with both high economic and scientific importance in China. To facilitate physiological investigations of SG peptide/hormone function in this species, we have been employed tissue extract fractionation by HPLC to obtain a complete description of neuropeptidome and used Electrospray ionization-Fourier transform mass spectrometry (ESI-FTMS) to detect the peptidome present in its organ. In total, 48 peptide sequences belonging to several known neuropeptide families including crustacean cardioactive peptide, CHH precursor-related peptides (CPRPs), orcokinins and pigment dispersing hormones were identified. Among these 48 sequences, 26 are novel peptides and 22 are previously identified. Overall, the results give a stimulus for future physiological studies of SG neuropeptides in P. clarkii and other crustaceans.

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Seven novel FMRFamide-like neuropeptide sequences from the eyestalk of the giant tiger prawn Penaeus monodon

Cited by 46 publications

References 21 publications

Identification of Neuropeptides from the Sinus Gland of the Crayfish Orconectes limosus Using Nanoscale On-line Liquid Chromatography Tandem Mass Spectrometry

Identification of Neuropeptides from the Sinus Gland of the Crayfish Orconectes limosus Using Nanoscale On-line Liquid Chromatography Tandem Mass Spectrometry

Midgut epithelial endocrine cells are a rich source of the neuropeptides APSGFLGMRamide (Cancer borealis tachykinin-related peptide Ia) and GYRKPPFNGSIFamide (Gly1-SIFamide) in the crabs Cancer borealis, Cancer magister and Cancer productus

Identification of peptides from sinus gland extracts in the red swampcrayfish Procambarus clarkii by mass spectrometry

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