Amino acid sequence of crustacean hyperglycemic hormone (CHH) from the crayfish, Orconectes limousus: Emergence of a novel neuropeptide family

Kegel, Günter; Reichwein, Barbara; Tensen, Cornelis P.; Keller, Rainer

doi:10.1016/0196-9781(91)90036-o

Cited by 87 publications

(38 citation statements)

References 16 publications

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“…The SG peptides CPRP A/A* (12, 13) and PDH (14) from O. limosus could be identified (CPRP A/A*) or fully characterized (PDH) by a sequence coverage of 100% (Tables I and II). Additionally, the existence of four CPRP variants (CPRP v1-4) and two new genetic PDH variants (PDHA and PDHB) not observed using conventional chromatographic systems (12,13) or molecular cloning (14, 15) was proved.…”

Section: Discussionmentioning

confidence: 99%

“…If SG peptide extract has been separated by a gradient up to 80% solvent B, we were able to detect it in the UV profile peptides, which were potential CHH (12) and MIH (Swiss-Prot accession no. P83636) candidates (Fig.…”

Section: Identification Of Neuropeptides Using Nanolc-msmentioning

confidence: 99%

“…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.…”

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confidence: 99%

“…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.…”

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confidence: 99%

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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: Discussionmentioning

confidence: 99%

Section: Identification Of Neuropeptides Using Nanolc-msmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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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“…The amino acid sequences of CHH from several species have been determined (Kegel et al, 1989;Kegel et al, 1991;Tensen et al, 1991b;Huberman et al, 1993;Martin et al, 1993;Yang et al, 1995;Gu and Chang, 1998). The presence of multiple molecular forms of CHH in a single species was observed.…”

Section: Introductionmentioning

confidence: 98%

Molecular Structure and Organization of Crustacean Hyperglycemic Hormone Genes of Penaeus monodon

Wiwegweaw¹,

Udomkit²,

Panyim³

2004

BMB Reports

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The Crustacean hyperglycemic hormone (CHH) has been shown to exist as multiple molecular forms in several crustacean species. In Penaeus monodon, a gene encoding CHH (so-called Pem-CHH1) was recently described. In this study, the molecular structures of two other CHH genes (Pem-CHH2 and Pem-CHH3) are reported. Both the Pem-CHH2 and Pem-CHH3 genes contain three exons that are separated by two introns that are similar to the structure of other genes in the same family. An analysis of the upstream nucleotide sequences of each Pem-CHH gene has identified the putative promoter element (TATA box) and putative binding sites for several transcription factors. The binding sites for CREB, Pit-1, and AP-1 were found upstream of all three Pem-CHH genes. A Southern blot analysis showed that at least one copy of each Pem-CHH gene was located within the same 10 kb genomic DNA fragment. These results suggest that the CHH genes are arranged in a cluster in the genome of P. monodon, and that their expression may be modulated by similar mechanisms.

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Purification and characterization of an isoform of crustacean hyperglycemic hormone from the eyestalk ofMacrobrachium rosenbergii

et al. 1999

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Amino acid sequence of crustacean hyperglycemic hormone (CHH) from the crayfish, Orconectes limousus: Emergence of a novel neuropeptide family

Cited by 87 publications

References 16 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

Molecular Structure and Organization of Crustacean Hyperglycemic Hormone Genes of Penaeus monodon

Purification and characterization of an isoform of crustacean hyperglycemic hormone from the eyestalk ofMacrobrachium rosenbergii

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