Isolation and characterization of red-pigment-concentrating hormone (RPCH) from six crustacean species

Gaus, Gabriele; Kleinholz, L. H.; Kegel, Günter; Keller, Rainer

doi:10.1007/bf01075668

Cited by 43 publications

(20 citation statements)

References 16 publications

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“…RPCH has a functional role opposite to that of PDH (Garfias et al, 1995;Rao, 1985;Gaus et al, 1990). In our results some similarity was observed between PDF-ir (unpublished data) and AKHir in some positions (LG, dorsal part of OL and NPMD) in P. scaber and in NPMD in A. vulgare (Fouda et al, 2010) and the other cells are different in position.…”

Section: The Distribution Of α-Msh-irsupporting

confidence: 78%

Immunolocalization of Two Putative Pigmentotropins Akh I and -MSH-Like Immunoreactivities in the Brain of Rough Woodlouse, Porcellio Scaber and Pill Bugs Armadillidium Vulgare (Crustacea, Isopoda).

Fouda

2013

Al-Azhar Bulletin of Science- Basic Science Sector

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Antisera against putative pigmentotropic neuropeptides, Adipokinetic hormone I (AKH I) and α-Melanocyte stimulating hormone (α-MSH) reacted with small sets of neurons in the cephalic ganglia of the isopoda Porcellio scaber and Armadillidium vulgare. The distributions of immunoreactivities resembled in the two species. AKH I-like immunoreactivity (AKH I-ir) occurs in both species. In P scaber 5 cells occurred in the optic lobe (OL) (3 small near Lamina ganglionaris, LG and 2 large dorsally) while in A.vulgare only one small cell near LG. The accessory lobe (AL) and subesophageal mass (SM) have the same pattern in both species. There are 2 cells in AL and 6 cells in SM (in the cells of mandibular ganglion,CMD). α-MSH immunoreactivity (α-MSH-ir) were located in OL, and SM in both species and in AL of A.vulgare. In P. scaber two large perikarya were located dorsally, one small ventrally, while in A.vulgare 4 large dorsally, one small ventrally and strong reactivity in pseudo-frontal organ (PFO). In AL, 3 immunopositive cells were observed. In SM 6 cells (4 in CMD, 2 in the cells of maxillulary ganglion, CML) in P scaber and 8 cells (6 in CMD, 2 in CML) were observed in A. vulgare. These results suggest the possible existence of AKH-like and α-MSHlike peptides in isopoda. No differences were detected between males and females. The projections of immunoreactive fibers were traced to several brain regions, the somatogastric nervous system and the neurohaemal organs, which suggest multiple functions of these peptides.

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Section: The Distribution Of α-Msh-irsupporting

confidence: 78%

Immunolocalization of Two Putative Pigmentotropins Akh I and -MSH-Like Immunoreactivities in the Brain of Rough Woodlouse, Porcellio Scaber and Pill Bugs Armadillidium Vulgare (Crustacea, Isopoda).

Fouda

2013

Al-Azhar Bulletin of Science- Basic Science Sector

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“…This is a blocked octapeptide, pGlu-LeuAsn-Phe-Ser-Pro-Gly-Trp-NH,, the same sequence also occurring in C. nzuenm (Gaus et al, 1990). The adipokinetic hormones of insects have a common structure to the RPCH peptides prompting the designation of an RPCH-AKH arthropod superfamily (for a review of structures see Gade et al, 1994).…”

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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“…For that reason, and their relatively small size, their structures are now known for a considerable number of insect species (for review see Gade, 1991). A striking feature of this peptide family is its large structural variety within insects, from which several different peptides have been isolated, while in crustaceans only a single peptide has been found (Gaus et al, 1990). This suggests that different evolutionary pressures are operating in crustaceans as compared to insects, and it also suggests that this peptide family may be a good model to study the evolution of neuropeptides.…”

Section: Introductionmentioning

confidence: 98%

Isolation of two AKH‐related peptides from cicadas

Veenstra

Hagedorn

1995

Arch Insect Biochem Physiol

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Two peptides related to locust adipokinetic hormone and crustacean red pigment concentrating hormone were isolated by high performance liquid chromatography from the cicadas Cacama valavata and Diceroprocta semicincta. Both species have the same peptides. The structure of one of the peptides is pGlu-Val-Asn-Phe-Ser-Pro-Ser-Trp-Gly-Asn-amide. The mass spectrum, amino acid composition, and amino acid sequence of the other peptide suggest that it is almost identical to the first peptide. However, the exact nature of the difference between the two peptides could not be determined.

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Isolation and characterization of red-pigment-concentrating hormone (RPCH) from six crustacean species

Cited by 43 publications

References 16 publications

Immunolocalization of Two Putative Pigmentotropins Akh I and -MSH-Like Immunoreactivities in the Brain of Rough Woodlouse, Porcellio Scaber and Pill Bugs Armadillidium Vulgare (Crustacea, Isopoda).

Immunolocalization of Two Putative Pigmentotropins Akh I and -MSH-Like Immunoreactivities in the Brain of Rough Woodlouse, Porcellio Scaber and Pill Bugs Armadillidium Vulgare (Crustacea, Isopoda).

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

Isolation of two AKH‐related peptides from cicadas

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