Molecular cloning of crustacean pigment dispersing hormone precursor

Klein, Jörg; Kleijn, Dominique P.V. de; Keller, Rainer; Weidemann, Wolfgang

doi:10.1016/0006-291x(92)90246-h

Cited by 37 publications

(22 citation statements)

References 10 publications

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“…Crustacean neuropeptides for which there are as yet no known insect homologues include the orcokinins, initially isolated from the crayfish Orconectes limosus as a 13-residue peptide with myotropic activity, NFDEIDRSGFGFN (Stangier et al, 1992), with closely related analogues now identified from C. maenas (Bungart et al, 1995); the 18-residue pigment dispersing hormones, that of c. maenas having the structure NSEL-INSILGLPKVMNDA-NH, (Klein et al, 1992); and an important family of peptides that are concerned with the physiological processes of glycaemia, moulting and reproduction. The latter peptides are characterised by an unusually large size of 70-80 amino acid residues.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Identification of Multiple Neuropeptides of the Allatostatin Superfamily in the Shore Crab Carcinus Maenas

Duve

Johnsen

Maestro

et al. 1997

European Journal of Biochemistry

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20 neuropeptides belonging to the allatostatin superfamily were isolated from extracts of cerebral and thoracic ganglia of the shore crab Carcinus maenas. They were purified by HPLC, monitored by radioimmunoassay and identified by mass spectrometry and amino acid sequencing. The allatostatins are characterised by a common C‐terminal pentapeptide sequence ‐YXFGL‐NH2. Previously such peptides have only been reported from insects. In insects the variable post‐tyrosyl residue is restricted to Ala, Asn, Asp, Gly or Ser. In C. maenas, however, there are only two types; thirteen of the peptides having a post‐tyrosyl Ala and the other seven, a post‐tyrosyl Ser. The crab peptides include the shortest allatostatins so far identified (YAFGL‐NH2 and YSFGL‐NH2) as well as the longest, a 27‐residue peptide. The total of 20 peptides exceeds the highest number of allatostatins found in any of the insects investigated so far (14 in Periplaneta americana). It is of interest that, despite their clear homology, none of the peptides of C. maenas is identical to any of the more than 50 known insect allatostatins. The crab allatostatins show evidence of gene duplication and mutation that has resulted in several sub‐groups with close structural similarities. For example, there are four heptapeptides with the common C‐terminus ‐PYAFGL‐NH2 that differ only at the N‐terminal residue, which is either Glu, Asp, Asn or Ser. Other motifs, variously extended at the N‐terminus, include ‐GPY(A/S)FGL‐NH2 (three peptides), ‐DMY(A/S)FGL‐NH2 (three peptides), and ‐GQY(A/S)FGL‐NH2 (two peptides). Unique among the allatostatin superfamily, one of the crab peptides has a Tyr for Phe substitution at position three from the C‐terminus (GGPYSYGL‐NH2). Immunocytochemistry has provided clues to the functions of the allatostatins in crustaceans by showing their widespread presence in the central and stomatogastric nervous systems.

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Section: Discussionmentioning

confidence: 99%

Isolation and Identification of Multiple Neuropeptides of the Allatostatin Superfamily in the Shore Crab Carcinus Maenas

Duve

Johnsen

Maestro

et al. 1997

European Journal of Biochemistry

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“…With the subsequent identification of the structurally related peptide NSELINSILGLPKVMNDAamide from the crab Uca pugilator [180], the Pandalus peptide was redesignated a-PDH and the Uca isoform b-PDH. Since their initial descriptions, other PDH isoforms have been identified biochemically, molecularly and/or via mass spectrometry from a wide variety of decapod species (e.g., [49,50,63,[181][182][183][184][185][186][187][188][189]), with those possessing sequence, acidity, and charge similarity to a-PDH forming one subgroup and those with similarity to b-PDH forming a second subfamily [190]. While members of the b-PDH subfamily have been identified in species from a number of decapod infraorders, detection of members of the a-PDH subfamily has thus far been limited to members of the Caridea [191].…”

Section: Pigment Dispersing Hormonementioning

confidence: 99%

Crustacean neuropeptides

Christie

Stemmler

Dickinson

2010

Cell. Mol. Life Sci.

194

407

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Crustaceans have long been used for peptide research. For example, the process of neurosecretion was first formally demonstrated in the crustacean X-organ-sinus gland system, and the first fully characterized invertebrate neuropeptide was from a shrimp. Moreover, the crustacean stomatogastric and cardiac nervous systems have long served as models for understanding the general principles governing neural circuit functioning, including modulation by peptides. Here, we review the basic biology of crustacean neuropeptides, discuss methodologies currently driving their discovery, provide an overview of the known families, and summarize recent data on their control of physiology and behavior.

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“…:** . (Klein et al, 1992) with those deduced from the D. pulex transcriptome (Dappu-T) (Gard et al, 2009) and genome (Dappu-G) . For each protein, the signal peptide is shown in gray, with all prohormone convertase cleavage sites shown in black.…”

Section: Introductionmentioning

confidence: 75%

From genes to behavior: investigations of neurochemical signaling come of age for the model crustacean Daphnia pulex

Christie

McCoole

2012

Journal of Experimental Biology

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SummaryThe cladoceran crustacean Daphnia pulex has served as a standard organism for aquatic toxicity testing for decades. The model organism status of D. pulex rests largely on its remarkable ability to rapidly adapt morphologically, physiologically and behaviorally to a wide range of environmental challenges, as well as on its parthenogenetic reproduction and ease of laboratory culture. As in all multicellular organisms, neurochemical control systems are undoubtedly major contributors to the functional flexibility of Daphnia. Surprisingly, little work has focused on understanding its neurochemistry at any level. Recently, D. pulex has been the subject of extensive genome and transcriptome sequencing, and it is currently the only crustacean with a fully sequenced, publicly accessible genome. Although the molecular work was initiated for gene-based investigations of ecotoxicology and toxicogenomics, the data generated have allowed for investigations into numerous aspects of Daphnia biology, including its neurochemical signaling. This Commentary summarizes our knowledge of D. pulex neurochemistry obtained from recent genomic and transcriptomic studies, and places these data in context with other anatomical, biochemical and physiological experiments using D. pulex and its sister species Daphnia magna. Suggestions as to how the Daphnia molecular data may be useful for future investigations of crustacean neurochemical signaling are also provided.

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Molecular cloning of crustacean pigment dispersing hormone precursor

Cited by 37 publications

References 10 publications

Isolation and Identification of Multiple Neuropeptides of the Allatostatin Superfamily in the Shore Crab Carcinus Maenas

Isolation and Identification of Multiple Neuropeptides of the Allatostatin Superfamily in the Shore Crab Carcinus Maenas

Crustacean neuropeptides

From genes to behavior: investigations of neurochemical signaling come of age for the model crustacean Daphnia pulex

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