I. Aplysia californica neurons R3-R14: Primary structure of the myoactive histidine-rich basic peptide and peptide I

Gregg T. Nagle, Susan L. Knock, Sherry D. Painter, James E. Blankenship, Richard R. Fritz, Alexander Kurosky

    Research output: Contribution to journalArticle

    16 Citations (Scopus)

    Abstract

    The R3-R14 neurons of the marine mollusc Aplysia are neuroendocrine cells that express a gene encoding peptides I, II and histidine-rich basic peptide (HRBP), a myoactive peptide that excites Aplysia heart and enhances gut motility in vitro. Peptide II has been chemically characterized (35), but the complete primary structures of peptide I and HRBP have not been established by amino acid sequence analysis. HRBP, peptide I, and the prohormone (proHRBP) were therefore purified from acid extracts of Aplysia californica neural tissue using sequential gel filtration and reversed-phase high-performance liquid chromatography and chemically characterized. Amino acid sequence analysis demonstrated that HRBP was a 43-residue peptide whose sequence was: <Glu-Val-Ala-Gln-Met-His-Val-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-Asn-His-Gly-Thr-Gly-Ser-Gly-Arg-His-Gly-Arg-Phe-Leu-Ile-Arg-Asn- Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. Compositional and sequence analyses of peptide I and proHRBP demonstrated that peptide I was a 26-residue peptide with the following sequence: NH2-Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp-Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Phe-Lys-Asp-COOH. These results demonstrated that the pro-HRBP sequence predicted by nucleotide sequence analysis of a cDNA clone (24) was in fact synthesized in R3-R14 neurons. Hydrophilicity and hydrophobicity profiles of preproHRBP, combined with charge distribution profiles and predictive secondary structural analysis, showed that cleavage at dibasic sequences was strongly associated with peaks of hydrophilicity in α-helical regions of the preprohormone.

    Original languageEnglish (US)
    Pages (from-to)849-857
    Number of pages9
    JournalPeptides
    Volume10
    Issue number4
    DOIs
    StatePublished - 1989

    Fingerprint

    Aplysia
    Histidine
    Neurons
    Peptides
    Hydrophobic and Hydrophilic Interactions
    Protein Sequence Analysis
    Hydrophilicity
    Sequence Analysis
    peptide I
    Molluscs
    Amino Acids
    Neuroendocrine Cells
    Gene encoding
    Mollusca
    Charge distribution
    High performance liquid chromatography
    Reverse-Phase Chromatography
    Hydrophobicity
    Structural analysis
    Gel Chromatography

    Keywords

    • Amino acid sequence
    • Aplysia californica
    • Histidine-rich basic peptide
    • Molluscan neuropeptide
    • Peptide I
    • R3-R14 neurons

    ASJC Scopus subject areas

    • Biochemistry
    • Endocrinology
    • Physiology
    • Cellular and Molecular Neuroscience

    Cite this

    Nagle, G. T., Knock, S. L., Painter, S. D., Blankenship, J. E., Fritz, R. R., & Kurosky, A. (1989). I. Aplysia californica neurons R3-R14: Primary structure of the myoactive histidine-rich basic peptide and peptide I. Peptides, 10(4), 849-857. https://doi.org/10.1016/0196-9781(89)90124-1

    I. Aplysia californica neurons R3-R14 : Primary structure of the myoactive histidine-rich basic peptide and peptide I. / Nagle, Gregg T.; Knock, Susan L.; Painter, Sherry D.; Blankenship, James E.; Fritz, Richard R.; Kurosky, Alexander.

    In: Peptides, Vol. 10, No. 4, 1989, p. 849-857.

    Research output: Contribution to journalArticle

    Nagle, GT, Knock, SL, Painter, SD, Blankenship, JE, Fritz, RR & Kurosky, A 1989, 'I. Aplysia californica neurons R3-R14: Primary structure of the myoactive histidine-rich basic peptide and peptide I', Peptides, vol. 10, no. 4, pp. 849-857. https://doi.org/10.1016/0196-9781(89)90124-1
    Nagle, Gregg T. ; Knock, Susan L. ; Painter, Sherry D. ; Blankenship, James E. ; Fritz, Richard R. ; Kurosky, Alexander. / I. Aplysia californica neurons R3-R14 : Primary structure of the myoactive histidine-rich basic peptide and peptide I. In: Peptides. 1989 ; Vol. 10, No. 4. pp. 849-857.
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    AU - Fritz, Richard R.

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    AB - The R3-R14 neurons of the marine mollusc Aplysia are neuroendocrine cells that express a gene encoding peptides I, II and histidine-rich basic peptide (HRBP), a myoactive peptide that excites Aplysia heart and enhances gut motility in vitro. Peptide II has been chemically characterized (35), but the complete primary structures of peptide I and HRBP have not been established by amino acid sequence analysis. HRBP, peptide I, and the prohormone (proHRBP) were therefore purified from acid extracts of Aplysia californica neural tissue using sequential gel filtration and reversed-phase high-performance liquid chromatography and chemically characterized. Amino acid sequence analysis demonstrated that HRBP was a 43-residue peptide whose sequence was: <Glu-Val-Ala-Gln-Met-His-Val-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-Asn-His-Gly-Thr-Gly-Ser-Gly-Arg-His-Gly-Arg-Phe-Leu-Ile-Arg-Asn- Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. Compositional and sequence analyses of peptide I and proHRBP demonstrated that peptide I was a 26-residue peptide with the following sequence: NH2-Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp-Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Phe-Lys-Asp-COOH. These results demonstrated that the pro-HRBP sequence predicted by nucleotide sequence analysis of a cDNA clone (24) was in fact synthesized in R3-R14 neurons. Hydrophilicity and hydrophobicity profiles of preproHRBP, combined with charge distribution profiles and predictive secondary structural analysis, showed that cleavage at dibasic sequences was strongly associated with peaks of hydrophilicity in α-helical regions of the preprohormone.

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