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Berlin Brandenburg

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  • 1
    Language: English
    In: Regulatory Peptides, 2/1994, Vol.50(1), pp.37-43
    Description: FMRFamide was isolated originally from neural-tissue extracts of a bivalve mollusc, since when either authentic FMRFamide or a series of structurally-related peptides have been isolated from representative arthropods, annelids and many additional molluscs. However, to date no information exists as to the definitive presence and primary structure of a FaRP in a free-living flatworm. Here, we report the isolation and primary structure of a FaRP from the free-living turbellarian, Artioposthia triangulata , a species from which NPF has been previously structurally-characterised. Unlike molluscs and insects, in which several FaRPs are expressed, only a single member of this family was detected in this turbellarian. The primary structure of this turbellarian FaRP was established as Arg-Tyr-Ile-Arg-Phe-NH 2 (RYIRFamide) and the molecular mass as 752.7 Da. These data have established unequivocally that FaRPs occur in the nervous systems of the most phylogenetically-ancient invertebrates which display bilaterally-symmetrical neuronal plans and that authentic FMRFamide is probably not the original member of the family in molecular evolutionary terms.
    Keywords: Fmrfamide ; Fmrfamide-Related Peptide ; Platyhelminth ; Turbellarian ; Primary Structure ; Molecular Evolution ; Invertebrate Neuropeptide;
    ISSN: 01670115
    E-ISSN: 18731686
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  • 2
    Language: English
    In: Regulatory Peptides, 6/1992, Vol.39(2-3), p.255
    Keywords: Chemistry ; Anatomy & Physiology;
    ISSN: 01670115
    E-ISSN: 18731686
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  • 3
    Language: English
    In: Regulatory Peptides, 8/1993, Vol.47(1), p.91
    Keywords: Chemistry ; Anatomy & Physiology;
    ISSN: 01670115
    E-ISSN: 18731686
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  • 4
    Language: English
    In: Regulatory Peptides, 9/1993, Vol.47(2), pp.187-194
    Description: Chicken pancreatic polypeptide is the prototype of the neuropeptide Y (NPY)/PP superfamily of regulatory peptides. This polypeptide was appended the descriptive term avian, despite the presence of some 8600 extant species of bird. Additional primary structures from other avian species, including turkey, goose and ostrich, would suggest that the primary structure of this polypeptide has been highly-conserved during avian evolution. Avian pancreatic polypeptides structurally-characterised to date have distinctive primary structural features unique to this vertebrate group including an N-terminal glycyl residue and a histidyl residue at position 34. The crow family, Corvidae, is representative of the order Passeriformes, generally regarded as the most evolutionarily recent and diverse avian taxon. Pancreatic polypeptide has been isolated from pancreatic tissues from five representative Eurasian species (the magpie, Pica pica ; the jay, Garrulus glandarius ; the hooded crow, Corvus corone ; the rook, Corvus frugilegus ; the jackdaw, Corvus monedula ) and subjected to structural analyses. Mass spectroscopy estimated the molecular mass of each peptide as 4166 ± 2 Da . The entire primary structures of 36 amino acid residue peptides were established in single gas-phase sequencing runs. The primary structures of pancreatic polypeptides from all species investigated were identical: APAQPAYGDDAPVEDLLRFYNDLQQYLNVVTRPRY. The peptides were deemed to be amidated due to their full molar cross-reactivity with the amide-requiring PP antiserum employed. The molecular mass (4165.6 Da), calculated from the sequences, was in close agreement with mass spectroscopy estimates. The presence of an N-terminal alanyl residue and a prolyl residue at position 34 differentiates crow PP from counterparts in other avian species. These residues are analogous to those found in most mammalian analogues. These data suggest that the term avian, appended to the chicken peptide, is no longer tenable due to the presence of an Ala 1 , Pro 34 peptide in five species from the largest avian order. These data might also suggest that, in keeping with the known structure/activity requirements of this peptide family, crow PP should interact identically to mammalian analogues on mammalian receptors.
    Keywords: Pancreatic Polypeptide ; Primary Structure ; Eurasian Crow ; Neuropeptide Y;
    ISSN: 01670115
    E-ISSN: 18731686
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