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  • 1
    Electronic Resource
    Electronic Resource
    Ranakinin: A Novel NK1 Tachykinin Receptor Agonist Isolated with Neurokinin B from the Brain of the Frog Rana ridibunda (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 57 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: An extract of the whole brain of the frog Rana ridibunda contained high concentrations of substance P-like immunoreactivity, measured with an antiserum directed against the COOH-terminal region of mammalian substance p and neurokinin b-like immurtoreactivity, measured with an antiserum directed against the NH2-terminus of neurokinin B. The primary structure of the substance p-related peptide (ranakinin) was established as: Lys-Pro-Asn-Pro-Glu-Arg-Phe-Tyr-Gly-Leu-Met-NH2. Mammalian substance P was not present in the extract. The primary structure of the neurokinin b-related peptide was established as: Asp-Met-His-Asp-Phe-Phe-Val-Gly-Leu-Met-NH2. This amino acid sequence is the same as that of mammalian neurokinin B.Ranakinin was equipotent with substance p and [Sar9,-Met(O2)11]substance p in inhibiting the binding of 125I-Bolton-Hunter-[Sar9, Met(O2)11]substance p, a selective radio-ligand for the NK1 receptor, to binding sites in rat subman-dibular gland membranes (IC50 1.6 ± 0.3 nM; n = 5). It is concluded that ranakinin is a preferred agonist for the mammalian NK1 tachykinin receptor subtype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb06426.x
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  • 2
    Electronic Resource
    Electronic Resource
    Carassin: A Tachykinin That Is Structurally Related to Neuropeptide-γ from the Brain of the Goldfish (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 56 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A 21-amino-acid residue tachykinin-related peptide, carassin, was isolated in pure form from an extract of the brain of the goldfish, Carrassius auratus, by reversedphase HPLC. The primary structure of the peptide was established as the following: Ser-Pro-Ala-Asn-Ala-Gln-IIe-Thr-Arg - Lys - Arg - His - Lys - Hle - Asn - Ser - Phe - Val - Gly - Leu-Met · NH2. This amino acid sequence is the same length as and shows structural similarity (57% homology) to the mammalian tachykinin, neuropeptide-γ, which is a product of the posttranslational processing of γ-preprotachykinin. The mammalian tachykinins, substance P and neurokinin B, were not detected in the extract by using specific antisera directed against the NH2-termini of the peptides, but an antiserum directed against the COOH-terminal region of substance P did detect a low concentration of immunoreactive material.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb11442.x
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  • 3
    Electronic Resource
    Electronic Resource
    Neuropeptide γ-(l-9)-Peptide: A Major Product of the Posttranslational Processing of γ-Preprotachykinin in Rat Tissues (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 61 (1993), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: γ-Preprotachykinin mRNA is the most abundant tachykinin mRNA in rat tissues, but the pathway of posttranslational processing of its translation product is unknown. An antiserum was raised against the synthetic peptide Asp-Ala-Gly-His-Gly-Gln-lle-Ser-His [neuropeptide γ-(1-9)-peptide, equivalent to γ-preprotachykinin-(72-80)-peptide], that showed 〈1% reactivity with intact neuropeptide γ and other tachykinins. Neuropeptide γ-(1-9)-peptide was detected by radioimmunoassay in relatively high concentrations in extracts of regions of rat brain and gastrointestinal tract. These concentrations correlated with (r = 0.99), but were significantly (p 〈 0.05) less than, the concentrations of neurokinin A-like immunoreactivity. The neuropeptide γ-(1-9)-like immunoreactivity in an extract of rat brain was eluted from a reverse-phase HPLC column in a single fraction with the same retention time as synthetic neuropeptide γ-(1 -9)-peptide. The synthetic peptide did not contract or relax isolated rat trachea, superior mesenteric artery, stomach fundus, or ileum, and the peptide did not affect the ability of neuropeptide 7 to contract the rat fundus. It is concluded that, in rat tissues, Lys70-Arg71 in 7-preprotachykinin is a major site of posttranslational processing, but the resulting product, neuropeptide γ-(1-9)-peptide, is neither an agonist nor an antagonist at the neurokinin-2 (NK-2) receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb13613.x
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  • 4
    Electronic Resource
    Electronic Resource
    Quantitation and Characterization of Peptides from the C-Terminal Flanking Region of Rat and Bovine Preprotachykinins (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 53 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Sequence analysis of cDNAs has shown that the biosynthetic precursors of substance P (α-,β-, and γ-prepro-tachykinins) contain a common amino acid sequence in the C-terminal flanking region that has not been conserved between species. Antisera have been raised against the synthetic peptide Tyr-Glu-Arg-Ser-Ala-Met-Gln-Asn-Tyr-Glu, which represents rat β-preprotachykinin-(117-126)-peptide, and used in radioimmunoassays. Antiserum R50 reacted strongly with C-flanking peptides in extracts of rat and bovine tissues whereas antiserum GP-4 reacted only with the rat peptides. The primary structure of the predominant molecular form of prepro tachykinin C-flanking peptide in an extract of bovine corpus striatum was established as: Ala-Leu-Asn-Ser-Val5-Ala-Tyr-Glu-Arg-Ser10-Val-Met-Gln-Asp-Tyr15-GIu. This sequence represents β-preprotachykinin-(111-126)-peptide which is equivalent to γ-preprotachykinin-(96-111)-peptide. A C-flanking peptide with similar chromatographic properties was identified in extracts of rat brain and gut together with a second immunoreactive component that may represent a fragment or a posttranslationally modified variant. A peptide corresponding to the 37-amino-acid residue C-flanking peptide derived from α-preprotachykinin was not detected in the extracts as expected from the known low abundance of SaL-preprotachykinin mRNA in rat brain and gut.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb09255.x
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of Peptides Related to α- and γ-Melanocyte-Stimulating Hormone from the Brain of the Frog Rana ridibunda (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 680 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb19758.x
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  • 6
    Electronic Resource
    Electronic Resource
    Presence of a Neuropeptide in a Model Cholinergic System (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 493 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb27190.x
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  • 7
    Electronic Resource
    Electronic Resource
    Neuroanatomical and Physiological Evidence for the Involvement of Pituitary Adenylate Cyclase-Activating Polypeptide in the Regulation of the Distal Lobe of the Frog Pituitary (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neuroendocrinology 5 (1993), S. 0 
    Details
    ISSN: 1365-2826
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38 amino-acid peptide which belongs to the glucagon/secretin/ vasoactive intestinal peptide superfamily. The sequence of PACAP is identical in all mammalian species studied so far but frog PACAP differs by one amino-acid from mammalian PACAP. The aim of the present study was to investigate the presence of PACAP in the hypothalamo-pituitary complex of the frog Rana ridibunda and to determine the biological activity of frog PACAP on homologous pituitary cells. The distribution of PACAP-containing neurons and fibers was examined by the indirect immunofluores-cence method using an antiserum raised against the N-terminal region of the peptide. In the hypothalamus, PACAP-immunoreactive perikarya were localized in the preoptic nucleus and the dorsal and ventral infundibular nuclei. Beaded nerve fibers were observed coursing from the ventral infundibular nucleus to the external vascular layer of the median eminence. A dense network of immunoreactive axons terminated in the vicinity of the capillaries of the hypophysial portal system. The neurointermediate lobe and the distal lobe of the pituitary were devoid of immunoreactive elements. The amount of PACAP-like immunoreactive material in hypothalamus extracts was measured by radioimmunoassay; the apparent concentration of PACAP was 4.5 ng/mg protein. Synthetic frog PACAP38 and PACAP27 induced a similar dose-dependent stimulation of cAMP production in isolated frog distal lobe pituitary fragments (ED50= 2 × 10−8 M). At the maximum dose tested (5 × 10−6 M), both frog PACAP38 and PACAP27 produced a 4-fold increase in cAMP production. In contrast, the truncated form [Des-His1frog PACAP38 did not affect adenylate cyclase activity demonstrating therefore that the N-terminal histidyl residue is essential for the biological activity of the peptide. [Des-His1]frog PACAP38 did not antagonize the stimulatory effect of frog PACAP38 or PACAP27 on cAMP production. Taken together, these data support the concept that, in amphibians as in mammals, PACAP may act as a hypophysiotropic neuropeptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2826.1993.tb00485.x
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  • 8
    Electronic Resource
    Electronic Resource
    ⃛and turn back again (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 389 (1997), S. 246-246 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The conventional view of evolutionary relationships within the living reptiles is that turtles are basal to the other groups. Their placement is based largely on the absence in turtles of temporal fenestrae, openings on either side of the skull involved in jaw muscle attachment, which all other ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/38425
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